Les viandes

**Exemples d’allergies aux viandes**
Nb de patients	bœuf / veau	mouton / agneau	porc	lapin	cheval
6	3		6	1
2	2	1	1	1
1	0			0	1
1	1	1	0
2	0		0	2
2	2	2	2
1	0	1
1	1	1		1
1	1	1	1	1

[1] - Lemerdy P, Moneret-Vautrin DA, Rancé F, Kanny G, Parisot L. Prévalence des allergies alimentaires chez l'enfant et l'adulte. Alim'Inter 2003;8:5-8

[3] - Rancé F, Kanny G, Dutau G, Moneret-Vautrin DA. Food hypersensitivity in children: clinical aspects and distribution of allergens. Pediatr Allergy Immunol 1999;10:33-38

The aims of this work were to investigate, in children and adolescents, the clinical aspects of food hypersensitivity and the distribution of allergens, in a prospective and descriptive study. Five hundred and forty-four pediatric cases from a series of 703 patients with food allergies, confirmed by food challenge, were studied. Their clinical characteristics and the distribution according to allergen were investigated. There was a family history of atopic disease in 70.5% of patients. Atopic dermatitis was the main symptom (275/544; 50.5% of patients), followed by urticaria and angio-edema (165/544; 30%). There was asthma in 8.6% of patients (47 children) and anaphylaxis in 4.5% (27 patients). The rarest signs were rhinitis (n=2; 0.3%), oral allergy syndrome (n=8; 1.4%), and gastrointestinal signs (n=11; 2%). Five allergens accounted for 78% of food hypersensitivity. These allergens were: eggs (36%), peanuts (24%), cow's milk (8%), mustard (6%), and cod (4%). Peanut was the most common allergen for children over the age of 3 yr. In this selected population, sensitivity of individuals to more than three foods was unusual (5%). Atopic dermatitis was the main symptom of food allergy in children. The symptoms changed over time, with respiratory disorders, oral allergy syndrome and ocular problems occuring later. Anaphylaxis also occured mostly in older children. Five allergens were responsible for more than three-quarters of food allergies in children. However, the number of allergens implicated was higher for the group of children over the age of 6 yr than for younger children.

↩

[4] - Moneret-Vautrin M. Allergies aux viandes de mammifères. Alim'Inter 2009;14:12-14

↩

[5] - Restani P, Ballabio C, Tripodi S, Fiocchi A. Meat allergy. Curr Opin Allergy Clin Immunol 2009;9:265-269

PURPOSE OF REVIEW: This review summarizes the scientific evidence on meat allergy, an unusual disorder, whose prevalence in some European countries (such as Italy) may be increasing. RECENT FINDINGS: Data reported in this review underline some interesting points: in meats rarely consumed, such as kangaroo, whale and seal, the main allergens are only partially correlated to those detected in beef or other usually consumed meats; cross-reactivity and cross-contamination are critical aspects, which should be seriously considered by allergologists. SUMMARY: Meat allergy is normally outgrown during the first years of life, so that it is rare in adults. Beef among mammals and chicken among birds are most frequently involved. The major allergens are serum albumins and immunoglobulins, but there are a few reports of allergies to muscle proteins (actin, myosin and tropomyosin). As meat allergenicity can be reduced by various treatments (heat, homogenization and freeze-drying), the consumption of meat derivatives by children allergic to meat proteins is often permitted. Cross-reactivity has been described between different meats, between meat and milk or eggs and between meat and animal dander. There are some reports of cross-contamination associated with the inadequate cleaning of industrial or butchers' equipment. All these aspects may have serious implications for clinical practice.

↩

[6] - Drouet M. Allergènes des viandes. Rev Fr Allergol 2009;49:160-165

L‚allergie aux viandes de vertébrés est passée en revue à partir des divers rapports et travaux de la littérature. Nous présentons les diverses allergies aux viandes et leurs particularités. Nous évoquons les allergies croisées démontrées ou simplement suspectées pour chacune d‚entre elles.

↩

[7] - Walker A, Przybilla B, Ruëff F. Exercise-induced anaphylaxis in a patient with ‘‘porc-chat’’- syndrome. Allergy 2008;63(suppl. 88):290-291

Background: Allergy to meat is very uncommon. Furthermore, the identification of the elicitor may be very difficult in those cases where the elicitor transiently does not induce allergic reactions. Case report: A 59-year-old businessman man was referred to our hospital with a history of recurrent Quincke edema and generalised urticaria. The first episode of urticaria had occurred 40 years ago. After having been free of symptoms for decades the patient suddenly experienced similar complaints 2 1/2 years before the admission, one-time with unconsciousness. The patient was an enthusiastic hunter regularly consuming huge amounts of meat from different mammals and had not noticed an incompatibility to any meat in the past. There was no history of allergic rhinoconjunctivitis upon exposure to cats, or of contact urticaria due to skin exposure to bags. Skin prick tests with common inhalant allergens and with various food allergens were negative. In contrast, intradermal tests showed several immediate type reactions, in particular towards pork, beef, and cat epithelia. Specific IgE serum levels were clearly elevated with respect to pork (10.7 kU/L), beef (23.3 kU/L), cat epithelia (25.7 kU/L), and some other animal allergens. Oral provocation tests with pork (750 g), beef (420 g), and 1800 mg acetylsalicylic acid (ASS) were initially well tolerated. However, in a subsequent test the patient had to consume again equal doses of pork and beef in combination with 500 mg ASS and pale beer (0.5L Augustiner Edelstoff). Then, the patient underwent a bout of ergometric exercise (for half an hour) at which he developed a generalised urticaria. In contrast, oral provocation with milk (1600 mL) in combination with the same cofactors (ASS, exercise and alcohol) did not reveal a hypersensitivity reaction. Challenge tests with cat epithelia at the conjunctiva were positive. Conclusion: If skin prick tests are negative in a patient with a history of an anaphylactic reaction, one should perform intradermal tests. Our patient denied prior intake of ASS or exceptional physical exercise when he had experienced anaphylactic reactions after meat ingestion. According to our experience the combined exposure to the suspicious food allergen and to ASS, exercise and alcohol is very effective to provoke objective anaphylactic reactions in those patients who transiently tolerate the responsible elicitor.

↩

[8] - Biedermann T, Schopf P, Rueff F, Przybilla B. [Exertion-induced anaphylaxis after eating pork and beef]. Dtsch Med Wochenschr 1999;124:456-458

HISTORY AND CLINICAL FINDINGS: A 72-year-old woman developed generalized urticaria. Quincke oedema, shortness of breath and hypotension two hours after eating a meal containing pork and after mild physical activity (ironing) in-between. She was treated by an emergency physician and then admitted to hospital for one day of monitoring her condition. During the past several years such episodes of generalized urticaria had recurred twice to four times a year. INVESTIGATIONS: Pin-prick tests gave an immediate-type reaction to beef but not to pork. Specific serum IgE antibodies were demonstrated to pork and beef, cat's epithelia, milk albumin and casein. Oral provocation tests were negative for pork and beef. But when pork and beef were eaten mild physical activity (bicycle ergometry at 20 W), generalized urticaria occurred after eating pork and beef, but not after drinking milk. TREATMENT AND COURSE: Exercise-induced anaphylaxis to pork and beef was diagnosed. No allergic reaction has occurred in more than 12 months of avoiding eating these meats. CONCLUSION: The picture of exercise-induced anaphylaxis caused by food allergy can be precipitated by even mild activity. This must be taken into account in the diagnosis of systemic rapid-reaction response and in the performance of provocation tests.

↩

[9] - Ayuso R, Lehrer SB, Lopez M, Reese G, Ibanez RM, Martin-Esteban M, et al. Identification of bovine IgG as a major cross-reactive vertebrate meat allergen. Allergy 2000;55:348-354

Although beef is a main source of protein in Western diets, very little has been published on allergic reactions to beef or the main allergens implicated in these reactions. The aim was to evaluate the IgE antibody response to beef in suspected meat-allergic subjects and assess cross-reactivity of beef with other vertebrate meats. METHODS: Fifty-seven sera from suspected meat-allergic subjects were tested by grid blot for specific IgE antibodies to vertebrate meats (beef, lamb, pork, venison, and chicken), and the patterns of recognition of meat proteins were assessed by immunoblot studies. RESULTS: A 160-kDa band, identified as bovine IgG, was detected in raw beef in 83% (10/12) of beef-allergic subjects but in only 24% of the beef-tolerant subjects. IgE reactivity to a band of similar mol. mass was detected also in lamb and venison, but rarely in pork or chicken. Complete inhibition of the IgE reactivity to the bovine IgG was obtained with lamb, venison, and milk. IgE reactivity to this band also completely disappeared when beef or lamb extracts were separated under reducing conditions, indicating conformational epitopes. CONCLUSIONS: Bovine IgG appears to be a major cross-reacting meat allergen that could predict beef allergy. Further studies with oral IgG challenges should be performed to document the conclusion that in vitro reactivity correlates with clinical hypersensitivity. The role of bovine IgG in other bovine products such as milk, dander, or hair must also be studied, and the hypothesis that it is a cross-reacting allergen with other mammalian products validated.

↩

[10] - Chiciudean M. Food-dependent exercise-induced anaphylaxis to pork meat and its crossreactivities. Allergy 2008;63(suppl. 88):290

Background: Pork IgE-mediated allergy is a rare cause of food-dependent exercise-induced anaphylaxis (FDEIA) and its clinical features and cross-reactivities have not been fully elucidated. Methods and results: We report the case of a 16 year-old girl who presented two episodes of FDEIA to pork meat. The patient was known for 5 years for mild persistent asthma, sensitised to cat dander and mites and well controled on low-dose inhaled corticosteroids. No other medication taken. No food allergy known. The first episode consisted in a reaction with flush, wheezing and loss of conscience after eating cooked pork meat, during jogging. The second episode occured in a medical setting, during a stress ECG in searching of congenital dysrhythmias after eating sausages of mixed meat. This time it consisted in urticaria, wheezing and hypotension. The serum tryptase and histamine were elevated. Skin prick tests revealed a sensitisation to cat dander (10/20 mm), to mites (7/12mm) and to pork (7/15 mm). Prick-to-prick to raw and cooked pork meat were also positives. No positivity was found for other respiratory or food allergens. Total IgE was 527 IU/L. CAP/RAST showed a value of 7 kU/L for pork meat, of 55 kU/L for cat dander and of 32 kU/L for cat serum albumine. RAST inhibition confirmed the significant cross-reactivity between the two allergen sources. A challange test with pork meat in training conditions was not performed, due to severity of previous reactions. The elimination of pork meat from the diet was followed by safe reintroduction of exercise (patient follow-up for 1 year). Conclusion: To the best of our knowledge, this is the first case of specific FDEIA to pork meat. Positive allergologic tests to pork meat and important sensitisation to cat, included in the pork-cat syndrome, suggest that the same allergens may be implicated in the two syndromes. We suggest that the allergens responsable for the pork-cat syndrome (serum albumine), may be at the same time implicated in cases of FDEIA to pork meat.

↩

[11] - Cahen YD, Fritsch R, Wüthrich B. Food allergy with monovalent sensitivity to poultry meat. Clin Exp Allergy 1998;28:1026-1030

BACKGROUND: Allergy to poultry meat is only rarely covered in science. The few reports are usually related to patients allergic to eggs or bird feathers. OBJECTIVE: Two patients with a clear history of monovalent, ingestive allergy to chicken and turkey meat, without other food allergies, were analysed. The relevant allergens were to be identified by immunoblotting. METHODS: Both patients were evaluated with skin tests and specific IgE determination (CAP). Allergens were identified by SDS-PAGE and immunoblotting. Cross-reactivity of chicken and turkey meat was examined by IgE inhibition experiments. RESULTS: Skin tests and specific IgE were positive for chicken and turkey in both patients. Cross-reactivities to other poultry meats were documented for duck and goose meat. No sensitization to egg components or poultry feathers could be found. Allergenic proteins of poultry meat were detected at molecular weights of 21, 23 and 50 kDa (distinct bands) and 13, 27 and 33kDa (faint bands). An additional band at 91 kDa for turkey, can probably not be considered a distinct allergenic epitope. Immunoblot inhibition confirmed cross-reactivity of chicken and turkey meat allergens. CONCLUSION: Food allergy to poultry meat is a distinct disorder with crossreactivity among chicken, turkey and other poultries. The relevant allergens were identified by immunoblotting. Associated food allergy to egg-components is unlikely as the patients were able to tolerate egg and eggs products.

↩

[12] - Fiocchi A, Restani P, Bouygue GR, Martelli A. Beef allergy in adults and children. Allergy 2005;60:126

↩

[13] - Drouet M, Sabbah A. The pork/cat syndrome or crossed reactivity between cat epithelia and pork meat. Monogr Allergy 1996;32:164-173

↩

[14] - Allergie à la viande de porc. Alim'Inter 2000;5(23):3-4

↩

[15] - Palacios Benito R, Alvarez-Lovel MC, Martinez-Cocera C, Del Castillo Paya MM, Romanillos RA. Allergy to meat. Allergy 2002;57:858-859

↩

[16] - Cisteró-Bahíma A, Enrique E, San Miguel-Moncin MM, Alonso R, Bartra J, Fernandez-Parra B, et al. Meat allergy and cross-reactivity with hamster epithelium. Allergy 2003;58:161-162

↩

[17] - Fuentes MM, Palacios R, Garcés MM, Caballero ML, Moneo I. Isolation and characterization of a heat-resistant beef allergen: myoglobin. Allergy 2004;59:327-331

BACKGROUND: Meat allergy is rarely reported. Most of the described cases are sensitizations to bovine serum albumin . OBJECTIVE: The aim of the study was to describe a case of allergy to a new meat allergen and, after its characterization . METHODS: A 35-year-old nonatopic female with allergic episodes after ingestion of several types of meat was studied. Skin tests (prick and prick-to-prick); total and specific immunoglobulin E (IgE) determination; sodium dodecyl sulphate-polyacrylamide gel electrophoresis and specific IgE determination by immunoblotting under different conditions were performed. A 17-kDa allergen was semipurified by ethanol fractionation and its amino-terminal sequence was determined. The existence of specific IgE directed to this protein was studied by immunoblot in 80 atopic patients . RESULTS: The patient showed specific IgE antibodies to a 17-kDa protein. During the isolation of this allergen it was found that a 70-90% (vol/vol) ethanol concentration was able to purify the protein. The characterization revealed that it was a heat-resistant protein without disulfide bonds. N-terminal amino acid sequence (16 residues) showed identity with myoglobin. The study of specific IgE to this allergen among atopic patients showed that it was recognized by about 1% of the subjects . CONCLUSIONS: We describe a case of meat allergy caused by myoglobin. This is the first described case of monosensitization to this protein.

↩

[18] - Benito C, Fernandez-Rivas M. Combined respiratory and food allergies to rabbit. Allergy Clin Immunol Int 2005;17(Suppl. 1):361

Background. Exposure to rabbits as domestic pets or laboratory animals can induce respiratory allergy. Allergic reactions to the ingestion of rabbit meat in patients with respiratory allergy to rabbit has not been reported. Patients. Case 1. A 22 years-old woman reported since childhood rhinoconjunctivitis (RC) and asthma while playing with rabbits, and oropharyngeal itching (OAS) after eating rabbit meat. At 14 years of age she presented an anaphylaxis while playing volleyball one hour after having eaten rabbit. Case 2. A 10 years-old boy reported since the age of 6, several episodes of RC and asthma after exposure to rabbits. At the age of 7 he presented OAS while eating rabbit, immediately followed by RC and asthma, that required emergency room treatment. Both patients tolerated all foods of animal origin, including meats of other species. Patient 1 presented RC due to cat allergy. No other inhalant allergies where present in these 2 patients. Methods. Different rabbit extracts were prepared from epithelium, meat, serum, urine, and albumin, and used in skin prick tests (SPTs), ELISA-IgE, ELISAinhibition assays, and immunoblots. Results. Case 1: SPTs (wheal mm) epithelium 10, meat 5; ELISA (aKU/L) epithelium 56.73, meat 0.93, serum 0.56, urine 4.30, albumin 1.79. Case 2: SPTs epithelium 11, meat 4; ELISA epithelium 110.16, meat 1.11, serum 0.74, urine 5.81, albumin 1.34. The ELISA to rabbit meat was completely inhibited by rabbit epithelium, urine and albumin. The maximum inhibitions of the ELISA to rabbit epithelium by rabbit meat were below 44%, whereas the figures for rabbit urine were over 90%, and for rabbit albumin over 73%. Several allergens were identified in the immunoblots, but the most prominent ones were a band 60kDa (albumin) in epithelium, meat, serum and urine (cases 1,2), a band 42 kDa (probably actin) only observed in the meat (cases 1,2), a band 150 kDa (probably IgG) in epithelium, serum and urine (case 2), a band 17 kDa in epithelium (probably Ory c 1) (case 2). Conclusion. We present 2 cases of RC and asthma induced by inhaled exposure to rabbit who have subsequently developed severe reactions after the intake of rabbit meat. The reactivity to rabbit meat might result from sensitisation to rabbit allergens present in epitelium and urine by the inhalant route, together with a primary sensitisation to meat allergens (such as actin) through the oral route.

↩

[19] - Gex-Collet CM, Huber C, Reimers A, Helbling A. Does the Pork-Cat Syndrome exist? EAACI 23th Congress, Amsterdam, 12-16 June, 2004, Poster n°1037

Background: The pork-cat syndrome has been described for the first time by a French group in 1994 postulating a cross-reactivity based on serum-albumin between cat and pork meat allergens. In the literature only few case-reports can be found. In the last 4 years 3 cat allergic subjects with immediate-type adverse reactions following ingestion of pork and cow meat referred for allergological evaluation have been recognized and assigned to this entity. Methods: History and allergological findings of the 3 identified cases will be presented. Results: In 2 out of 3 patients a positive skin prick test to pork meat, specific serum IgE to cat dander, pork and cat serum albumin have been demonstrated. In the third subject a positive skin prick test as well a serum specific IgE to cow meat have been found, but not to pork. Conclusion: So far the pork-cat syndrome rarely has been described, but it does exist. Since mammalian albumins are quite similar in composition, it is likely that the reactivity to the pork-albumin is due to a cross-reactive mechanism between the albumins. However, sensitization may have occurred by the inhalative way as it is suggested by the pre-existent respiratory allergy to cat.

↩

[20] - Welt K, Hinrichs R, Ott S, Thalmann M, Dieckmännken J, Schneider LA, et al. Anaphylaxis after the ingestion of lamb meat. Allergy 2005;60:545

↩

[21] - Bourne HC, Restani P, Moutzouris M, Katelaris CH. An unusual pattern of meat allergy. Allergy 2005;60:706-707

↩

[22] - Fuentes Aparicio V, Sanchez Marcen I, Perez Montero A, Baeza ML, de Barrio Fernandez M. Allergy to mammal's meat in adult life: immunologic and follow-up study. J Investig Allergol Clin Immunol 2005;15:228-231

Allergy to bovine meat and Bovine serum albumin (BSA) is exceptional, especially in the adult life. BSA is considered a minor allergen in cow's milk allergy, but there is little information about this antigen in reactions produced by other beef products as meat. To our knowledge, evolutive studies of beef's allergic patients have not been reported. OBJECTIVE: To present one patient with several allergic reactions (urticaria-angioedema) after eating different mammals' meat. METHODS: The patient underwent allergy testing through skin prick test (SPT), specific IgE detection and SDS-PAGE Immunoblotting and Immunodot inhibition studies. Periodic determinations of specific IgE to meats and epithelia were performed. RESULTS: Routine studies for chronic urticaria were normal or negative. SPT showed positive responses to pork, cow, rabbit and lamb meat, and dog, pork, sheep and cow epithelia. It was negative to cat, horse, guinea pig, rabbit, lamb, mouse epithelia, mixture of feathers, cow milk, soybean, mustard, mites and chicken meat and Anisakis simplex. Intradermal testing to BSA was positive. Determinations of specific IgE were positive to beef meat, lamb meat, pork meat and rabbit meat, dog, cat, cow, sheep and pork dander, cow's milk, and negative to chicken meat. Immunoblot and immunodot studies showed IgE recognition bands to bovine and lamb meat which were totally inhibited by BSA. A progressive reduction of the total and specific IgE, the latter until its total negativization, has been observed in the following three-year period. CONCLUSION: We report a case of IgE-mediated urticaria-angioedema due to BSA hypersensitivity, possibly induced by a subclinical sensitivity to dog and cat epithelium. The exclusion diet in patients allergic to these foods may be a progressive loss of clinical allergy.

↩

[23] - Ayuso R, Lehrer SB, Lopez M, Reese G, Ibanez RM, Martin-Esteban M, et al. Identification of bovine IgG as a major cross-reactive vertebrate meat allergen. Allergy 2000;55:348-354

Although beef is a main source of protein in Western diets, very little has been published on allergic reactions to beef or the main allergens implicated in these reactions. The aim was to evaluate the IgE antibody response to beef in suspected meat-allergic subjects and assess cross-reactivity of beef with other vertebrate meats. METHODS: Fifty-seven sera from suspected meat-allergic subjects were tested by grid blot for specific IgE antibodies to vertebrate meats (beef, lamb, pork, venison, and chicken), and the patterns of recognition of meat proteins were assessed by immunoblot studies. RESULTS: A 160-kDa band, identified as bovine IgG, was detected in raw beef in 83% (10/12) of beef-allergic subjects but in only 24% of the beef-tolerant subjects. IgE reactivity to a band of similar mol. mass was detected also in lamb and venison, but rarely in pork or chicken. Complete inhibition of the IgE reactivity to the bovine IgG was obtained with lamb, venison, and milk. IgE reactivity to this band also completely disappeared when beef or lamb extracts were separated under reducing conditions, indicating conformational epitopes. CONCLUSIONS: Bovine IgG appears to be a major cross-reacting meat allergen that could predict beef allergy. Further studies with oral IgG challenges should be performed to document the conclusion that in vitro reactivity correlates with clinical hypersensitivity. The role of bovine IgG in other bovine products such as milk, dander, or hair must also be studied, and the hypothesis that it is a cross-reacting allergen with other mammalian products validated.

↩

[24] - Vereda A, Cuesta J, Barderas M, de la Cuesta F, Pastor C, Vivanco F, et al. Beef allergy. EAACI 25th Congress, Vienna, 10-14 June, 2006, Poster n°1529

Background: Although beef meat is widely consumed in Western diets, beef allergy is rarely reported. The aim of the study was to describe a case of beef allergy and to identify the allergens. Method:A 16-month-old male, with atopic dermatitis and several food allergies (egg, fish and legumes), was studied. At the age of 7 months, he suffered labial angioedema and perioral erythema after the ingestion of scarcely cooked beef. He tolerated well done beef, as well as other meats and cow's milk. Skin tests, oral challenge and specific IgE determination were performed. Meat allergens were studied by SDS-PAGE, IgE-immunoblotting, inhibition assays and mass spectrometry. Results: Prick tests were positive to egg, fish, legumes, bovine serum albumin (BSA),bovine gamma globulin (BGG) and cow epithelium, and negative to the remaining milk proteins. Prick-prick tests were positive to raw and cooked beef, pork and lamb, and negative to chicken meat. Oral challenge test with raw beef meat elicited a positive response, with perioral wheals and erithema, and labial angioedema. However, the oral challenge was negative with cooked beef. Specific IgE was positive to BSA, cow's epithelium and milk, beef, pork and lamb meat. SDS-PAGE and immunoblotting with the beef extract revealed some prominent IgE-binding protein bands at >130, 67, 60 and 25 kDa, which were common to other meats (pork, rabbit, lamb), as well as to cow's epithelium and milk. IgE binding was decreased by heating the beef meat extract. Inhibition assays demonstrated cross-reactivity among the different meats, mainly between beef and lamb. BSA, b-enolase and creatin kinase were identified by mass spectrometry as allergens in the beef meat extract. Conclusions: We present a child with beef allergy, also sensitized to cow‚s milk and other meats. The responsible allergens are heat-labile, and could correspond to BSA and IGG. We also identified two proteins (b-enolase and creatin kinase), which have not been previously described as allergens.

↩

[25] - Fuentes Aparicio V, Sanchez Marcen I, Perez Montero A, Baeza ML, de Barrio Fernandez M. Allergy to mammal's meat in adult life: immunologic and follow-up study. J Investig Allergol Clin Immunol 2005;15:228-231

Allergy to bovine meat and Bovine serum albumin (BSA) is exceptional, especially in the adult life. BSA is considered a minor allergen in cow's milk allergy, but there is little information about this antigen in reactions produced by other beef products as meat. To our knowledge, evolutive studies of beef's allergic patients have not been reported. OBJECTIVE: To present one patient with several allergic reactions (urticaria-angioedema) after eating different mammals' meat. METHODS: The patient underwent allergy testing through skin prick test (SPT), specific IgE detection and SDS-PAGE Immunoblotting and Immunodot inhibition studies. Periodic determinations of specific IgE to meats and epithelia were performed. RESULTS: Routine studies for chronic urticaria were normal or negative. SPT showed positive responses to pork, cow, rabbit and lamb meat, and dog, pork, sheep and cow epithelia. It was negative to cat, horse, guinea pig, rabbit, lamb, mouse epithelia, mixture of feathers, cow milk, soybean, mustard, mites and chicken meat and Anisakis simplex. Intradermal testing to BSA was positive. Determinations of specific IgE were positive to beef meat, lamb meat, pork meat and rabbit meat, dog, cat, cow, sheep and pork dander, cow's milk, and negative to chicken meat. Immunoblot and immunodot studies showed IgE recognition bands to bovine and lamb meat which were totally inhibited by BSA. A progressive reduction of the total and specific IgE, the latter until its total negativization, has been observed in the following three-year period. CONCLUSION: We report a case of IgE-mediated urticaria-angioedema due to BSA hypersensitivity, possibly induced by a subclinical sensitivity to dog and cat epithelium. The exclusion diet in patients allergic to these foods may be a progressive loss of clinical allergy.

↩

[26] - Moore LM, Rathkopf MM, Sanner CJ, Whisman BA, Demain JG. Seal and whale meat: two newly recognized food allergies. Ann Allergy Asthma Immunol 2007;98:92-96

BACKGROUND: Alaska's marine mammals compose a large portion of the diet of indigenous coastal Alaskan people. Bowhead whales (Balaena mysticetus) and bearded seals (Erignathus barbatus), inhabitants of the Bering and Beaufort seas along Alaska's western and northern coasts, are 2 of the most important subsistence species, serving as major food sources to the native population. OBJECTIVE: To describe an Inupiaq boy with symptoms consistent with an IgE-mediated food allergy after ingestion of bowhead whale and bearded seal meat. METHODS: Extracts of cooked bowhead whale and bearded seal were prepared, lyophilized, and evaluated for protein content. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis was performed for each extract, followed by transfer to nitrocellulose and IgE immunoblots. Skin prick testing was conducted using reconstituted extracts of 1:10 wt/vol dilution. RESULTS: Immunoblots revealed serum specific IgE binding with the extracts of bowhead whale and bearded seal meat. Protein bands of approximately 25, 40, 50, and 90 kDa were found in the seal meat. Protein bands of 55 and 90 kDa were found in the whale meat. Skin prick test results were positive to whale and seal extracts with appropriate positive and negative controls. Ten control subjects had negative reactions to both extracts. CONCLUSION: A patient with moderate anaphylaxis to bowhead whale and bearded seal meat demonstrated serum specific IgE by means of immunoblot and positive skin prick test results. This is the first known reported case of specific IgE to these species.

↩

[27] - Codreanu F. L'activité du réseau Allergo-Vigilance: allergies alimentaires. Alim'Inter 2007;12:239-242

↩

[28] - Moneret-Vautrin DA, Lemerdy P. Allergie à la viande de canard. Alim'Inter 2007;12:67-68

↩

[29] - Besler M, Fiocchi A, Restani P. Allergen Data Collection: Chicken Meat (Gallus domesticus). Internet Symp Food Allergens 2001;3(4):193-201

↩

[30] - Escudero C, Cuesta J, Bartolomé B, de Miguel J, Compés E, de las Heras M, et al. Avian meat as a hidden allergen: double blind, placebo controlled, oral challenge study. EAACI 22th Congress, Paris, 7-11 June, 2003, Poster n°139

Chicken meat is a fundamental food in our diets. However, the food allergy to this food has been scantly documented and generally, into the context of the „bird-egg syndrome‰. Case report: 22-year-old man without personal history of atopy and family history of hay fever. He was refereed oral syndrome after the ingestion of frankfurter and foie gras that contains small amounts of avian meats. Moreover, he experienced oral syndrome, nausea, vomits and abdominal pain immediately after the ingestion of cooked chicken meat. He developed similar symptoms after the ingestion of turkey, duck, quail, partridge and pheasant meats. He could eat egg and mammalian meats, and he hadn‚t exposed to birds. He experiences oral itching after the ingestion of chickpea, kidney bean and lentil. The causative role of avian meats in the anaphylactic response of the patient was investigated by immunologic and double blind, placebo controlled, oral challenge tests (DBPCOC). Skin prick tests (SPT) were performed with a panel of foods. We obtained positive responses with chicken meat. SPT with raw chicken and turkey meats, performed by the prick-prick method, were positive. SPT with egg (egg white, egg yolk, ovalbumin, ovomucoid, conalbumin, and lysozyme), chicken albumin and feathers mixture were negative. Specific IgE were determined by CAP System (Pharmacia, Sweden). Specific IgE determinations to avian meats were positive (chicken 2.95; turkey 0.96 kU/L). Oral challenge with frankfurter that contains chicken meat was positive. DBPCOC with an accumulative dose of 3 gr. of chicken meat reproduced the symptoms. Placebo was prepared with green vegetable puree and cooked cow meat. Conclusion: Small amounts of poultry meat may be present in frankfurters and other foodstuffs and cause anaphylactic reactions in sensitised patients. We could demonstrate by means of skin tests, IgE determinations and DBPCOC that chicken meat caused anaphylaxis in the patient through an IgE-dependent mechanism. Crossreactive among various avian meats is clinically suggestive.

↩

[31] - Leynadier F. Tests cutanés et allergie croisée aux myorelaxants. Rev Fr Allergol Immunol Clin 1995;35:305-306

↩

[32] - Escudero C, Cuesta J, Bartolomé B, de Miguel J, Compés E, de las Heras M, et al. Avian meat as a hidden allergen: double blind, placebo controlled, oral challenge study. EAACI 22th Congress, Paris, 7-11 June, 2003, Poster n°139

Chicken meat is a fundamental food in our diets. However, the food allergy to this food has been scantly documented and generally, into the context of the „bird-egg syndrome‰. Case report: 22-year-old man without personal history of atopy and family history of hay fever. He was refereed oral syndrome after the ingestion of frankfurter and foie gras that contains small amounts of avian meats. Moreover, he experienced oral syndrome, nausea, vomits and abdominal pain immediately after the ingestion of cooked chicken meat. He developed similar symptoms after the ingestion of turkey, duck, quail, partridge and pheasant meats. He could eat egg and mammalian meats, and he hadn‚t exposed to birds. He experiences oral itching after the ingestion of chickpea, kidney bean and lentil. The causative role of avian meats in the anaphylactic response of the patient was investigated by immunologic and double blind, placebo controlled, oral challenge tests (DBPCOC). Skin prick tests (SPT) were performed with a panel of foods. We obtained positive responses with chicken meat. SPT with raw chicken and turkey meats, performed by the prick-prick method, were positive. SPT with egg (egg white, egg yolk, ovalbumin, ovomucoid, conalbumin, and lysozyme), chicken albumin and feathers mixture were negative. Specific IgE were determined by CAP System (Pharmacia, Sweden). Specific IgE determinations to avian meats were positive (chicken 2.95; turkey 0.96 kU/L). Oral challenge with frankfurter that contains chicken meat was positive. DBPCOC with an accumulative dose of 3 gr. of chicken meat reproduced the symptoms. Placebo was prepared with green vegetable puree and cooked cow meat. Conclusion: Small amounts of poultry meat may be present in frankfurters and other foodstuffs and cause anaphylactic reactions in sensitised patients. We could demonstrate by means of skin tests, IgE determinations and DBPCOC that chicken meat caused anaphylaxis in the patient through an IgE-dependent mechanism. Crossreactive among various avian meats is clinically suggestive.

↩

[33] - Halloy JL. Allergie aux viandes d'oiseaux. Alim'Inter 2005;10:289-291

↩

[34] - Cahen YD, Fritsch R, Wüthrich B. Food allergy with monovalent sensitivity to poultry meat. Clin Exp Allergy 1998;28:1026-1030

BACKGROUND: Allergy to poultry meat is only rarely covered in science. The few reports are usually related to patients allergic to eggs or bird feathers. OBJECTIVE: Two patients with a clear history of monovalent, ingestive allergy to chicken and turkey meat, without other food allergies, were analysed. The relevant allergens were to be identified by immunoblotting. METHODS: Both patients were evaluated with skin tests and specific IgE determination (CAP). Allergens were identified by SDS-PAGE and immunoblotting. Cross-reactivity of chicken and turkey meat was examined by IgE inhibition experiments. RESULTS: Skin tests and specific IgE were positive for chicken and turkey in both patients. Cross-reactivities to other poultry meats were documented for duck and goose meat. No sensitization to egg components or poultry feathers could be found. Allergenic proteins of poultry meat were detected at molecular weights of 21, 23 and 50 kDa (distinct bands) and 13, 27 and 33kDa (faint bands). An additional band at 91 kDa for turkey, can probably not be considered a distinct allergenic epitope. Immunoblot inhibition confirmed cross-reactivity of chicken and turkey meat allergens. CONCLUSION: Food allergy to poultry meat is a distinct disorder with crossreactivity among chicken, turkey and other poultries. The relevant allergens were identified by immunoblotting. Associated food allergy to egg-components is unlikely as the patients were able to tolerate egg and eggs products.

↩

[35] - Liccardi G, Szepfalusi Z, Noschese P, D'Amato M. The significance of chicken meat allergy without sensitization to egg proteins. Ann Allergy Asthma Immunol 2000;85:84

↩

[36] - Sokolova A, Costa AC, Santos MC, Bartolomé B, Pereira Barbosa M. Severe allergy to poultry meat without sensitisation to egg proteins with concomitant Leguminosae allergy. Case report. Allergol Immunopathol (Madr) 2009;37:168-171

↩

[37] - Zacharisen MC. Severe allergy to chicken meat. WMJ 2006;105:50-52

INTRODUCTION: While allergic reactions to poultry products in the form of feathers and eggs are common, allergic reactions to chicken meat are rare. Despite the popularity of chicken in today's healthy diet, severe reactions after ingesting chicken meat are rarely described. This report describes a patient who developed chicken meat anaphylaxis without experiencing allergy to eggs or feathers. METHODS: A carefully obtained history from a 41-year-old male suggested chicken meat as the cause of his symptoms. He developed abdominal cramping, generalized urticaria, and chest tightness after ingestion of chicken meat. Percutaneous allergy skin testing with commercial chicken and turkey extract and freshly cooked chicken utilizing the prick-prick test was performed. RESULTS: Skin testing was positive with all extracts of chicken and turkey in the patient, and negative in 4 healthy adult controls. Skin tests with feather and egg extract were negative. CONCLUSION: This is the third report of severe allergy to chicken meat in the absence of egg allergy. Physicians should be aware of the presence of chicken allergy without concomitant feather or egg allergy, particularly in adults.

↩

[38] - Liccardi G, Szepfalusi Z, Noschese P, Nentwich I, D'Amato M, D'Amato G. Allergy to chicken meat without sensitization to egg proteins: A case report. J Allergy Clin Immunol 1997;100:577-579

↩

[39] - Moneret-Vautrin DA, Lemerdy P. Allergie à la viande de canard. Alim'Inter 2007;12:67-68

↩

[40] - Fontaine JF, Lavaud F, Sabouraud-Leclerc D, Perdu D, Prévost A. Allergie alimentaire à la viande de poulet et de dinde: à propos de 2 observations. Rev Fr Allergol Immunol Clin 1997;37:397

↩

[41] - Cahen YD, Fritsch R, Wüthrich B. Food allergy with monovalent sensitivity to poultry meat. Clin Exp Allergy 1998;28:1026-1030

BACKGROUND: Allergy to poultry meat is only rarely covered in science. The few reports are usually related to patients allergic to eggs or bird feathers. OBJECTIVE: Two patients with a clear history of monovalent, ingestive allergy to chicken and turkey meat, without other food allergies, were analysed. The relevant allergens were to be identified by immunoblotting. METHODS: Both patients were evaluated with skin tests and specific IgE determination (CAP). Allergens were identified by SDS-PAGE and immunoblotting. Cross-reactivity of chicken and turkey meat was examined by IgE inhibition experiments. RESULTS: Skin tests and specific IgE were positive for chicken and turkey in both patients. Cross-reactivities to other poultry meats were documented for duck and goose meat. No sensitization to egg components or poultry feathers could be found. Allergenic proteins of poultry meat were detected at molecular weights of 21, 23 and 50 kDa (distinct bands) and 13, 27 and 33kDa (faint bands). An additional band at 91 kDa for turkey, can probably not be considered a distinct allergenic epitope. Immunoblot inhibition confirmed cross-reactivity of chicken and turkey meat allergens. CONCLUSION: Food allergy to poultry meat is a distinct disorder with crossreactivity among chicken, turkey and other poultries. The relevant allergens were identified by immunoblotting. Associated food allergy to egg-components is unlikely as the patients were able to tolerate egg and eggs products.

↩

[42] - Martinez Alonso JC, Dominguez Ortega FJ, Fuentes Gonzalo MJ. Angioedema por sensibilización a carne de gallina. Allergol Immunopathol (Madr) 2003;31:50-52

BACKGROUND: Egg is the most frequent cause of food allergy in children. The bird-egg syndrome, found in a group of patients sensitized to egg through bird proteins, was infrequent in children. We report a patient with former history of hypersensitivity to egg who developed episodes of angioedema after ingestion of hen meat. METHODS: Prick testing with egg and their different antigenic protein fractions, alpha-livetin and chicken meat was performed. Antigens of hen meat were used for the skin prick test and prick-by-prick. Serum-specific IgE was identified with use of the CAP techniques and SDS-PAGE Immunoblotting. RESULTS: Prick test was positive with egg yolk, alpha-livetin and chicken meat. A prick-by-prick test with hen meat resulted positive in our patient, but the same test in four controls patients were negative. Serum specific IgE was positive for egg yolk and hen meat. CONCLUSION: Allergy reactions to hen meat are exceptional. We report a case of children with allergy to egg proteins and hen meat that suggest an IgE mediated hypersensitivity reaction. Skin test reveal sensitivity to egg yolk and alpha-livetin, but this pattern of sensitization was infrequent in children.

↩

[43] - Fontaine JF, Lavaud F, Sabouraud-Leclerc D, Perdu D, Prévost A. Allergie alimentaire à la viande de poulet et de dinde: à propos de 2 observations. Rev Fr Allergol Immunol Clin 1997;37:397

↩

[44] - Cahen YD, Fritsch R, Wüthrich B. Food allergy with monovalent sensitivity to poultry meat. Clin Exp Allergy 1998;28:1026-1030

BACKGROUND: Allergy to poultry meat is only rarely covered in science. The few reports are usually related to patients allergic to eggs or bird feathers. OBJECTIVE: Two patients with a clear history of monovalent, ingestive allergy to chicken and turkey meat, without other food allergies, were analysed. The relevant allergens were to be identified by immunoblotting. METHODS: Both patients were evaluated with skin tests and specific IgE determination (CAP). Allergens were identified by SDS-PAGE and immunoblotting. Cross-reactivity of chicken and turkey meat was examined by IgE inhibition experiments. RESULTS: Skin tests and specific IgE were positive for chicken and turkey in both patients. Cross-reactivities to other poultry meats were documented for duck and goose meat. No sensitization to egg components or poultry feathers could be found. Allergenic proteins of poultry meat were detected at molecular weights of 21, 23 and 50 kDa (distinct bands) and 13, 27 and 33kDa (faint bands). An additional band at 91 kDa for turkey, can probably not be considered a distinct allergenic epitope. Immunoblot inhibition confirmed cross-reactivity of chicken and turkey meat allergens. CONCLUSION: Food allergy to poultry meat is a distinct disorder with crossreactivity among chicken, turkey and other poultries. The relevant allergens were identified by immunoblotting. Associated food allergy to egg-components is unlikely as the patients were able to tolerate egg and eggs products.

↩

[45] - Martinez Alonso JC, Dominguez Ortega FJ, Fuentes Gonzalo MJ. Angioedema por sensibilización a carne de gallina. Allergol Immunopathol (Madr) 2003;31:50-52

BACKGROUND: Egg is the most frequent cause of food allergy in children. The bird-egg syndrome, found in a group of patients sensitized to egg through bird proteins, was infrequent in children. We report a patient with former history of hypersensitivity to egg who developed episodes of angioedema after ingestion of hen meat. METHODS: Prick testing with egg and their different antigenic protein fractions, alpha-livetin and chicken meat was performed. Antigens of hen meat were used for the skin prick test and prick-by-prick. Serum-specific IgE was identified with use of the CAP techniques and SDS-PAGE Immunoblotting. RESULTS: Prick test was positive with egg yolk, alpha-livetin and chicken meat. A prick-by-prick test with hen meat resulted positive in our patient, but the same test in four controls patients were negative. Serum specific IgE was positive for egg yolk and hen meat. CONCLUSION: Allergy reactions to hen meat are exceptional. We report a case of children with allergy to egg proteins and hen meat that suggest an IgE mediated hypersensitivity reaction. Skin test reveal sensitivity to egg yolk and alpha-livetin, but this pattern of sensitization was infrequent in children.

↩

[46] - Hilger C, Swiontek K, Hentges F, de Blay F, Pauli G. Cross-sensitization to hemoglobin in a case of respiratory allergy to pork and food allergy to chicken meat. 3rd International Symposium on Molecular Allergology, Salzburg, April 18-20, 2008, Poster n°48

↩

[47] - Besler M, Fiocchi A, Restani P. Allergen Data Collection: Beef (Bos domesticus). Internet Symp Food Allergens 2001;3(4):171-184

↩

[48] - Pilette C, Sohy C, Sauvage C, Just N, Wallaert B. L'allergie aux albumines sériques. Rev Fr Allergol Immunol Clin 2003;43:180-185

L'allergie à l'albumine sérique d'origine animale est une affection fréquente, nettement sous-diagnostiquée actuellement. Les voies de sensibilisation à cette protéine sont multiples étant donnée sa présence ubiquitaire dans les fluides biologiques. L'allergie à l'albumine contenue dans la viande de boeuf est la plus souvent rapportée et est fréquemment croisée avec les autres viandes. Les manifestations cliniques sont variées : diarrhée récurrente, dermatite atopique, syndrome oral, voire angio-oedème ou choc anaphylactique. L'albumine contenue dans les phanères des chats ou des chiens peut être responsable d'une rhinite ou d'un asthme. Les allergies croisées sont fréquentes, comme le classique syndrome porc-chat, mais aussi entre les oeufs et le lait ou les volailles. Le diagnostic est confirmé par tests épicutanés avec l'albumine pure et/ou par la recherche d'anticorps IgE spécifiques. Selon la symptomatologie, le traitement pourra consister en la cuisson attentive des aliments, l'éviction des contacts avec les chats ou les chiens ou en un traitement symptomatique.

↩

[49] - Fiocchi A, Restani P, Riva E, Qualizza R, Bruni P, Restelli AR, et al. Meat allergy: I--Specific IgE to BSA and OSA in atopic, beef sensitive children. J Am Coll Nutr 1995;14:239-244

The use of lamb meat products has been suggested as an alternative diet for polyallergic children, although until now this clinical practice has not been supported by in-depth biochemical/immunological studies. The aims of this research were: to evaluate cross-reactivity between lamb and beef; to evaluate the role of BSA and OSA as allergens in beef allergic children; and to evaluate cross-reactivity between BSA and OSA. METHODS: 16 children suffering from atopic dermatitis (AD), aged 12 months-8 8 years (mean age 2.61 +/- 1.93 years) were found skin prick test (SPT)--positive to bovine meat; all of them were also SPT-positive to ovine meat and to milk. After a period of restricted diet, the selected 16 children were recalled; 12 AD-free children (8 males and 14 females, aged 12 months-4.33 years (mean age 2.21 +/- 1.05 years) were evaluated by SPT and radioallergosorbent test (RAST) for the following allergens: bovine meat, ovine meat, BSA 1 mg/ml, OSA 1 mg/ml. Double-blind, placebo-controlled food challenge (DBPCFC) with bovine serum albumin (BSA) and ovine serum albumin (OSA) were performed. For SPT, the results were expressed in mm of wheal, and 3 mm was considered as the end point; correlation between wheal diameters was calculated by Spearman rank test. For DBPCFC, according to the Sampson's experimental procedure, BSA and OSA were given in pear juice (the dermal negative response to the pear juice was verified by fresh food SPT before starting the oral challenge test). The total dose administered to the children corresponded to the amount of albumin present in 180 g of calf or lamb meat (90 and 63 mg respectively, as calculated by Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SPS-PAGE). The administration of pear juice (containing placebo or albumin) and symptom evaluation were entrusted to medical people who did not know what the child received. RESULTS: All children tested SPT positive to bovine and ovine meat, and to BSA and OSA. Significant correlations were observed between the following diameters of wheal: BSA vs OSA (R = 0.846, p < 0.0001); ovine meat vs OSA (R = 0.769, p < 0.005); b.meat vs o.meat (R = 0.771, p < 0.005); and ovine meat vs BSA (R = 0.594, p < 0.043). In RAST, 6 of 12 children were positive to bovine meat, 3 to lamb meat, 4 to BSA and 3 to OSA. DBPCFC showed an immediate reaction to BSA or OSA in 2 and 3 children, respectively. One other child developed severe dyspnea, cough and asthma 3 hours after OSA challenge. CONCLUSIONS: BSA and OSA are important beef and lamb allergens; they share not only proteic sequences, but also allergenic properties. Clinical tolerance to BSA and OSA can be present in beef and lamb SPT-positive children.

↩

[50] - Vereda A, Cuesta J, Barderas M, de la Cuesta F, Pastor C, Vivanco F, et al. Beef allergy. EAACI 25th Congress, Vienna, 10-14 June, 2006, Poster n°1529

Background: Although beef meat is widely consumed in Western diets, beef allergy is rarely reported. The aim of the study was to describe a case of beef allergy and to identify the allergens. Method:A 16-month-old male, with atopic dermatitis and several food allergies (egg, fish and legumes), was studied. At the age of 7 months, he suffered labial angioedema and perioral erythema after the ingestion of scarcely cooked beef. He tolerated well done beef, as well as other meats and cow's milk. Skin tests, oral challenge and specific IgE determination were performed. Meat allergens were studied by SDS-PAGE, IgE-immunoblotting, inhibition assays and mass spectrometry. Results: Prick tests were positive to egg, fish, legumes, bovine serum albumin (BSA),bovine gamma globulin (BGG) and cow epithelium, and negative to the remaining milk proteins. Prick-prick tests were positive to raw and cooked beef, pork and lamb, and negative to chicken meat. Oral challenge test with raw beef meat elicited a positive response, with perioral wheals and erithema, and labial angioedema. However, the oral challenge was negative with cooked beef. Specific IgE was positive to BSA, cow's epithelium and milk, beef, pork and lamb meat. SDS-PAGE and immunoblotting with the beef extract revealed some prominent IgE-binding protein bands at >130, 67, 60 and 25 kDa, which were common to other meats (pork, rabbit, lamb), as well as to cow's epithelium and milk. IgE binding was decreased by heating the beef meat extract. Inhibition assays demonstrated cross-reactivity among the different meats, mainly between beef and lamb. BSA, b-enolase and creatin kinase were identified by mass spectrometry as allergens in the beef meat extract. Conclusions: We present a child with beef allergy, also sensitized to cow‚s milk and other meats. The responsible allergens are heat-labile, and could correspond to BSA and IGG. We also identified two proteins (b-enolase and creatin kinase), which have not been previously described as allergens.

↩

[51] - Ayuso R, Lehrer SB, Lopez M, Reese G, Ibanez RM, Martin-Esteban M, et al. Identification of bovine IgG as a major cross-reactive vertebrate meat allergen. Allergy 2000;55:348-354

Although beef is a main source of protein in Western diets, very little has been published on allergic reactions to beef or the main allergens implicated in these reactions. The aim was to evaluate the IgE antibody response to beef in suspected meat-allergic subjects and assess cross-reactivity of beef with other vertebrate meats. METHODS: Fifty-seven sera from suspected meat-allergic subjects were tested by grid blot for specific IgE antibodies to vertebrate meats (beef, lamb, pork, venison, and chicken), and the patterns of recognition of meat proteins were assessed by immunoblot studies. RESULTS: A 160-kDa band, identified as bovine IgG, was detected in raw beef in 83% (10/12) of beef-allergic subjects but in only 24% of the beef-tolerant subjects. IgE reactivity to a band of similar mol. mass was detected also in lamb and venison, but rarely in pork or chicken. Complete inhibition of the IgE reactivity to the bovine IgG was obtained with lamb, venison, and milk. IgE reactivity to this band also completely disappeared when beef or lamb extracts were separated under reducing conditions, indicating conformational epitopes. CONCLUSIONS: Bovine IgG appears to be a major cross-reacting meat allergen that could predict beef allergy. Further studies with oral IgG challenges should be performed to document the conclusion that in vitro reactivity correlates with clinical hypersensitivity. The role of bovine IgG in other bovine products such as milk, dander, or hair must also be studied, and the hypothesis that it is a cross-reacting allergen with other mammalian products validated.

↩

[52] - Ayuso R, Lehrer SB, Lopez M, Reese G, Ibanez RM, Martin-Esteban M, et al. Identification of bovine IgG as a major cross-reactive vertebrate meat allergen. Allergy 2000;55:348-354

Although beef is a main source of protein in Western diets, very little has been published on allergic reactions to beef or the main allergens implicated in these reactions. The aim was to evaluate the IgE antibody response to beef in suspected meat-allergic subjects and assess cross-reactivity of beef with other vertebrate meats. METHODS: Fifty-seven sera from suspected meat-allergic subjects were tested by grid blot for specific IgE antibodies to vertebrate meats (beef, lamb, pork, venison, and chicken), and the patterns of recognition of meat proteins were assessed by immunoblot studies. RESULTS: A 160-kDa band, identified as bovine IgG, was detected in raw beef in 83% (10/12) of beef-allergic subjects but in only 24% of the beef-tolerant subjects. IgE reactivity to a band of similar mol. mass was detected also in lamb and venison, but rarely in pork or chicken. Complete inhibition of the IgE reactivity to the bovine IgG was obtained with lamb, venison, and milk. IgE reactivity to this band also completely disappeared when beef or lamb extracts were separated under reducing conditions, indicating conformational epitopes. CONCLUSIONS: Bovine IgG appears to be a major cross-reacting meat allergen that could predict beef allergy. Further studies with oral IgG challenges should be performed to document the conclusion that in vitro reactivity correlates with clinical hypersensitivity. The role of bovine IgG in other bovine products such as milk, dander, or hair must also be studied, and the hypothesis that it is a cross-reacting allergen with other mammalian products validated.

↩

[53] - Fiocchi A, Restani P, Riva E, Qualizza R, Bruni P, Restelli AR, et al. Meat allergy: I--Specific IgE to BSA and OSA in atopic, beef sensitive children. J Am Coll Nutr 1995;14:239-244

The use of lamb meat products has been suggested as an alternative diet for polyallergic children, although until now this clinical practice has not been supported by in-depth biochemical/immunological studies. The aims of this research were: to evaluate cross-reactivity between lamb and beef; to evaluate the role of BSA and OSA as allergens in beef allergic children; and to evaluate cross-reactivity between BSA and OSA. METHODS: 16 children suffering from atopic dermatitis (AD), aged 12 months-8 8 years (mean age 2.61 +/- 1.93 years) were found skin prick test (SPT)--positive to bovine meat; all of them were also SPT-positive to ovine meat and to milk. After a period of restricted diet, the selected 16 children were recalled; 12 AD-free children (8 males and 14 females, aged 12 months-4.33 years (mean age 2.21 +/- 1.05 years) were evaluated by SPT and radioallergosorbent test (RAST) for the following allergens: bovine meat, ovine meat, BSA 1 mg/ml, OSA 1 mg/ml. Double-blind, placebo-controlled food challenge (DBPCFC) with bovine serum albumin (BSA) and ovine serum albumin (OSA) were performed. For SPT, the results were expressed in mm of wheal, and 3 mm was considered as the end point; correlation between wheal diameters was calculated by Spearman rank test. For DBPCFC, according to the Sampson's experimental procedure, BSA and OSA were given in pear juice (the dermal negative response to the pear juice was verified by fresh food SPT before starting the oral challenge test). The total dose administered to the children corresponded to the amount of albumin present in 180 g of calf or lamb meat (90 and 63 mg respectively, as calculated by Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SPS-PAGE). The administration of pear juice (containing placebo or albumin) and symptom evaluation were entrusted to medical people who did not know what the child received. RESULTS: All children tested SPT positive to bovine and ovine meat, and to BSA and OSA. Significant correlations were observed between the following diameters of wheal: BSA vs OSA (R = 0.846, p < 0.0001); ovine meat vs OSA (R = 0.769, p < 0.005); b.meat vs o.meat (R = 0.771, p < 0.005); and ovine meat vs BSA (R = 0.594, p < 0.043). In RAST, 6 of 12 children were positive to bovine meat, 3 to lamb meat, 4 to BSA and 3 to OSA. DBPCFC showed an immediate reaction to BSA or OSA in 2 and 3 children, respectively. One other child developed severe dyspnea, cough and asthma 3 hours after OSA challenge. CONCLUSIONS: BSA and OSA are important beef and lamb allergens; they share not only proteic sequences, but also allergenic properties. Clinical tolerance to BSA and OSA can be present in beef and lamb SPT-positive children.

↩

[54] - Restani P, Fiocchi A, Beretta B, Velona T, Galli CL. Meat allergy - III: proteins involved and cross-reactivity between different animal species. J Am Coll Nutr 1997;16:383-389

Although relatively infrequent, meat allergy represents a serious problem for children both because it is generally associated with intolerance to other protein sources and because of the suggested role of meat in stimulating the gastrointestinal development during weaning. OBJECTIVE: With these considerations, the aim of our work was to improve biological-biochemical knowledge of meat allergy. METHODS: This study was performed using in vivo skin prick test (SPT) and in vitro (electrophoresis associated with the immunoblotting technique) tests. RESULTS: Bovine serum albumin (BSA) and actin were the proteins most frequently involved in binding with the circulating IgE. BSA involvement was confirmed by SPT; the high number of positive responses observed with actin in immunoblotting was not confirmed by SPT data. Cross-reactivity between serum albumins from different animal species was demonstrated. Our studies show that in this group of children, the correspondence between the percentage of sequence identity (phylogenetic similarity) and the number of positive responses was surprisingly high. CONCLUSIONS: Although further studies are necessary, the data reported here provide new biochemical data on meat allergy.

↩

[55] - Fuentes MM, Palacios R, Garcés MM, Caballero ML, Moneo I. Isolation and characterization of a heat-resistant beef allergen: myoglobin. Allergy 2004;59:327-331

BACKGROUND: Meat allergy is rarely reported. Most of the described cases are sensitizations to bovine serum albumin . OBJECTIVE: The aim of the study was to describe a case of allergy to a new meat allergen and, after its characterization . METHODS: A 35-year-old nonatopic female with allergic episodes after ingestion of several types of meat was studied. Skin tests (prick and prick-to-prick); total and specific immunoglobulin E (IgE) determination; sodium dodecyl sulphate-polyacrylamide gel electrophoresis and specific IgE determination by immunoblotting under different conditions were performed. A 17-kDa allergen was semipurified by ethanol fractionation and its amino-terminal sequence was determined. The existence of specific IgE directed to this protein was studied by immunoblot in 80 atopic patients . RESULTS: The patient showed specific IgE antibodies to a 17-kDa protein. During the isolation of this allergen it was found that a 70-90% (vol/vol) ethanol concentration was able to purify the protein. The characterization revealed that it was a heat-resistant protein without disulfide bonds. N-terminal amino acid sequence (16 residues) showed identity with myoglobin. The study of specific IgE to this allergen among atopic patients showed that it was recognized by about 1% of the subjects . CONCLUSIONS: We describe a case of meat allergy caused by myoglobin. This is the first described case of monosensitization to this protein.

↩

[56] - Ayuso R, Lehrer SB, Tanaka L, Ibanez MD, Pascual C, Burks AW, et al. IgE antibody response to vertebrate meat proteins including tropomyosin. Ann Allergy Asthma Immunol 1999;83:399-405

Although meat is a main source of proteins in western diets, little information is available regarding allergy to vertebrate meats or the allergens implicated in these reactions. OBJECTIVE: To evaluate the in vitro IgE antibody response to different vertebrate meats in suspected meat-allergic subjects, as well as the possible role of tropomyosin in meat allergy and to analyze the cross-reactivity between vertebrate meats and the effect of heating on the IgE-binding to meat proteins. METHODS: Fifty-seven sera from suspected meat-allergic subjects were tested by grid blot to extracts of beef, lamb, pork, venison, chicken, and turkey and to four mammalian tropomyosins of different origins. RESULTS: Meat-allergic subjects have IgE antibodies to proteins in different mammalian meats (43/57 subjects); cross-reactivity with avian meat was limited: less than 50% (19/43) of meat positive sera reacted to chicken. In contrast, most of the poultry-positive sera also reacted to different mammalian meats. In general, there was stronger IgE reactivity to raw meats in comparison to cooked meats; an exception was six cases in which IgE reactivity to cooked poultry was stronger. Weak IgE reactivity to tropomyosin was detected in only 2/57 sera tested. CONCLUSIONS: Suspected meat-allergic subjects have serum IgE directed to meat proteins. In vitro cross-reactivity among mammalian meats appears to be important, while cross-reactivity to poultry is limited indicating mammalian-specific proteins. Although cooking in general denatures meat proteins rendering them less allergenic, in some cases the process of cooking may result in the formation of new allergenic moieties. The muscle protein tropomyosin is not an important vertebrate meat allergen.

↩

[57] - Mullins RJA, Apostolou E. Anaphylaxis to Beef, Gelatin and Haemaccel. AAAAI 60th Annual Meeting, San Francisco, 19-23 March 2004, Poster n°861

Rationale Meat-derived gelatin is commonly added to processed foods. 3 pts were seen initially, 1 allergic to topical & oral gelatin & 2 with anaphylaxis (Ax) to Haemaccel. All subsequently developed allergy to beef, suggesting that gelatin was a trigger. Method s : 14 patients with suspected beef/gelatin Ax, 62 controls & 31 with idiopathic Ax (IAx; 14 prospectively) were investigated for gelatin sensitivity by skin testing (ST) & RAST. Result s : 8/14 patients with beef allergy reacted clinically to gelatin on separate occasions; gelatin RAST/ST were positive in 7 & 8/8, respectively. Gelatin ST were positive in 3 additional patients (6-20mm weals). Overall, 3/14 beef allergics had positive beef ST. 3 with negative gelatin ST/RAST had positive RAST to other beef proteins - BSA, bovine gammaglobulin & betalipoprotein IV, betalactobulin. 1/18 recalled IAx patients 1995-2001 had positive gelatin ST. By contrast, ST were negative in RJM (45 occasions) & 62 controls. 10/10 control sera had negative RAST. 92 patients with Ax were evaluated prospectively 2002-3. Triggers were animals, exercise, medication, idiopathic, stings, food allergy, healthy controls (1, 5, 5, 13,18, 47, 2 cases, respectively). Ax occurred after beef in 2/2 with positive gelatin ST, but only 1 had positive beef ST. The beef ST negative subject nonetheless reacted to deliberate Haemaccel challenge (~1.1gm IVI gelatin). Conclusions : Gelatin is an important beef allergen and may account for some cases of IAx. A positive ST convey risk for gelatin, meat & Haemaccel Ax which may be missed if one relies only on commercial beef allergens.

↩

[58] - Sakaguchi M, Nakayama T, Inouye S. Food allergy to gelatin in children with systemic immediate-type reactions, including anaphylaxis, to vaccines. J Allergy Clin Immunol 1996;98:1058-1061

BACKGROUND: Anaphylaxis to measles-mumps-rubella vaccines has been reported. We have suspected that most such reactions are caused by gelatin contained in the vaccines. OBJECTIVE: To confirm the relation between systemic allergic reactions to vaccines and the presence of anti-gelatin IgE, we measured anti-gelatin IgE in children who demonstrated allergy to gelatin-containing vaccines. Furthermore, to clarify the relation between allergic reactions to gelatin in vaccines and foods, we surveyed the occurrence of allergic reactions to gelatin-containing foods in the same children. METHODS: Serum samples were taken from 26 children who had systemic immediate-type reactions, including anaphylactic shock, to vaccines and the same number of children without allergic reactions. Specific IgE to gelatin in these samples was measured. We then surveyed whether these children had allergic reactions to gelatin-containing foods before and after vaccination. RESULTS: Twenty-four of the 26 children with allergic reactions to vaccines had anti-gelatin IgE ranging from 1.2 to 250 Ua/ml. Seven had allergic reactions on ingestion of gelatin-containing foods. Of these, two had reactions before vaccination, and five had reactions after vaccination. All the control children without allergic reactions to vaccines had no anti-gelatin IgE. CONCLUSION: We reconfirmed a strong relationship between systemic immediate-type allergic reactions, including anaphylaxis, to vaccines and the presence of specific IgE to gelatin. Moreover, some of the children also had allergic reactions to food gelatin before or after vaccination.

↩

[59] - Sakaguchi M, Hori H, Ebihara T, Irie S, Yanagida M, Inouye S. Reactivity of the immunoglobulin E in bovine gelatin-sensitive children to gelatins from various animals. Immunology 1999;96:286-290

It has been reported that most children who showed anaphylaxis to measles, mumps and rubella vaccines containing bovine gelatin as a stabilizer have anti-bovine gelatin IgE. The present study was designed to investigate the reactivity of IgE in bovine gelatin-sensitive children to gelatins from various animals, and the antigenic cross-reactivity between the gelatins. Serum samples taken from 10 children who showed anaphylaxis to vaccines containing bovine gelatin were used in this study. The level of anti-bovine gelatin IgE in these serum samples ranged from 11.0 to 251 Ua/ml. The IgE in most of the children reacted to kangaroo and mouse gelatins, to which they had had little or no exposure as a food or a vaccine stabilizer. The IgE binding to kangaroo and mouse gelatins was completely inhibited by bovine gelatin, whereas reciprocal inhibition was not complete, indicating that antigenic cross-reactivity is present between the mammalian gelatins. Only one child had strong IgE reactivity to fish gelatins, and this reactivity was not inhibited by bovine gelatin, indicating that no antigenic cross-reactivity exists between bovine and fish gelatins. Most of the children who displayed sensitivity to bovine gelatin showed IgE reactivity to other mammalian gelatins. This reactivity may be due primarily to the antigenic cross-reactivity between mammalian gelatins.

↩

[60] - Vereda A, Cuesta J, Barderas M, de la Cuesta F, Pastor C, Vivanco F, et al. Beef allergy. EAACI 25th Congress, Vienna, 10-14 June, 2006, Poster n°1529

Background: Although beef meat is widely consumed in Western diets, beef allergy is rarely reported. The aim of the study was to describe a case of beef allergy and to identify the allergens. Method:A 16-month-old male, with atopic dermatitis and several food allergies (egg, fish and legumes), was studied. At the age of 7 months, he suffered labial angioedema and perioral erythema after the ingestion of scarcely cooked beef. He tolerated well done beef, as well as other meats and cow's milk. Skin tests, oral challenge and specific IgE determination were performed. Meat allergens were studied by SDS-PAGE, IgE-immunoblotting, inhibition assays and mass spectrometry. Results: Prick tests were positive to egg, fish, legumes, bovine serum albumin (BSA),bovine gamma globulin (BGG) and cow epithelium, and negative to the remaining milk proteins. Prick-prick tests were positive to raw and cooked beef, pork and lamb, and negative to chicken meat. Oral challenge test with raw beef meat elicited a positive response, with perioral wheals and erithema, and labial angioedema. However, the oral challenge was negative with cooked beef. Specific IgE was positive to BSA, cow's epithelium and milk, beef, pork and lamb meat. SDS-PAGE and immunoblotting with the beef extract revealed some prominent IgE-binding protein bands at >130, 67, 60 and 25 kDa, which were common to other meats (pork, rabbit, lamb), as well as to cow's epithelium and milk. IgE binding was decreased by heating the beef meat extract. Inhibition assays demonstrated cross-reactivity among the different meats, mainly between beef and lamb. BSA, b-enolase and creatin kinase were identified by mass spectrometry as allergens in the beef meat extract. Conclusions: We present a child with beef allergy, also sensitized to cow‚s milk and other meats. The responsible allergens are heat-labile, and could correspond to BSA and IGG. We also identified two proteins (b-enolase and creatin kinase), which have not been previously described as allergens.

↩

[61] - Wong KN, Lee WS, Ong SY, Lim YP, Chew FT. Identification of allergen homologues among 59,454 unigenes of Sus scrofa (pig), Bos taurus (cow), Gallus gallus (chicken) and Oncorhynchus mykiss (trout). EAACI 23th Congress, Amsterdam, 12-16 June, 2004, Poster n°1056

Background: Many allergenic components from food have been identified, but little is known about allergy to vertebrate meat or the allergens involved. cDNA and PCR-based cloning methods have successfully defined the primary structures of many allergens. We previously described the use of in-house expressed sequence tag (EST) catalogues to rapidly identify many new allergens from dust mites, cockroaches, fungi and pollen. We describe here the identification of putative allergens and isoforms obtained from the Sus scrofa (pig), Bos taurus (cow), Gallus gallus (chicken) and Oncorhynchus mykiss (trout) EST and Unigene databases obtained from the public domain that showed high degree of identity to other known allergens in the GenBank. This study was initiated after observations that specific IgE levels to pork, beef, chicken and fish were relatively high and prevalent in a number of Asian populations. METHOD: A total of 59,454 Unigenes of Sus scrofa, Bos taurus, Gallus gallus and Oncorhynchus mykiss (representing more than 640,000 mRNA or EST sequences) were matched to genes identified from other organisms in the public databases. Queries that showed high degree of identity to known allergens were selected (bit score>100; E<0.001; and identity of >50% over long [80] consecutive amino acid sequences). Upon identification of putative allergen homologues, complete full-length sequences were then obtained. RESULTS: To date, a total of 662 clusters (1.1%) from these four species showed significant sequence identity to known allergens. Among the putative allergen homologues identified are homologues to enolases, arginine kinases, aldehyde dehydrogenases, conalbumin / ovotransferrin, fatty acid binding proteins, serum albumin (Bos d, Gal d, Can f and Fel d allergen homologues), beta-lactoglobulin, alpha lactalbumin, paramyosin, trypomyosin, heat shock proteins, calcium-binding proteins, various dust mite allergens, and Can f 1 and Equ c 1 homologues. CONCLUSION: The EST and Unigene catalogues are thus valuable resources that have enabled us to identify and isolate possible putative allergens. Our current work has extended to include possible cross reactive allergens from major staple plant foods such as rice, wheat, barley, maize, soybean and potato.

↩

[62] - Kelso JM, Cockrell G, Helm RM, Burks AW. Common allergens in avian meats. J Allergy Clin Immunol 1999;104:202-204

BACKGROUND: Reports of allergy to bird meats are uncommon, and most have been in patients with "bird-egg syndrome." OBJECTIVE: We sought to evaluate 3 patients who reported allergic reactions to several avian meats, but who denied allergic reactions to eating eggs. The patients required yellow fever vaccine for entry into the military. METHODS: Patients were skin tested with commercial extracts of chicken, turkey, and egg, as well as with crude extracts made from dove and quail meat, and with yellow fever vaccine. Immunoblots for IgE antibody were performed by using the same materials used for skin testing plus extracts of duck and goose meat. RESULTS: Skin tests were positive in all 3 patients to chicken, turkey, dove, quail, and yellow fever vaccine and negative to egg. This included some positive skin test responses to bird meats the patients denied ever having eaten. The vaccine was administered in graded doses. Immunoblots revealed IgE binding to several proteins of similar molecular weights in all of the avian meats but not to egg or yellow fever vaccine. Again, this included IgE antibody to some bird meats the patients denied ever having eaten. CONCLUSION: Patients allergic to one bird meat may be allergic to others, including game birds, probably because of cross-reacting allergens. Such patients may have to exercise caution even when eating bird meats they have not previously ingested. The relationship of this allergy to yellow fever vaccine, if any, remains to be determined

↩

[63] - Tauer-Reich I, Fruhmann G, Czuppon AB, Baur X. Allergens causing bird fancier's asthma. Allergy 1994;49:448-453

The study investigates to what extent bird feathers contain relevant allergens/antigens involved in bird fancier's asthma. The study group consisted of two budgerigar fanciers, two parrot fanciers and one canary fancier. All subjects complained of asthmatic symptoms, caused by contact with their birds, and they showed a significant bronchial hyperreactivity to acetylcholine. Positive IgE antibody reactions to bird sera as well as to extracts of feathers were observed in RAST. Well-defined major allergenic bands could be detected and identified in the IgE immunoblots with feather extracts as well as with serum proteins of budgerigar, parrot, pigeon, canary, and hen (mol. mass 20-30 kDa and 67 kDa). The most pronounced bands appeared with the extracts of species to which an exposure had taken place. Weaker IgG-binding patterns were also observed. Our results show that inhalable feather dust contains several allergenic components which cross-react with serum allergens/antigens of the same as well as of other bird species. This emphasizes the significance of bird feathers for immediate-type allergic reactions.

↩

[64] - Zacharisen MC. Severe allergy to chicken meat. WMJ 2006;105:50-52

INTRODUCTION: While allergic reactions to poultry products in the form of feathers and eggs are common, allergic reactions to chicken meat are rare. Despite the popularity of chicken in today's healthy diet, severe reactions after ingesting chicken meat are rarely described. This report describes a patient who developed chicken meat anaphylaxis without experiencing allergy to eggs or feathers. METHODS: A carefully obtained history from a 41-year-old male suggested chicken meat as the cause of his symptoms. He developed abdominal cramping, generalized urticaria, and chest tightness after ingestion of chicken meat. Percutaneous allergy skin testing with commercial chicken and turkey extract and freshly cooked chicken utilizing the prick-prick test was performed. RESULTS: Skin testing was positive with all extracts of chicken and turkey in the patient, and negative in 4 healthy adult controls. Skin tests with feather and egg extract were negative. CONCLUSION: This is the third report of severe allergy to chicken meat in the absence of egg allergy. Physicians should be aware of the presence of chicken allergy without concomitant feather or egg allergy, particularly in adults.

↩

[65] - Liccardi G, Szepfalusi Z, Noschese P, Nentwich I, D'Amato M, D'Amato G. Allergy to chicken meat without sensitization to egg proteins: A case report. J Allergy Clin Immunol 1997;100:577-579

↩

[66] - Kuehn A, Lehners-Weber C, Hentges F. Allergy to chicken meat with sensitization to chicken alpha parvalbumin. 3rd International Symposium on Molecular Allergology, Salzburg, April 18-20, 2008, Poster n°49

↩

[67] - Hilger C, Swiontek K, Hentges F, de Blay F, Pauli G. Cross-sensitization to hemoglobin in a case of respiratory allergy to pork and food allergy to chicken meat. 3rd International Symposium on Molecular Allergology, Salzburg, April 18-20, 2008, Poster n°48

↩

[68] - Ayuso R, Lehrer SB, Tanaka L, Ibanez MD, Pascual C, Burks AW, et al. IgE antibody response to vertebrate meat proteins including tropomyosin. Ann Allergy Asthma Immunol 1999;83:399-405

Although meat is a main source of proteins in western diets, little information is available regarding allergy to vertebrate meats or the allergens implicated in these reactions. OBJECTIVE: To evaluate the in vitro IgE antibody response to different vertebrate meats in suspected meat-allergic subjects, as well as the possible role of tropomyosin in meat allergy and to analyze the cross-reactivity between vertebrate meats and the effect of heating on the IgE-binding to meat proteins. METHODS: Fifty-seven sera from suspected meat-allergic subjects were tested by grid blot to extracts of beef, lamb, pork, venison, chicken, and turkey and to four mammalian tropomyosins of different origins. RESULTS: Meat-allergic subjects have IgE antibodies to proteins in different mammalian meats (43/57 subjects); cross-reactivity with avian meat was limited: less than 50% (19/43) of meat positive sera reacted to chicken. In contrast, most of the poultry-positive sera also reacted to different mammalian meats. In general, there was stronger IgE reactivity to raw meats in comparison to cooked meats; an exception was six cases in which IgE reactivity to cooked poultry was stronger. Weak IgE reactivity to tropomyosin was detected in only 2/57 sera tested. CONCLUSIONS: Suspected meat-allergic subjects have serum IgE directed to meat proteins. In vitro cross-reactivity among mammalian meats appears to be important, while cross-reactivity to poultry is limited indicating mammalian-specific proteins. Although cooking in general denatures meat proteins rendering them less allergenic, in some cases the process of cooking may result in the formation of new allergenic moieties. The muscle protein tropomyosin is not an important vertebrate meat allergen.

↩

[69] - Palacios Benito R, Alvarez-Lovel MC, Martinez-Cocera C, Del Castillo Paya MM, Romanillos RA. Allergy to meat. Allergy 2002;57:858-859

↩

[70] - Cisteró-Bahíma A, Enrique E, San Miguel-Moncin MM, Alonso R, Bartra J, Fernandez-Parra B, et al. Meat allergy and cross-reactivity with hamster epithelium. Allergy 2003;58:161-162

↩

[71] - Fuentes MM, Palacios R, Garcés MM, Caballero ML, Moneo I. Isolation and characterization of a heat-resistant beef allergen: myoglobin. Allergy 2004;59:327-331

BACKGROUND: Meat allergy is rarely reported. Most of the described cases are sensitizations to bovine serum albumin . OBJECTIVE: The aim of the study was to describe a case of allergy to a new meat allergen and, after its characterization . METHODS: A 35-year-old nonatopic female with allergic episodes after ingestion of several types of meat was studied. Skin tests (prick and prick-to-prick); total and specific immunoglobulin E (IgE) determination; sodium dodecyl sulphate-polyacrylamide gel electrophoresis and specific IgE determination by immunoblotting under different conditions were performed. A 17-kDa allergen was semipurified by ethanol fractionation and its amino-terminal sequence was determined. The existence of specific IgE directed to this protein was studied by immunoblot in 80 atopic patients . RESULTS: The patient showed specific IgE antibodies to a 17-kDa protein. During the isolation of this allergen it was found that a 70-90% (vol/vol) ethanol concentration was able to purify the protein. The characterization revealed that it was a heat-resistant protein without disulfide bonds. N-terminal amino acid sequence (16 residues) showed identity with myoglobin. The study of specific IgE to this allergen among atopic patients showed that it was recognized by about 1% of the subjects . CONCLUSIONS: We describe a case of meat allergy caused by myoglobin. This is the first described case of monosensitization to this protein.

↩

[72] - Benito C, Fernandez-Rivas M. Combined respiratory and food allergies to rabbit. Allergy Clin Immunol Int 2005;17(Suppl. 1):361

Background. Exposure to rabbits as domestic pets or laboratory animals can induce respiratory allergy. Allergic reactions to the ingestion of rabbit meat in patients with respiratory allergy to rabbit has not been reported. Patients. Case 1. A 22 years-old woman reported since childhood rhinoconjunctivitis (RC) and asthma while playing with rabbits, and oropharyngeal itching (OAS) after eating rabbit meat. At 14 years of age she presented an anaphylaxis while playing volleyball one hour after having eaten rabbit. Case 2. A 10 years-old boy reported since the age of 6, several episodes of RC and asthma after exposure to rabbits. At the age of 7 he presented OAS while eating rabbit, immediately followed by RC and asthma, that required emergency room treatment. Both patients tolerated all foods of animal origin, including meats of other species. Patient 1 presented RC due to cat allergy. No other inhalant allergies where present in these 2 patients. Methods. Different rabbit extracts were prepared from epithelium, meat, serum, urine, and albumin, and used in skin prick tests (SPTs), ELISA-IgE, ELISAinhibition assays, and immunoblots. Results. Case 1: SPTs (wheal mm) epithelium 10, meat 5; ELISA (aKU/L) epithelium 56.73, meat 0.93, serum 0.56, urine 4.30, albumin 1.79. Case 2: SPTs epithelium 11, meat 4; ELISA epithelium 110.16, meat 1.11, serum 0.74, urine 5.81, albumin 1.34. The ELISA to rabbit meat was completely inhibited by rabbit epithelium, urine and albumin. The maximum inhibitions of the ELISA to rabbit epithelium by rabbit meat were below 44%, whereas the figures for rabbit urine were over 90%, and for rabbit albumin over 73%. Several allergens were identified in the immunoblots, but the most prominent ones were a band 60kDa (albumin) in epithelium, meat, serum and urine (cases 1,2), a band 42 kDa (probably actin) only observed in the meat (cases 1,2), a band 150 kDa (probably IgG) in epithelium, serum and urine (case 2), a band 17 kDa in epithelium (probably Ory c 1) (case 2). Conclusion. We present 2 cases of RC and asthma induced by inhaled exposure to rabbit who have subsequently developed severe reactions after the intake of rabbit meat. The reactivity to rabbit meat might result from sensitisation to rabbit allergens present in epitelium and urine by the inhalant route, together with a primary sensitisation to meat allergens (such as actin) through the oral route.

↩

[73] - Asensio T, Crespo JF, Sanchez-Monge R, Lopez-Torrejon G, Somoza ML, Rodriguez J, et al. Novel plant pathogenesis-related protein family involved in food allergy. J Allergy Clin Immunol 2004;114:896-899

Background Members belonging to 9 different families of plant pathogenesis-related (PR) proteins have been identified as pollen and food allergens. However, no PR-1 protein, a family widely distributed throughout the plant kingdom, has been involved so far in allergic reactions. On the other hand, melon ranges among the most relevant fruits causing food allergy in some countries, but the majority of its allergens remain still unidentified. Objective We sought to identify melon allergens related to plant PR proteins. Methods A serum pool or individual sera from 17 patients with allergy to melon confirmed by means of double-blind, placebo-controlled food challenge were used to detect IgE binding proteins of extracts from melon pulp and juice. Cuc m 3 was isolated from melon juice by reverse-phase HPLC and characterized by means of N-terminal amino acid sequencing of internal peptides, matrix-assisted laser desorption/ionization mass spectrometry analysis, direct and inhibition ELISA assays, and skin prick tests. Results Cuc m 3 was a minor component of the melon juice, with a molecular weight of 16,097 d and a blocked N-terminus. N-terminal amino acid sequences of 3 different peptides derived from endo-Lys C digestion (overall 41 residues) showed more than 60% of sequence identity with PR-1 proteins from grape and cucumber. Cuc m 3 bound IgE from 12 of 17 sera from patients allergic to melon and inhibited approximately 40% and 70% of the IgE binding to melon pulp and juice extracts, respectively. Positive skin prick test responses to purified Cuc m 3 were found in 2 of 14 allergic patients. Conclusion A new melon allergen belonging to the PR-1 protein family has been isolated and characterized. It is the first evidence of the involvement of this plant protein family in food allergy.

↩

[74] - Fuentes Aparicio V, Sanchez Marcen I, Perez Montero A, Baeza ML, de Barrio Fernandez M. Allergy to mammal's meat in adult life: immunologic and follow-up study. J Investig Allergol Clin Immunol 2005;15:228-231

Allergy to bovine meat and Bovine serum albumin (BSA) is exceptional, especially in the adult life. BSA is considered a minor allergen in cow's milk allergy, but there is little information about this antigen in reactions produced by other beef products as meat. To our knowledge, evolutive studies of beef's allergic patients have not been reported. OBJECTIVE: To present one patient with several allergic reactions (urticaria-angioedema) after eating different mammals' meat. METHODS: The patient underwent allergy testing through skin prick test (SPT), specific IgE detection and SDS-PAGE Immunoblotting and Immunodot inhibition studies. Periodic determinations of specific IgE to meats and epithelia were performed. RESULTS: Routine studies for chronic urticaria were normal or negative. SPT showed positive responses to pork, cow, rabbit and lamb meat, and dog, pork, sheep and cow epithelia. It was negative to cat, horse, guinea pig, rabbit, lamb, mouse epithelia, mixture of feathers, cow milk, soybean, mustard, mites and chicken meat and Anisakis simplex. Intradermal testing to BSA was positive. Determinations of specific IgE were positive to beef meat, lamb meat, pork meat and rabbit meat, dog, cat, cow, sheep and pork dander, cow's milk, and negative to chicken meat. Immunoblot and immunodot studies showed IgE recognition bands to bovine and lamb meat which were totally inhibited by BSA. A progressive reduction of the total and specific IgE, the latter until its total negativization, has been observed in the following three-year period. CONCLUSION: We report a case of IgE-mediated urticaria-angioedema due to BSA hypersensitivity, possibly induced by a subclinical sensitivity to dog and cat epithelium. The exclusion diet in patients allergic to these foods may be a progressive loss of clinical allergy.

↩

[75] - Vereda A, Cuesta J, Barderas M, de la Cuesta F, Pastor C, Vivanco F, et al. Beef allergy. EAACI 25th Congress, Vienna, 10-14 June, 2006, Poster n°1529

Background: Although beef meat is widely consumed in Western diets, beef allergy is rarely reported. The aim of the study was to describe a case of beef allergy and to identify the allergens. Method:A 16-month-old male, with atopic dermatitis and several food allergies (egg, fish and legumes), was studied. At the age of 7 months, he suffered labial angioedema and perioral erythema after the ingestion of scarcely cooked beef. He tolerated well done beef, as well as other meats and cow's milk. Skin tests, oral challenge and specific IgE determination were performed. Meat allergens were studied by SDS-PAGE, IgE-immunoblotting, inhibition assays and mass spectrometry. Results: Prick tests were positive to egg, fish, legumes, bovine serum albumin (BSA),bovine gamma globulin (BGG) and cow epithelium, and negative to the remaining milk proteins. Prick-prick tests were positive to raw and cooked beef, pork and lamb, and negative to chicken meat. Oral challenge test with raw beef meat elicited a positive response, with perioral wheals and erithema, and labial angioedema. However, the oral challenge was negative with cooked beef. Specific IgE was positive to BSA, cow's epithelium and milk, beef, pork and lamb meat. SDS-PAGE and immunoblotting with the beef extract revealed some prominent IgE-binding protein bands at >130, 67, 60 and 25 kDa, which were common to other meats (pork, rabbit, lamb), as well as to cow's epithelium and milk. IgE binding was decreased by heating the beef meat extract. Inhibition assays demonstrated cross-reactivity among the different meats, mainly between beef and lamb. BSA, b-enolase and creatin kinase were identified by mass spectrometry as allergens in the beef meat extract. Conclusions: We present a child with beef allergy, also sensitized to cow‚s milk and other meats. The responsible allergens are heat-labile, and could correspond to BSA and IGG. We also identified two proteins (b-enolase and creatin kinase), which have not been previously described as allergens.

↩

[76] - Touraine F, Principaud Perrier M, Brianchon C, Sagot L, Boumediene A, Sainte Laudy J, et al. Particularités de l'allergie alimentaire au porc. Rev Fr Allergol Immunol Clin 2006;46:388-391

L'allergie alimentaire au porc est rare. Cependant, nous en rapportons 13 cas, concernant surtout l'allergie aux rognons. Les réactions peuvent être sévères. Les sensibilisations croisées sont nombreuses avec d'autres mammifères. Une meilleure connaissance des allergènes en cause est nécessaire pour mieux identifier les risques chez ces patients.

↩

[77] - Perez A, Sanchez I, Vicente M, Baeza ML, Rodriguez JJ, Marañón F, et al. Allergy to mammal's meat. J Allergy Clin Immunol 2000;105(1 part 2):S139

↩

[78] - Savi E, Rossi A, Incorvaia C. Cat-pork syndrome: a case report with a thee years follow-up. Eur Ann Allergy Clin Immunol 2006;38:366-368

A case of cat-pork syndrome with subsequent follow-up in a 17-year-old male patient is reported. At the initial observation, the patient was sensitized to cat epithelium--along with house dust mites and grass pollen--from two years. In 2001 he had an immediate reaction with urticaria, angioedema and dyspnea after eating grilled meat and sausage, and skin tests and CAP/RAST revealed a sensitization to pork meat, with a value of 4.7 KU/L for pork meat, and of 55 KU/L for cat epithelium. The patient was followed up for three years with annual repetition of diagnostic tests. The elimination of pork meat from the diet was incomplete, with slight skin reactions to small amounts of cooked pork meat but tolerance to seasoned pork products such as salami. A challenge test with pork meat in 2004 was positive, with angioedema and asthma symptoms, and CAP/RAST showed a value of 43 KU/L for cat epithelium and 4 KU/L for pork meat. RAST inhibition confirmed the significant cross-reactivity between the two allergen sources. These findings provide some knowledge on the natural history of the cat-pork syndrome, and confirm that very prolonged avoidance of the offending foods are needed to expect a loss of sensitization.

↩

[79] - Kanny G, De Hauteclocque C, Moneret-Vautrin DA. Food anaphylaxis to bovine serum albumin. J Allergy Clin Immunol 1998;101:137-139

↩

[80] - Rico-Diaz A, Diaz Roman T, Costa-Dominguez M, Ledesma A. Cow milk and meat allergy in a patient with allergy to hamster can be mediated by sera albumin. Allergy 2009;64(Suppl. 90):234-235

Background: Pork meat is a common food in diet but the allergy to this is rare. Much of the allergies to meat have been produced by primary sensitization to animal aeroallergens. Thus, in patients with pork meat allergy, the sensitization has been produced by cat antigen. Sera albumin is a putative cross reactive antigen in response. We ought to know allergy mechanism in a poly-sensitive patient with allergy to dust mites, animal epithelia and a late debut of cow milk allergy. Methods: A 10 years old female with diagnostic of dust mites and animals epithelia allergy undergoes eczema, rhinitis and asthma. She was living with cats, dogs, and hamster. Since she was 14 years old, she had abdominals pains, vomits, diarrhea, oral itch, rash and facial urticaria, immediately after the ingestions of lacteous derivates, or fresh sausages. Cooked meat was always well tolerated. Skin Prick tests to aeroallergens, to commercial food extract including cow milk and to different meats were made. Prick-prick with cooked and uncooked meat and specific IgE to animal allergens were also determined. Western Blot (WB) test. An extract of beef meat at 10% (p/v) in phosphate buffers was obtained, and conveniently stored at -20°C until use. Commercial extracts of hamster and cat epithelia, pork and beef meat, were employed in a non reduced SDS PAGE assay and transferred to nitrocellulose membrane. The patient's serum was incubated with the nitrocellulose strips to detect proteins with affinity to serum IgE. Also, the patient's serum was incubated with extract of hamster or cow epithelium in other strips in a blocking WB assay. Results: Prick test. D Pteronyssinus 10mm, Hamster 8mm, Cat 5mm, Dog 5mm, Cow milk (-), casein (-), BLG (-), ALA 4mm, BSA 4mm, histamine (8mm). Prick-Prick. Pork meat 11mm, cooked pork meat (-), Beef meat 3mm, cooked beef meat (-). IgE to hamster > 100 KU/ l; pork meat 9,2 KU/l; BSA 0,38KU/l. WB: Several bands were observed: A 60Kd band in blots with beef meat, pork meat and hamster epithelium, suggesting IgE recognizing sera albumin, a 19Kd band on cat epithelium (Fel d1) and 15Kd band on hamster epithelium. An evident reduction in 60Kd band intensity was observed following inhibition of patient serum with hamster extract in blocking WB. That diminution of band was observed in pork meat but not in beef meat blot. Conclusion: Our results suggest a food allergy to cow milk and pork meat proteins probably in relation to primary sensitization of hamster.

↩

[81] - Aalberse RC, Stapel SO. Structure of food allergens in relation to allergenicity. Pediatr Allergy Immunol 2001;12(suppl. 14):10-14

↩

[82] - Spitzauer S, Schweiger C, Sperr WR, Pandjaitan B, Valent P, Muhl S, et al. Molecular characterization of dog albumin as a cross-reactive allergen. J Allergy Clin Immunol 1994;93:614-627

Indoor allergens comprise a group of allergenic proteins that are commonly derived from house dust mite and cat and dog dander. In addition to the two major dog allergens (molecular weights: 19 and 23 kd), dog albumin represents an important allergen for up to 35% of patients who are allergic to dogs. In IgE immunoblot inhibition studies and histamine release tests it has been demonstrated that patients who react to dog albumin exhibit IgE reactivity with purified albumins from cat, mouse, chicken, and rat. The proportion of dog-specific IgE directed against dog albumin was determined for patients allergic to dog albumin, and it ranges from 70% to 90%. By IgE immunoscreening of a lambda gt11 expression library from a dog salivary gland, we identified a number of reactive complementary DNA clones. All patients with IgE reactivity against natural dog albumin displayed IgE reactivity to the beta-galactosidase fusion protein encoded by clone 54c, which was therefore assumed to contain major IgE epitopes of dog albumin. The deduced amino acid sequence of clone 54c was compared with the Swiss-Prot library, and significant sequence homologies were found with albumins from different species (human: 82.6%, pig: 81.8%, cattle: 77.3%, sheep: 78.8%, mouse: 75.8%, and rat: 76.2%). Several other IgE-positive clones hybridized with oligonucleotides that were prepared according to this sequence. Partial complementary DNA coding for dog albumin fragments may be considered a useful tool for further characterization of major IgE epitopes of dog albumin.

↩

[83] - Hilger C, Swiontek K, Hentges F, de Blay F, Pauli G. Cross-sensitization to hemoglobin in a case of respiratory allergy to pork and food allergy to chicken meat. 3rd International Symposium on Molecular Allergology, Salzburg, April 18-20, 2008, Poster n°48

↩

[84] - Sabbah A, Lauret MG, Chene J, Boutet S, Drouet M. Le syndrome porc-chat ou l'allergie croisée entre viande de porc et épithelia de chat. Allerg Immunol (Paris) 1994;26:173-177

Is there a port-cat syndrome in food allergy? Many clinical observations have revealed a frequent association between allergy to cat epithelia in subjects who have allergy to pork meat. This second part, from clinical tests such as skin tests and laboratory tests such as CAP RAST, electrophoresis, Western blot and chromatography, confirms the existence of a crossed reaction between pork meat and cat extract. This crossed reaction is linked with a common epitope. A common protein has been found that has a molecular weight of 67,000 d. for subjects who are sensitive to cat extracts and pork meat.

↩

[85] - Drouet M, Sabbah A. The pork/cat syndrome or crossed reactivity between cat epithelia and pork meat. Monogr Allergy 1996;32:164-173

↩

[86] - Drouet M, Lauret MG, Sabbah A. Le syndrome porc-chat: influence de la sensibilisation au chat sur celle de la viande de porc. Allerg Immunol (Paris) 1994;26:305-306

A patient who presented with exercise-induced anaphylaxis, linked with a food allergy to pork meat (VP), about three years ago became allergic to VP though effort was necessary to trigger the anaphylactic reactions. These disappeared after suppression of the VP allergy, but the IgE response to VP persisted until the cat was removed from the environment.

↩

[87] - Savi E, Rossi A, Incorvaia C. Cat-pork syndrome: a case report with a thee years follow-up. Eur Ann Allergy Clin Immunol 2006;38:366-368

A case of cat-pork syndrome with subsequent follow-up in a 17-year-old male patient is reported. At the initial observation, the patient was sensitized to cat epithelium--along with house dust mites and grass pollen--from two years. In 2001 he had an immediate reaction with urticaria, angioedema and dyspnea after eating grilled meat and sausage, and skin tests and CAP/RAST revealed a sensitization to pork meat, with a value of 4.7 KU/L for pork meat, and of 55 KU/L for cat epithelium. The patient was followed up for three years with annual repetition of diagnostic tests. The elimination of pork meat from the diet was incomplete, with slight skin reactions to small amounts of cooked pork meat but tolerance to seasoned pork products such as salami. A challenge test with pork meat in 2004 was positive, with angioedema and asthma symptoms, and CAP/RAST showed a value of 43 KU/L for cat epithelium and 4 KU/L for pork meat. RAST inhibition confirmed the significant cross-reactivity between the two allergen sources. These findings provide some knowledge on the natural history of the cat-pork syndrome, and confirm that very prolonged avoidance of the offending foods are needed to expect a loss of sensitization.

↩

[88] - Sabbah A, Lauret MG, Chene J, Boutet S, Drouet M. Le syndrome porc-chat ou l'allergie croisée entre viande de porc et épithelia de chat. Allerg Immunol (Paris) 1994;26:173-177

Is there a port-cat syndrome in food allergy? Many clinical observations have revealed a frequent association between allergy to cat epithelia in subjects who have allergy to pork meat. This second part, from clinical tests such as skin tests and laboratory tests such as CAP RAST, electrophoresis, Western blot and chromatography, confirms the existence of a crossed reaction between pork meat and cat extract. This crossed reaction is linked with a common epitope. A common protein has been found that has a molecular weight of 67,000 d. for subjects who are sensitive to cat extracts and pork meat.

↩

[89] - Hilger C, Kohnen M, Grigioni F, Lehners C, Hentges F. Allergic cross-reactions between cat and pig serum albumin. Study at the protein and DNA levels. Allergy 1997;52:179-187

After observing a patient allergic to cat dander and pork but devoid of other allergies, we prospectively screened patients known to be allergic to cat for a second sensitization to pork. After collecting the sera of 10 young patients found to contain specific IgE to cat dander and pork, we undertook this study to detect the possible cross-reactive allergen, define its molecular characteristics, and evaluate its clinical relevance. Through immunoblotting techniques, cat and porcine serum albumin were found to be jointly recognized molecules. These findings were further analyzed by specific anti-albumin IgE titrations and cross-inhibition experiments. Cat serum albumin cDNA was obtained from cat liver, and the corresponding amino acid sequence was deduced and compared to the known porcine and human serum albumin sequences. Inhibition experiments showed that the spectrum of IgE reactivity to cat serum albumin completely contained IgE reactivity to porcine serum albumin, suggesting that sensitization to cat was the primary event. In two cohorts of cat-allergic persons, the frequency of sensitization to cat serum albumin was found to lie between 14% and 23%. Sensitization to porcine albumin was found to lie between 3% and 10%. About 1/3 of these persons are likely to experience allergic symptoms in relation to pork consumption. Sensitization to cat serum albumin should be considered a useful marker of possible cross-sensitization not only to porcine serum albumin but also to other mammalian serum albumins.

↩

[90] - Hilger C, Swiontek K, Hentges F, de Blay F, Pauli G. Cross-sensitization to hemoglobin in a case of respiratory allergy to pork and food allergy to chicken meat. 3rd International Symposium on Molecular Allergology, Salzburg, April 18-20, 2008, Poster n°48

↩

[91] - Kanny G, De Hauteclocque C, Moneret-Vautrin DA. Food anaphylaxis to bovine serum albumin. J Allergy Clin Immunol 1998;101:137-139

↩

[92] - Palacios Benito R, Alvarez-Lovel MC, Martinez-Cocera C, Del Castillo Paya MM, Romanillos RA. Allergy to meat. Allergy 2002;57:858-859

↩

[93] - Hilger C, Kohnen M, Grigioni F, Lehners C, Hentges F. Allergic cross-reactions between cat and pig serum albumin. Study at the protein and DNA levels. Allergy 1997;52:179-187

After observing a patient allergic to cat dander and pork but devoid of other allergies, we prospectively screened patients known to be allergic to cat for a second sensitization to pork. After collecting the sera of 10 young patients found to contain specific IgE to cat dander and pork, we undertook this study to detect the possible cross-reactive allergen, define its molecular characteristics, and evaluate its clinical relevance. Through immunoblotting techniques, cat and porcine serum albumin were found to be jointly recognized molecules. These findings were further analyzed by specific anti-albumin IgE titrations and cross-inhibition experiments. Cat serum albumin cDNA was obtained from cat liver, and the corresponding amino acid sequence was deduced and compared to the known porcine and human serum albumin sequences. Inhibition experiments showed that the spectrum of IgE reactivity to cat serum albumin completely contained IgE reactivity to porcine serum albumin, suggesting that sensitization to cat was the primary event. In two cohorts of cat-allergic persons, the frequency of sensitization to cat serum albumin was found to lie between 14% and 23%. Sensitization to porcine albumin was found to lie between 3% and 10%. About 1/3 of these persons are likely to experience allergic symptoms in relation to pork consumption. Sensitization to cat serum albumin should be considered a useful marker of possible cross-sensitization not only to porcine serum albumin but also to other mammalian serum albumins.

↩

[94] - Palacios Benito R, Alvarez-Lovel MC, Martinez-Cocera C, Del Castillo Paya MM, Romanillos RA. Allergy to meat. Allergy 2002;57:858-859

↩

[95] - Gex-Collet CM, Huber C, Reimers A, Helbling A. Does the Pork-Cat Syndrome exist? EAACI 23th Congress, Amsterdam, 12-16 June, 2004, Poster n°1037

Background: The pork-cat syndrome has been described for the first time by a French group in 1994 postulating a cross-reactivity based on serum-albumin between cat and pork meat allergens. In the literature only few case-reports can be found. In the last 4 years 3 cat allergic subjects with immediate-type adverse reactions following ingestion of pork and cow meat referred for allergological evaluation have been recognized and assigned to this entity. Methods: History and allergological findings of the 3 identified cases will be presented. Results: In 2 out of 3 patients a positive skin prick test to pork meat, specific serum IgE to cat dander, pork and cat serum albumin have been demonstrated. In the third subject a positive skin prick test as well a serum specific IgE to cow meat have been found, but not to pork. Conclusion: So far the pork-cat syndrome rarely has been described, but it does exist. Since mammalian albumins are quite similar in composition, it is likely that the reactivity to the pork-albumin is due to a cross-reactive mechanism between the albumins. However, sensitization may have occurred by the inhalative way as it is suggested by the pre-existent respiratory allergy to cat.

↩

[96] - Savi E, Rossi A, Incorvaia C. Cat-pork syndrome: a case report with a thee years follow-up. Eur Ann Allergy Clin Immunol 2006;38:366-368

A case of cat-pork syndrome with subsequent follow-up in a 17-year-old male patient is reported. At the initial observation, the patient was sensitized to cat epithelium--along with house dust mites and grass pollen--from two years. In 2001 he had an immediate reaction with urticaria, angioedema and dyspnea after eating grilled meat and sausage, and skin tests and CAP/RAST revealed a sensitization to pork meat, with a value of 4.7 KU/L for pork meat, and of 55 KU/L for cat epithelium. The patient was followed up for three years with annual repetition of diagnostic tests. The elimination of pork meat from the diet was incomplete, with slight skin reactions to small amounts of cooked pork meat but tolerance to seasoned pork products such as salami. A challenge test with pork meat in 2004 was positive, with angioedema and asthma symptoms, and CAP/RAST showed a value of 43 KU/L for cat epithelium and 4 KU/L for pork meat. RAST inhibition confirmed the significant cross-reactivity between the two allergen sources. These findings provide some knowledge on the natural history of the cat-pork syndrome, and confirm that very prolonged avoidance of the offending foods are needed to expect a loss of sensitization.

↩

[97] - Drouet M, Sabbah A, Le Sellin J, Bonneau JC, Gay G, Dubois-Gosnet C. Anaphylaxie mortelle apres ingestion de sanglier chez un patient porteur du syndrome porc-chat. Allerg Immunol (Paris) 2001;33:163-165

Crossed allergy between pork and cat epithelia was described by us in 1994. It is due to serum albumin. Nowadays, other bio-chemical observations allow "completion" of the syndrome by extension of the crossed reactivity between other mammal meats and other epithelia of dog and horse. The authors report an observation of the pork-cat syndrome (developing in the form of anaphylaxis, and then ending in the death of the patient), following consumption of wild boar meat. Co-factors, such as effort, taking alcohol or hormonal condition may complicate the picture to make diagnosis more difficult.

↩

[98] - Hilger C, Kohnen M, Grigioni F, Lehners C, Hentges F. Allergic cross-reactions between cat and pig serum albumin. Study at the protein and DNA levels. Allergy 1997;52:179-187

After observing a patient allergic to cat dander and pork but devoid of other allergies, we prospectively screened patients known to be allergic to cat for a second sensitization to pork. After collecting the sera of 10 young patients found to contain specific IgE to cat dander and pork, we undertook this study to detect the possible cross-reactive allergen, define its molecular characteristics, and evaluate its clinical relevance. Through immunoblotting techniques, cat and porcine serum albumin were found to be jointly recognized molecules. These findings were further analyzed by specific anti-albumin IgE titrations and cross-inhibition experiments. Cat serum albumin cDNA was obtained from cat liver, and the corresponding amino acid sequence was deduced and compared to the known porcine and human serum albumin sequences. Inhibition experiments showed that the spectrum of IgE reactivity to cat serum albumin completely contained IgE reactivity to porcine serum albumin, suggesting that sensitization to cat was the primary event. In two cohorts of cat-allergic persons, the frequency of sensitization to cat serum albumin was found to lie between 14% and 23%. Sensitization to porcine albumin was found to lie between 3% and 10%. About 1/3 of these persons are likely to experience allergic symptoms in relation to pork consumption. Sensitization to cat serum albumin should be considered a useful marker of possible cross-sensitization not only to porcine serum albumin but also to other mammalian serum albumins.

↩

[99] - Donnay C, Barderas R, Kopferschmitt-Kubler MC, Pauli G, de Blay F. Sensitization to pig albumin and gamma-globulin responsible for occupational respiratory allergy. Allergy 2006;61:143-144

↩

[100] - Palacios Benito R, Alvarez-Lovel MC, Martinez-Cocera C, Del Castillo Paya MM, Romanillos RA. Allergy to meat. Allergy 2002;57:858-859

↩

[101] - Gex-Collet CM, Huber C, Reimers A, Helbling A. Does the Pork-Cat Syndrome exist? EAACI 23th Congress, Amsterdam, 12-16 June, 2004, Poster n°1037

Background: The pork-cat syndrome has been described for the first time by a French group in 1994 postulating a cross-reactivity based on serum-albumin between cat and pork meat allergens. In the literature only few case-reports can be found. In the last 4 years 3 cat allergic subjects with immediate-type adverse reactions following ingestion of pork and cow meat referred for allergological evaluation have been recognized and assigned to this entity. Methods: History and allergological findings of the 3 identified cases will be presented. Results: In 2 out of 3 patients a positive skin prick test to pork meat, specific serum IgE to cat dander, pork and cat serum albumin have been demonstrated. In the third subject a positive skin prick test as well a serum specific IgE to cow meat have been found, but not to pork. Conclusion: So far the pork-cat syndrome rarely has been described, but it does exist. Since mammalian albumins are quite similar in composition, it is likely that the reactivity to the pork-albumin is due to a cross-reactive mechanism between the albumins. However, sensitization may have occurred by the inhalative way as it is suggested by the pre-existent respiratory allergy to cat.

↩

[102] - Drouet M, Sabbah A, Le Sellin J, Bonneau JC, Gay G, Dubois-Gosnet C. Anaphylaxie mortelle apres ingestion de sanglier chez un patient porteur du syndrome porc-chat. Allerg Immunol (Paris) 2001;33:163-165

Crossed allergy between pork and cat epithelia was described by us in 1994. It is due to serum albumin. Nowadays, other bio-chemical observations allow "completion" of the syndrome by extension of the crossed reactivity between other mammal meats and other epithelia of dog and horse. The authors report an observation of the pork-cat syndrome (developing in the form of anaphylaxis, and then ending in the death of the patient), following consumption of wild boar meat. Co-factors, such as effort, taking alcohol or hormonal condition may complicate the picture to make diagnosis more difficult.

↩

[103] - Kanny G, De Hauteclocque C, Moneret-Vautrin DA. Food anaphylaxis to bovine serum albumin. J Allergy Clin Immunol 1998;101:137-139

↩

[104] - Cisteró-Bahíma A, Enrique E, San Miguel-Moncin MM, Alonso R, Bartra J, Fernandez-Parra B, et al. Meat allergy and cross-reactivity with hamster epithelium. Allergy 2003;58:161-162

↩

[105] - Drouet M, Lauret MG, Sabbah A. Le syndrome porc-chat: influence de la sensibilisation au chat sur celle de la viande de porc. Allerg Immunol (Paris) 1994;26:305-306

A patient who presented with exercise-induced anaphylaxis, linked with a food allergy to pork meat (VP), about three years ago became allergic to VP though effort was necessary to trigger the anaphylactic reactions. These disappeared after suppression of the VP allergy, but the IgE response to VP persisted until the cat was removed from the environment.

↩

[106] - Savi E, Rossi A, Incorvaia C. Cat-pork syndrome: a case report with a thee years follow-up. Eur Ann Allergy Clin Immunol 2006;38:366-368

A case of cat-pork syndrome with subsequent follow-up in a 17-year-old male patient is reported. At the initial observation, the patient was sensitized to cat epithelium--along with house dust mites and grass pollen--from two years. In 2001 he had an immediate reaction with urticaria, angioedema and dyspnea after eating grilled meat and sausage, and skin tests and CAP/RAST revealed a sensitization to pork meat, with a value of 4.7 KU/L for pork meat, and of 55 KU/L for cat epithelium. The patient was followed up for three years with annual repetition of diagnostic tests. The elimination of pork meat from the diet was incomplete, with slight skin reactions to small amounts of cooked pork meat but tolerance to seasoned pork products such as salami. A challenge test with pork meat in 2004 was positive, with angioedema and asthma symptoms, and CAP/RAST showed a value of 43 KU/L for cat epithelium and 4 KU/L for pork meat. RAST inhibition confirmed the significant cross-reactivity between the two allergen sources. These findings provide some knowledge on the natural history of the cat-pork syndrome, and confirm that very prolonged avoidance of the offending foods are needed to expect a loss of sensitization.

↩

[107] - Kanny G, De Hauteclocque C, Moneret-Vautrin DA. Food anaphylaxis to bovine serum albumin. J Allergy Clin Immunol 1998;101:137-139

↩

[108] - Hilger C, Kohnen M, Grigioni F, Lehners C, Hentges F. Allergic cross-reactions between cat and pig serum albumin. Study at the protein and DNA levels. Allergy 1997;52:179-187

After observing a patient allergic to cat dander and pork but devoid of other allergies, we prospectively screened patients known to be allergic to cat for a second sensitization to pork. After collecting the sera of 10 young patients found to contain specific IgE to cat dander and pork, we undertook this study to detect the possible cross-reactive allergen, define its molecular characteristics, and evaluate its clinical relevance. Through immunoblotting techniques, cat and porcine serum albumin were found to be jointly recognized molecules. These findings were further analyzed by specific anti-albumin IgE titrations and cross-inhibition experiments. Cat serum albumin cDNA was obtained from cat liver, and the corresponding amino acid sequence was deduced and compared to the known porcine and human serum albumin sequences. Inhibition experiments showed that the spectrum of IgE reactivity to cat serum albumin completely contained IgE reactivity to porcine serum albumin, suggesting that sensitization to cat was the primary event. In two cohorts of cat-allergic persons, the frequency of sensitization to cat serum albumin was found to lie between 14% and 23%. Sensitization to porcine albumin was found to lie between 3% and 10%. About 1/3 of these persons are likely to experience allergic symptoms in relation to pork consumption. Sensitization to cat serum albumin should be considered a useful marker of possible cross-sensitization not only to porcine serum albumin but also to other mammalian serum albumins.

↩

[109] - San-Juan S, Lezaun A, Caballero ML, Moneo I. Occupational allergy to raw beef due to cross-reactivity with dog epithelium. Allergy 2005;60:839-840

↩

[110] - Vicente-Serrano J, Caballero ML, Rodriguez-Pérez R, Carretero P, Pérez R, Blanco JG, et al. Sensitization to serum albumins in children allergic to cow’s milk and epithelia. Pediatr Allergy Immunol 2007;18:503-507

Patients with persistent milk allergy and specific immunoglobulin E (IgE) to bovine serum albumin (BSA) have a greater risk of rhinoconjunctivitis and asthma because of animal dander. To prove the cross-reactivity between serum albumin (SA) of different mammals in milk, meat, and epithelia and determine if heat treatment of meats decrease the allergenicity of albumins. The study was performed using SDS-PAGE and IgE-immunoblotting using sera from eight patients sensitized to milk, BSA, and animal danders. Sera from non-allergic and only animal dander allergic subjects served as a control. With one exception, all patients' sera recognized SA in different meats (beef, lamb, deer, and pork), epithelia (dog, cat, and cow), and cow's milk. Some patients even were only sensitized to SA in meat and epithelia. Danders' allergic only recognized other proteins in epithelia but not SA. No patients reacted to SA from heated meat extracts. Serum albumin is an important allergen involved in milk, meat, and epithelia allergy. The first contact with SA was through cow's milk and patients developed sensitization to epithelia SA even without direct contact with animals. Patients with both BSA and cow's milk allergy must avoid raw meats and furry pets.

↩

[111] - Hilger C, Kohnen M, Grigioni F, Lehners C, Hentges F. Allergic cross-reactions between cat and pig serum albumin. Study at the protein and DNA levels. Allergy 1997;52:179-187

After observing a patient allergic to cat dander and pork but devoid of other allergies, we prospectively screened patients known to be allergic to cat for a second sensitization to pork. After collecting the sera of 10 young patients found to contain specific IgE to cat dander and pork, we undertook this study to detect the possible cross-reactive allergen, define its molecular characteristics, and evaluate its clinical relevance. Through immunoblotting techniques, cat and porcine serum albumin were found to be jointly recognized molecules. These findings were further analyzed by specific anti-albumin IgE titrations and cross-inhibition experiments. Cat serum albumin cDNA was obtained from cat liver, and the corresponding amino acid sequence was deduced and compared to the known porcine and human serum albumin sequences. Inhibition experiments showed that the spectrum of IgE reactivity to cat serum albumin completely contained IgE reactivity to porcine serum albumin, suggesting that sensitization to cat was the primary event. In two cohorts of cat-allergic persons, the frequency of sensitization to cat serum albumin was found to lie between 14% and 23%. Sensitization to porcine albumin was found to lie between 3% and 10%. About 1/3 of these persons are likely to experience allergic symptoms in relation to pork consumption. Sensitization to cat serum albumin should be considered a useful marker of possible cross-sensitization not only to porcine serum albumin but also to other mammalian serum albumins.

↩

[112] - Goubran Botros H, Grégoire C, Rabillon J, David B, Dandeu JP. Cross-antigenicity of horse serum albumin with dog and cat albumins: study of three short peptides with significant inhibitory activity towards specific human IgE and IgG antibodies. Immunology 1996;88:340-347

Horse serum albumin is present in the near vicinity of the animal, while dog and cat serum albumins are very common allergens present in house dust. Human patients clinically defined as allergic to horse could react with horse serum albumin by means of IgE or IgG antibodies. Studies regarding the specificities of these antibodies by inhibition enzyme-linked immunosorbent assay (ELISA) and depletion experiments have demonstrated that they are directed against dog serum albumin and cross-react not only with horse serum albumin but with other serum albumins from different origins. To investigate these observations further, we isolated and characterized three tryptic peptides (P1, P2 and P3) from horse serum albumin. The peptide P1 contains loops 1 and 2 of the first domain, P2 is derived from loop 4 of the second domain, and P3 contains the disulphide loop 9 of the third domain. These were able to inhibit the binding of the patients' IgE and IgG antibodies to horse albumin as well as to dog and cat serum albumins. This indicates that these peptides are involved in the observed cross-reactions. They also shared common epitopes, as revealed by human IgE antibodies. After reduction and alkylation, they totally lost their inhibitory capacity, suggesting that the intra-chain disulphide bridges, essential for the preservation of the loop structure, probably maintain their allergenic/antigenic reactivity.

↩

[113] - Spitzauer S, Pandjaitan B, Soregi G, Muhl S, Ebner C, Kraft D, et al. IgE cross-reactivities against albumins in patients allergic to animals. J Allergy Clin Immunol 1995;96:951-959

Type I allergic symptoms and severe asthma in particular are frequently caused by animal hair/dander proteins, among which albumins are possible cross-sensitizing allergenic components. METHODS: The significance and degree of IgE-cross-reactivities against various albumins were studied in a representative number (n = 200) of patients allergic to animals with hair/dander extracts, purified albumins from different animals, and a recombinant dog albumin fragment expressed in lysogenic Escherichia coli Y1089 and purified as a beta-galactosidase fusion protein. RESULTS: Despite a high degree of sequence homology among different albumins, a remarkable variability of IgE cross-reactivities was observed, indicating that some patients were sensitized preferentially against certain albumins. Most of the patients allergic to albumins, however, reacted to dog, cat, and horse albumin, which also bound a high percentage of albumin-specific IgE. CONCLUSION: The purified recombinant dog albumin fragment, representing 265 amino acids of the mature protein, bound IgE from all 15 patients allergic to albumin tested suggesting its potential usefulness for diagnosis and perhaps therapy.

↩

[114] - Benito C, Fernandez-Rivas M. Combined respiratory and food allergies to rabbit. Allergy Clin Immunol Int 2005;17(Suppl. 1):361

Background. Exposure to rabbits as domestic pets or laboratory animals can induce respiratory allergy. Allergic reactions to the ingestion of rabbit meat in patients with respiratory allergy to rabbit has not been reported. Patients. Case 1. A 22 years-old woman reported since childhood rhinoconjunctivitis (RC) and asthma while playing with rabbits, and oropharyngeal itching (OAS) after eating rabbit meat. At 14 years of age she presented an anaphylaxis while playing volleyball one hour after having eaten rabbit. Case 2. A 10 years-old boy reported since the age of 6, several episodes of RC and asthma after exposure to rabbits. At the age of 7 he presented OAS while eating rabbit, immediately followed by RC and asthma, that required emergency room treatment. Both patients tolerated all foods of animal origin, including meats of other species. Patient 1 presented RC due to cat allergy. No other inhalant allergies where present in these 2 patients. Methods. Different rabbit extracts were prepared from epithelium, meat, serum, urine, and albumin, and used in skin prick tests (SPTs), ELISA-IgE, ELISAinhibition assays, and immunoblots. Results. Case 1: SPTs (wheal mm) epithelium 10, meat 5; ELISA (aKU/L) epithelium 56.73, meat 0.93, serum 0.56, urine 4.30, albumin 1.79. Case 2: SPTs epithelium 11, meat 4; ELISA epithelium 110.16, meat 1.11, serum 0.74, urine 5.81, albumin 1.34. The ELISA to rabbit meat was completely inhibited by rabbit epithelium, urine and albumin. The maximum inhibitions of the ELISA to rabbit epithelium by rabbit meat were below 44%, whereas the figures for rabbit urine were over 90%, and for rabbit albumin over 73%. Several allergens were identified in the immunoblots, but the most prominent ones were a band 60kDa (albumin) in epithelium, meat, serum and urine (cases 1,2), a band 42 kDa (probably actin) only observed in the meat (cases 1,2), a band 150 kDa (probably IgG) in epithelium, serum and urine (case 2), a band 17 kDa in epithelium (probably Ory c 1) (case 2). Conclusion. We present 2 cases of RC and asthma induced by inhaled exposure to rabbit who have subsequently developed severe reactions after the intake of rabbit meat. The reactivity to rabbit meat might result from sensitisation to rabbit allergens present in epitelium and urine by the inhalant route, together with a primary sensitisation to meat allergens (such as actin) through the oral route.

↩

[115] - Khadavi A, Silverman B, Schneider A. Inhaled rabbit allergy leading to ingestion induced anaphylaxis. Ann Allergy Asthma Immunol 2005;94:130

Rabbit anaphylaxis is extremely rare, with one documented case upon inhalation only. We describe a patient with severe anaphylaxis upon consumption of a rabbit. A 6-year-old female with a 3-year history of asthma and allergic rhinitis was presented for evaluation. The patient complained of worsening asthma and rhinitis symptoms in the home and upon exposure to outdoor pollen. Further history revealed the family had a rabbit as a pet. Laboratory testing showed her total IgE was 865 kU/L, RAST results were normal for tree, ragweed and molds (<0.35 kIU/L). Positive results were found for ragweed, dust, cockroach, cat, dog, mouse, peanut and rabbit epithelium (8.43 kIU/L, class IV). Among other environmental control measures, the family was advised to eliminate the rabbit from the home environment, as it could be a potential trigger for their daughters allergy symptoms. Two days later, the patient presented to the emergency room with wheezing, coughing and angioedema of the hands and face. She was treated with albuterol, diphenhydramine and oral steroids. The parents said they followed all of our instructions and did not know why anaphylaxis occurred. Further questioning revealed that the family consumed the pet rabbit on the same night preceding the anaphylactic reaction. This was the first time the daughter ate rabbit. The parents assumed that only exposure to the live rabbit would worsen her allergy and asthma symptoms, never expecting an allergic reaction via ingestion. They were advised not to feed their daughter rabbit again and were given a prescription for self-injectable epinephrine. This demonstrates either complete identity, partial similarity or cross reactivity between inhaled and food allergens, as has been noted previously with certain other foods such as garlic and crustacean proteins. Physicians need to advise food allergic patients that an allergic reaction can develop upon inhalation of the food, as seen with peanuts. But also respiratory sensitization to an allergen can lead to allergic symptoms upon its ingestion. to a lack of cross-reactivity between the two drugs. Although these findings suggest that oral celecoxib could be a possible safe alternative in patients with naproxen-induced drug reactions, it would be prudent to first conduct careful challenges with the drug in a well-equipped medical setting where clinical acceptability and tolerability could be safely assessed.

↩

[116] - Asero R, Mistrello G, Falagiani P. Oral allergy syndrome from pork. Allergy 1997;52:684-686

↩

[117] - Restani P, Ballabio C, Tripodi S, Fiocchi A. Meat allergy. Curr Opin Allergy Clin Immunol 2009;9:265-269

PURPOSE OF REVIEW: This review summarizes the scientific evidence on meat allergy, an unusual disorder, whose prevalence in some European countries (such as Italy) may be increasing. RECENT FINDINGS: Data reported in this review underline some interesting points: in meats rarely consumed, such as kangaroo, whale and seal, the main allergens are only partially correlated to those detected in beef or other usually consumed meats; cross-reactivity and cross-contamination are critical aspects, which should be seriously considered by allergologists. SUMMARY: Meat allergy is normally outgrown during the first years of life, so that it is rare in adults. Beef among mammals and chicken among birds are most frequently involved. The major allergens are serum albumins and immunoglobulins, but there are a few reports of allergies to muscle proteins (actin, myosin and tropomyosin). As meat allergenicity can be reduced by various treatments (heat, homogenization and freeze-drying), the consumption of meat derivatives by children allergic to meat proteins is often permitted. Cross-reactivity has been described between different meats, between meat and milk or eggs and between meat and animal dander. There are some reports of cross-contamination associated with the inadequate cleaning of industrial or butchers' equipment. All these aspects may have serious implications for clinical practice.

↩

[118] - Fuentes Aparicio V, Sanchez Marcen I, Perez Montero A, Baeza ML, de Barrio Fernandez M. Allergy to mammal's meat in adult life: immunologic and follow-up study. J Investig Allergol Clin Immunol 2005;15:228-231

Allergy to bovine meat and Bovine serum albumin (BSA) is exceptional, especially in the adult life. BSA is considered a minor allergen in cow's milk allergy, but there is little information about this antigen in reactions produced by other beef products as meat. To our knowledge, evolutive studies of beef's allergic patients have not been reported. OBJECTIVE: To present one patient with several allergic reactions (urticaria-angioedema) after eating different mammals' meat. METHODS: The patient underwent allergy testing through skin prick test (SPT), specific IgE detection and SDS-PAGE Immunoblotting and Immunodot inhibition studies. Periodic determinations of specific IgE to meats and epithelia were performed. RESULTS: Routine studies for chronic urticaria were normal or negative. SPT showed positive responses to pork, cow, rabbit and lamb meat, and dog, pork, sheep and cow epithelia. It was negative to cat, horse, guinea pig, rabbit, lamb, mouse epithelia, mixture of feathers, cow milk, soybean, mustard, mites and chicken meat and Anisakis simplex. Intradermal testing to BSA was positive. Determinations of specific IgE were positive to beef meat, lamb meat, pork meat and rabbit meat, dog, cat, cow, sheep and pork dander, cow's milk, and negative to chicken meat. Immunoblot and immunodot studies showed IgE recognition bands to bovine and lamb meat which were totally inhibited by BSA. A progressive reduction of the total and specific IgE, the latter until its total negativization, has been observed in the following three-year period. CONCLUSION: We report a case of IgE-mediated urticaria-angioedema due to BSA hypersensitivity, possibly induced by a subclinical sensitivity to dog and cat epithelium. The exclusion diet in patients allergic to these foods may be a progressive loss of clinical allergy.

↩

[119] - Perez A, Sanchez I, Vicente M, Baeza ML, Rodriguez JJ, Marañón F, et al. Allergy to mammal's meat. J Allergy Clin Immunol 2000;105(1 part 2):S139

↩

[120] - Cisteró-Bahíma A, Enrique E, San Miguel-Moncin MM, Alonso R, Bartra J, Fernandez-Parra B, et al. Meat allergy and cross-reactivity with hamster epithelium. Allergy 2003;58:161-162

↩

[121] - Rico-Diaz A, Diaz Roman T, Costa-Dominguez M, Ledesma A. Cow milk and meat allergy in a patient with allergy to hamster can be mediated by sera albumin. Allergy 2009;64(Suppl. 90):234-235

Background: Pork meat is a common food in diet but the allergy to this is rare. Much of the allergies to meat have been produced by primary sensitization to animal aeroallergens. Thus, in patients with pork meat allergy, the sensitization has been produced by cat antigen. Sera albumin is a putative cross reactive antigen in response. We ought to know allergy mechanism in a poly-sensitive patient with allergy to dust mites, animal epithelia and a late debut of cow milk allergy. Methods: A 10 years old female with diagnostic of dust mites and animals epithelia allergy undergoes eczema, rhinitis and asthma. She was living with cats, dogs, and hamster. Since she was 14 years old, she had abdominals pains, vomits, diarrhea, oral itch, rash and facial urticaria, immediately after the ingestions of lacteous derivates, or fresh sausages. Cooked meat was always well tolerated. Skin Prick tests to aeroallergens, to commercial food extract including cow milk and to different meats were made. Prick-prick with cooked and uncooked meat and specific IgE to animal allergens were also determined. Western Blot (WB) test. An extract of beef meat at 10% (p/v) in phosphate buffers was obtained, and conveniently stored at -20°C until use. Commercial extracts of hamster and cat epithelia, pork and beef meat, were employed in a non reduced SDS PAGE assay and transferred to nitrocellulose membrane. The patient's serum was incubated with the nitrocellulose strips to detect proteins with affinity to serum IgE. Also, the patient's serum was incubated with extract of hamster or cow epithelium in other strips in a blocking WB assay. Results: Prick test. D Pteronyssinus 10mm, Hamster 8mm, Cat 5mm, Dog 5mm, Cow milk (-), casein (-), BLG (-), ALA 4mm, BSA 4mm, histamine (8mm). Prick-Prick. Pork meat 11mm, cooked pork meat (-), Beef meat 3mm, cooked beef meat (-). IgE to hamster > 100 KU/ l; pork meat 9,2 KU/l; BSA 0,38KU/l. WB: Several bands were observed: A 60Kd band in blots with beef meat, pork meat and hamster epithelium, suggesting IgE recognizing sera albumin, a 19Kd band on cat epithelium (Fel d1) and 15Kd band on hamster epithelium. An evident reduction in 60Kd band intensity was observed following inhibition of patient serum with hamster extract in blocking WB. That diminution of band was observed in pork meat but not in beef meat blot. Conclusion: Our results suggest a food allergy to cow milk and pork meat proteins probably in relation to primary sensitization of hamster.

↩

[122] - Palacios Benito R, Alvarez-Lovel MC, Martinez-Cocera C, Del Castillo Paya MM, Romanillos RA. Allergy to meat. Allergy 2002;57:858-859

↩

[123] - Allergie à la viande de porc. Alim'Inter 2000;5(23):3-4

↩

[124] - Fuentes Aparicio V, Sanchez Marcen I, Perez Montero A, Baeza ML, de Barrio Fernandez M. Allergy to mammal's meat in adult life: immunologic and follow-up study. J Investig Allergol Clin Immunol 2005;15:228-231

Allergy to bovine meat and Bovine serum albumin (BSA) is exceptional, especially in the adult life. BSA is considered a minor allergen in cow's milk allergy, but there is little information about this antigen in reactions produced by other beef products as meat. To our knowledge, evolutive studies of beef's allergic patients have not been reported. OBJECTIVE: To present one patient with several allergic reactions (urticaria-angioedema) after eating different mammals' meat. METHODS: The patient underwent allergy testing through skin prick test (SPT), specific IgE detection and SDS-PAGE Immunoblotting and Immunodot inhibition studies. Periodic determinations of specific IgE to meats and epithelia were performed. RESULTS: Routine studies for chronic urticaria were normal or negative. SPT showed positive responses to pork, cow, rabbit and lamb meat, and dog, pork, sheep and cow epithelia. It was negative to cat, horse, guinea pig, rabbit, lamb, mouse epithelia, mixture of feathers, cow milk, soybean, mustard, mites and chicken meat and Anisakis simplex. Intradermal testing to BSA was positive. Determinations of specific IgE were positive to beef meat, lamb meat, pork meat and rabbit meat, dog, cat, cow, sheep and pork dander, cow's milk, and negative to chicken meat. Immunoblot and immunodot studies showed IgE recognition bands to bovine and lamb meat which were totally inhibited by BSA. A progressive reduction of the total and specific IgE, the latter until its total negativization, has been observed in the following three-year period. CONCLUSION: We report a case of IgE-mediated urticaria-angioedema due to BSA hypersensitivity, possibly induced by a subclinical sensitivity to dog and cat epithelium. The exclusion diet in patients allergic to these foods may be a progressive loss of clinical allergy.

↩

[125] - Ferrer A, Carnes J, Marco FM, Andreu C, Fernandez-Caldas E. Occupational allergic rhinoconjunctivitis and asthma to goat and cross-reactivity with cow epithelium. Ann Allergy Asthma Immunol 2006;96:579-585

BACKGROUND: The development of sensitization and symptoms after the inhalation of epithelial allergens is common. OBJECTIVES: To investigate the allergic response (in vivo and in vitro) of 3 individuals clinically sensitive and occupationally exposed to cow and goat and to evaluate the allergenic cross-reactivity between cow and goat epithelium extracts. METHODS: Three patients--a butcher and 2 doctors in veterinary medicine--were evaluated. These patients reported allergic respiratory symptoms after occupational exposure to goats and cows. Extracts were prepared from epithelia of both animals. All the patients underwent organ-specific allergen challenges with cow and goat extracts. Four nasal and 2 bronchial challenges were conducted following standardized procedures. RESULTS: All 3 patients had positive challenge results with the offending allergen extract. Specific IgE to goat allergens was detected in all patients. Several IgE-binding bands were detected. Inhibition assays (enzyme allergosorbent test and immunoblots) confirmed moderate-to-high cross-reactivity between goat and cow extracts. CONCLUSIONS: We confirm clinical sensitivity and specific IgE binding to goat and cow allergens in occupationally exposed individuals. There was good correlation among the clinical history, exposure, and the laboratory findings.

↩

[126] - Valero Santiago AL, Rosell Vives E, Lluch Perez M, Sancho Gomez J, Piulats Xanco J, Malet Casajuana A. Occupational allergy caused by cow dander: detection and identification of the allergenic fractions. Allergol Immunopathol (Madr) 1997;25:259-265

We describe two cases involving cow farmers, both males, one aged 28 and the other 45, who attended our center because his presented symptoms of rhinoconjunctivitis and asthma with 18 months and 4 year of evolution respectively, related to this laboral environment. The study included the following tests: skin tests (prick tests) to inhalant allergens (mites, pollens, moulds, dog and cat epithelium), foods, cow epithelium-dander, cow serum, beef and milk proteins. We determined the total seric IgE, specific IgE (RAST-CAP System) to cow meat and cow dander. Nasal provocation test with freeze-dried biological standardized extract of cow epithelium-dander were carried out. We observed the symptoms and realized control with a previous active computerized rhinomanometry. Cow dander proteins used for the provocation test were separated by means of SDS-PAGE or isoelectric focusing (IEF). The allergenic component were identified by immunoblotting with the patients' serum. The skin tests were positive to cow dander, and negative to the other allergens tested, including cow serum, cow milk and beef. The seric IgE were 383 and 477 kU/L, and the RAST was positive to cow dander, 20.10 and 36.4 kU/L (class 4). The provocation test were positive with a concentration of 500 SBU. We observed that the IgE of the two patients reacted with the same allergens: 3 major bands were identified with MW of 11, 15, 62.3 kDa. All these bands correspond to protein with acid pl.

↩

[127] - San-Juan S, Lezaun A, Caballero ML, Moneo I. Occupational allergy to raw beef due to cross-reactivity with dog epithelium. Allergy 2005;60:839-840

↩

[128] - Donnay C, Barderas R, Kopferschmitt-Kubler MC, Pauli G, de Blay F. Sensitization to pig albumin and gamma-globulin responsible for occupational respiratory allergy. Allergy 2006;61:143-144

↩

[129] - Hilger C, Swiontek K, Hentges F, de Blay F, Pauli G. Cross-sensitization to hemoglobin in a case of respiratory allergy to pork and food allergy to chicken meat. 3rd International Symposium on Molecular Allergology, Salzburg, April 18-20, 2008, Poster n°48

↩

[130] - Drouet M, Menehould C. Les composants mammifères dans les médicaments. Colloque SAICO, Angers, 29 juin 2006

↩

[131] - Fiocchi A, de Chiara A, Martelli A, Isoardi P, Bouygue GR, Terracciano L. Unnecessary elimination diets in children with cow's milk allergy. ACAAI Annual Meeting, San Antonio, 15-20 Nov. 2002, Poster n° 62

Many children with Cow‚s Milk Allergy (CMA) have been prescribed an elimination diet for beef and lactose besides cow‚s milk before being referred to an allergist. We assessed beef and lactose avoidance advice in children referred for CMA at this institution. Forty-eight infants and children (18 girls and 30 boys, median age 0.95 yrs, range 0.82-3.25) reported with CMA at this tertiary level institution were recruited on history of prescribed beef and lactose avoidance.A questionnaire was administered to their parents during the first visit. Specific information on prescription of lactose and/or beef avoidance and on prescribers (whether their GP, a paediatric allergist, or both) was recorded. Rates of prescribed avoidance diets and diagnosed allergy were compared using non-parametric methods and contingency tables for beef and lactose avoidance were used in the disciminant analysis. Tweny-five children were told to avoid beef, 16/25 by the GP and 9/25 by the paediatric allergist. Fifteen children were told to avoid lactose, 10/15 by the GP and 5/15 by the paediatric allergist. Median duration of avoidance diet before referral was 0.92 yrs. (range: 0.25-2.50)for beef and 1.25 yrs. (range: 0.58 - 3.25) for lactose. Beef avoidance was prescribed more often to younger children (P <0.05). Lactose avoidance was not correlated to age at diagnosis (P = n.s.). Parents who had been so adviced did check labels of drugs and foods for the presence of lactose as an excipient or ingredient. Four of them had even been warned to check for lactose in toothpaste. No challenge was carried out before referral. Only 6/25 of children avoidaning beef had been assessed for beef allergy at SPT and/or RAST, but none/15 for lactose. Children with suspected CMA are more often prescribed avoidance diets for beef and lactose than can be confirmed by challenge. Unwarranted restricted diets may be proloonged before allergist-made evaluation and sometimes without evaluation. Intelligent non-compliance has not been found, thus confirming the convincing power of elimination diet prescriptions over patients and their parents.

↩

[132] - Xinias I, Mavroudi A, Chatziagorou E, Kirvasilis F, Deligiannidis A, Papastavrou T. Prevalence of food allergy to beef in greek children with ige mediated allergy to cow’s milk. Allergy 2008;63(suppl. 88):643

Introduction: Reported incidence of cow‚s milk allergy is 2-5% of infants in Europe. The estimated prevalence of beef allergy among children who are cow‚s milk allergic is 13-20% worldwide. However, this prevalence in Greece has not been investigated. Aim and patiens: The aim of this study is to investigate the prevalence of beef allergy in children with known cow‚s milk allergy in Greece. Patients and methods: We investigated 51 children (27 boys, 24 girls) with IgE mediated cow‚s milk allergy. The diagnosis has been based on clinical and laboratory criteria (specific IgE, typical or atypical clinical manifestations of CMA). Total IgE was assessed, as well as specific IgE antibodies against bovine proteins was, by using the method of Unicap system (Diagnostic, Uppsala, Sweden). Symptoms and manifestations that might be related to beef allergy have also been reported. Results: Beef allergy has been diagnosed in 3 children (5.9%). The diagnosis was based on clinical criteria and was confirmed by the laboratory investigation. Total IgE in all children was fluctuating from 2 to 1000 iu/ mL and it was higher in children with multiple food allergies. From these 3 patients, one had multiple food allergy, whereas the other two had CMA and beef allergy. Total IgE in these three cases was:>1000, 161 and 274 iu/mL respectively. Conclusions: In Greek children with IgE mediated allergy to cow‚s milk, beef allergy seems to be less frequent compared to previous reports in other countries (5.9% vs. ~16% respectively, P<0.05). This could be attributed to the Greek habit of consuming well baked beef, in which the antigenicity of the bovine (beef) proteins is altered and therefore beef allergy is reduced.

↩

[133] - Eigenmann PA. Anaphylaxis to cow's milk and beef meat proteins. Ann Allergy Asthma Immunol 2002;89(6 Suppl. 1):61-64

OBJECTIVE: This report summarizes a review of anaphylactic reactions to cow's milk and beef presented at a recent conference on adverse reactions to bovine proteins. DATA SOURCES: A review of pertinent PubMed (National Library of Medicine) articles was performed. Relevant publications were critically analyzed. STUDY SELECTION: The expert opinion of the author was used to select the relevant data for the review. RESULTS: Although cow's milk has been recognized for many years as one of the leading causes of food allergy, beef has only recently been identified as a cause of immunoglobulin (Ig)E-mediated reactions. Epidemiologic data indicate that the prevalence of cow's milk allergy is approximately 1 to 2%, but no definite data are available for beef allergy. Anaphylaxis to both foods has been well characterized in childhood; however, a subset of adult patients may become reactive to cow's milk and have the characteristic features of anaphylaxis. The diagnosis is primarily based on skin prick tests and measurement of cow's milk- or beef-specific IgE antibodies. In selected patients, a standardized food challenge might be necessary to determine the diagnosis. CONCLUSIONS: In the absence of a proactive treatment of food allergy, patients with anaphylaxis to cow's milk or beef must be instructed to avoid these foods in their diet. Although cow's milk allergy generally is associated with a good prognosis, with most young children spontaneously "outgrowing" the disease, current research is focusing on the prevention and the treatment of this condition.

↩

[134] - Werfel SJ, Cooke SK, Sampson HA. Clinical reactivity to beef in children allergic to cow's milk. J Allergy Clin Immunol 1997;99:293-300

↩

[135] - Ayuso R, Lehrer SB, Lopez M, Reese G, Ibanez RM, Martin-Esteban M, et al. Identification of bovine IgG as a major cross-reactive vertebrate meat allergen. Allergy 2000;55:348-354

Although beef is a main source of protein in Western diets, very little has been published on allergic reactions to beef or the main allergens implicated in these reactions. The aim was to evaluate the IgE antibody response to beef in suspected meat-allergic subjects and assess cross-reactivity of beef with other vertebrate meats. METHODS: Fifty-seven sera from suspected meat-allergic subjects were tested by grid blot for specific IgE antibodies to vertebrate meats (beef, lamb, pork, venison, and chicken), and the patterns of recognition of meat proteins were assessed by immunoblot studies. RESULTS: A 160-kDa band, identified as bovine IgG, was detected in raw beef in 83% (10/12) of beef-allergic subjects but in only 24% of the beef-tolerant subjects. IgE reactivity to a band of similar mol. mass was detected also in lamb and venison, but rarely in pork or chicken. Complete inhibition of the IgE reactivity to the bovine IgG was obtained with lamb, venison, and milk. IgE reactivity to this band also completely disappeared when beef or lamb extracts were separated under reducing conditions, indicating conformational epitopes. CONCLUSIONS: Bovine IgG appears to be a major cross-reacting meat allergen that could predict beef allergy. Further studies with oral IgG challenges should be performed to document the conclusion that in vitro reactivity correlates with clinical hypersensitivity. The role of bovine IgG in other bovine products such as milk, dander, or hair must also be studied, and the hypothesis that it is a cross-reacting allergen with other mammalian products validated.

↩

[136] - Martelli A, De Chiara A, Corvo M, Restani P, Fiocchi A. Beef allergy in children with cow's milk allergy; cow's milk allergy in children with beef allergy. Ann Allergy Asthma Immunol 2002;89(6 Suppl. 1):38-43

OBJECTIVE: To review the literature on the prevalence of beef allergy in children allergic to cow's milk and to report a series of patients with beef allergy evaluated for cow's milk allergy. DATA SOURCES: A MEDLINE search for cow's milk allergy and beef allergy was conducted. Also included in this report is a clinical evaluation of both these entities in a population of children with atopic dermatitis. STUDY SELECTION: Data from the literature were summarized. Recruited patients with beef allergy were evaluated on the basis of history, serology, skin prick tests, and double-blind, placebo-controlled food challenge (entry criterion), and presented between 1992 and 2000. RESULTS: In the literature, between 13 and 20% of children with cow's milk allergy also have beef allergy. In our personal series of patients, 28 children (18 boys and 10 girls) diagnosed with beef allergy underwent skin prick tests and double-blind, placebo-controlled food challenge, which showed that 26 (92.9%) were allergic to cow's milk. Two children nonallergic to cow's milk were the only ones who were not sensitized to bovine serum albumin. CONCLUSIONS: Most children with beef allergy are also allergic to cow's milk and should avoid the consumption of dairy products. Sensitization to bovine serum albumin is a marker of cow's milk allergy in children with beef allergy. Elimination of beef from the diet of children with cow's milk allergy should be evaluated on an individual basis after diagnostic workup.

↩

[137] - Martelli A, De Chiara A, Corvo M, Restani P, Fiocchi A. Beef allergy in children with cow's milk allergy; cow's milk allergy in children with beef allergy. Ann Allergy Asthma Immunol 2002;89(6 Suppl. 1):38-43

OBJECTIVE: To review the literature on the prevalence of beef allergy in children allergic to cow's milk and to report a series of patients with beef allergy evaluated for cow's milk allergy. DATA SOURCES: A MEDLINE search for cow's milk allergy and beef allergy was conducted. Also included in this report is a clinical evaluation of both these entities in a population of children with atopic dermatitis. STUDY SELECTION: Data from the literature were summarized. Recruited patients with beef allergy were evaluated on the basis of history, serology, skin prick tests, and double-blind, placebo-controlled food challenge (entry criterion), and presented between 1992 and 2000. RESULTS: In the literature, between 13 and 20% of children with cow's milk allergy also have beef allergy. In our personal series of patients, 28 children (18 boys and 10 girls) diagnosed with beef allergy underwent skin prick tests and double-blind, placebo-controlled food challenge, which showed that 26 (92.9%) were allergic to cow's milk. Two children nonallergic to cow's milk were the only ones who were not sensitized to bovine serum albumin. CONCLUSIONS: Most children with beef allergy are also allergic to cow's milk and should avoid the consumption of dairy products. Sensitization to bovine serum albumin is a marker of cow's milk allergy in children with beef allergy. Elimination of beef from the diet of children with cow's milk allergy should be evaluated on an individual basis after diagnostic workup.

↩

[138] - Besler M, Fiocchi A, Restani P. Allergen Data Collection: Beef (Bos domesticus). Internet Symp Food Allergens 2001;3(4):171-184

↩

[139] - Vicente-Serrano J, Caballero ML, Rodriguez-Pérez R, Carretero P, Pérez R, Blanco JG, et al. Sensitization to serum albumins in children allergic to cow’s milk and epithelia. Pediatr Allergy Immunol 2007;18:503-507

Patients with persistent milk allergy and specific immunoglobulin E (IgE) to bovine serum albumin (BSA) have a greater risk of rhinoconjunctivitis and asthma because of animal dander. To prove the cross-reactivity between serum albumin (SA) of different mammals in milk, meat, and epithelia and determine if heat treatment of meats decrease the allergenicity of albumins. The study was performed using SDS-PAGE and IgE-immunoblotting using sera from eight patients sensitized to milk, BSA, and animal danders. Sera from non-allergic and only animal dander allergic subjects served as a control. With one exception, all patients' sera recognized SA in different meats (beef, lamb, deer, and pork), epithelia (dog, cat, and cow), and cow's milk. Some patients even were only sensitized to SA in meat and epithelia. Danders' allergic only recognized other proteins in epithelia but not SA. No patients reacted to SA from heated meat extracts. Serum albumin is an important allergen involved in milk, meat, and epithelia allergy. The first contact with SA was through cow's milk and patients developed sensitization to epithelia SA even without direct contact with animals. Patients with both BSA and cow's milk allergy must avoid raw meats and furry pets.

↩

[140] - Drouet M. Allergènes des viandes. Rev Fr Allergol 2009;49:160-165

L‚allergie aux viandes de vertébrés est passée en revue à partir des divers rapports et travaux de la littérature. Nous présentons les diverses allergies aux viandes et leurs particularités. Nous évoquons les allergies croisées démontrées ou simplement suspectées pour chacune d‚entre elles.

↩

[141] - Asero R, Mistrello G, Falagiani P. Oral allergy syndrome from pork. Allergy 1997;52:684-686

↩

[142] - Ayuso R, Lehrer SB, Tanaka L, Ibanez MD, Pascual C, Burks AW, et al. IgE antibody response to vertebrate meat proteins including tropomyosin. Ann Allergy Asthma Immunol 1999;83:399-405

Although meat is a main source of proteins in western diets, little information is available regarding allergy to vertebrate meats or the allergens implicated in these reactions. OBJECTIVE: To evaluate the in vitro IgE antibody response to different vertebrate meats in suspected meat-allergic subjects, as well as the possible role of tropomyosin in meat allergy and to analyze the cross-reactivity between vertebrate meats and the effect of heating on the IgE-binding to meat proteins. METHODS: Fifty-seven sera from suspected meat-allergic subjects were tested by grid blot to extracts of beef, lamb, pork, venison, chicken, and turkey and to four mammalian tropomyosins of different origins. RESULTS: Meat-allergic subjects have IgE antibodies to proteins in different mammalian meats (43/57 subjects); cross-reactivity with avian meat was limited: less than 50% (19/43) of meat positive sera reacted to chicken. In contrast, most of the poultry-positive sera also reacted to different mammalian meats. In general, there was stronger IgE reactivity to raw meats in comparison to cooked meats; an exception was six cases in which IgE reactivity to cooked poultry was stronger. Weak IgE reactivity to tropomyosin was detected in only 2/57 sera tested. CONCLUSIONS: Suspected meat-allergic subjects have serum IgE directed to meat proteins. In vitro cross-reactivity among mammalian meats appears to be important, while cross-reactivity to poultry is limited indicating mammalian-specific proteins. Although cooking in general denatures meat proteins rendering them less allergenic, in some cases the process of cooking may result in the formation of new allergenic moieties. The muscle protein tropomyosin is not an important vertebrate meat allergen.

↩

[143] - Fuentes MM, Palacios R, Garcés MM, Caballero ML, Moneo I. Isolation and characterization of a heat-resistant beef allergen: myoglobin. Allergy 2004;59:327-331

BACKGROUND: Meat allergy is rarely reported. Most of the described cases are sensitizations to bovine serum albumin . OBJECTIVE: The aim of the study was to describe a case of allergy to a new meat allergen and, after its characterization . METHODS: A 35-year-old nonatopic female with allergic episodes after ingestion of several types of meat was studied. Skin tests (prick and prick-to-prick); total and specific immunoglobulin E (IgE) determination; sodium dodecyl sulphate-polyacrylamide gel electrophoresis and specific IgE determination by immunoblotting under different conditions were performed. A 17-kDa allergen was semipurified by ethanol fractionation and its amino-terminal sequence was determined. The existence of specific IgE directed to this protein was studied by immunoblot in 80 atopic patients . RESULTS: The patient showed specific IgE antibodies to a 17-kDa protein. During the isolation of this allergen it was found that a 70-90% (vol/vol) ethanol concentration was able to purify the protein. The characterization revealed that it was a heat-resistant protein without disulfide bonds. N-terminal amino acid sequence (16 residues) showed identity with myoglobin. The study of specific IgE to this allergen among atopic patients showed that it was recognized by about 1% of the subjects . CONCLUSIONS: We describe a case of meat allergy caused by myoglobin. This is the first described case of monosensitization to this protein.

↩

[144] - Benito C, Fernandez-Rivas M. Combined respiratory and food allergies to rabbit. Allergy Clin Immunol Int 2005;17(Suppl. 1):361

Background. Exposure to rabbits as domestic pets or laboratory animals can induce respiratory allergy. Allergic reactions to the ingestion of rabbit meat in patients with respiratory allergy to rabbit has not been reported. Patients. Case 1. A 22 years-old woman reported since childhood rhinoconjunctivitis (RC) and asthma while playing with rabbits, and oropharyngeal itching (OAS) after eating rabbit meat. At 14 years of age she presented an anaphylaxis while playing volleyball one hour after having eaten rabbit. Case 2. A 10 years-old boy reported since the age of 6, several episodes of RC and asthma after exposure to rabbits. At the age of 7 he presented OAS while eating rabbit, immediately followed by RC and asthma, that required emergency room treatment. Both patients tolerated all foods of animal origin, including meats of other species. Patient 1 presented RC due to cat allergy. No other inhalant allergies where present in these 2 patients. Methods. Different rabbit extracts were prepared from epithelium, meat, serum, urine, and albumin, and used in skin prick tests (SPTs), ELISA-IgE, ELISAinhibition assays, and immunoblots. Results. Case 1: SPTs (wheal mm) epithelium 10, meat 5; ELISA (aKU/L) epithelium 56.73, meat 0.93, serum 0.56, urine 4.30, albumin 1.79. Case 2: SPTs epithelium 11, meat 4; ELISA epithelium 110.16, meat 1.11, serum 0.74, urine 5.81, albumin 1.34. The ELISA to rabbit meat was completely inhibited by rabbit epithelium, urine and albumin. The maximum inhibitions of the ELISA to rabbit epithelium by rabbit meat were below 44%, whereas the figures for rabbit urine were over 90%, and for rabbit albumin over 73%. Several allergens were identified in the immunoblots, but the most prominent ones were a band 60kDa (albumin) in epithelium, meat, serum and urine (cases 1,2), a band 42 kDa (probably actin) only observed in the meat (cases 1,2), a band 150 kDa (probably IgG) in epithelium, serum and urine (case 2), a band 17 kDa in epithelium (probably Ory c 1) (case 2). Conclusion. We present 2 cases of RC and asthma induced by inhaled exposure to rabbit who have subsequently developed severe reactions after the intake of rabbit meat. The reactivity to rabbit meat might result from sensitisation to rabbit allergens present in epitelium and urine by the inhalant route, together with a primary sensitisation to meat allergens (such as actin) through the oral route.

↩

[145] - Welt K, Hinrichs R, Ott S, Thalmann M, Dieckmännken J, Schneider LA, et al. Anaphylaxis after the ingestion of lamb meat. Allergy 2005;60:545

↩

[146] - Bourne HC, Restani P, Moutzouris M, Katelaris CH. An unusual pattern of meat allergy. Allergy 2005;60:706-707

↩

[147] - Fuentes Aparicio V, Sanchez Marcen I, Perez Montero A, Baeza ML, de Barrio Fernandez M. Allergy to mammal's meat in adult life: immunologic and follow-up study. J Investig Allergol Clin Immunol 2005;15:228-231

Allergy to bovine meat and Bovine serum albumin (BSA) is exceptional, especially in the adult life. BSA is considered a minor allergen in cow's milk allergy, but there is little information about this antigen in reactions produced by other beef products as meat. To our knowledge, evolutive studies of beef's allergic patients have not been reported. OBJECTIVE: To present one patient with several allergic reactions (urticaria-angioedema) after eating different mammals' meat. METHODS: The patient underwent allergy testing through skin prick test (SPT), specific IgE detection and SDS-PAGE Immunoblotting and Immunodot inhibition studies. Periodic determinations of specific IgE to meats and epithelia were performed. RESULTS: Routine studies for chronic urticaria were normal or negative. SPT showed positive responses to pork, cow, rabbit and lamb meat, and dog, pork, sheep and cow epithelia. It was negative to cat, horse, guinea pig, rabbit, lamb, mouse epithelia, mixture of feathers, cow milk, soybean, mustard, mites and chicken meat and Anisakis simplex. Intradermal testing to BSA was positive. Determinations of specific IgE were positive to beef meat, lamb meat, pork meat and rabbit meat, dog, cat, cow, sheep and pork dander, cow's milk, and negative to chicken meat. Immunoblot and immunodot studies showed IgE recognition bands to bovine and lamb meat which were totally inhibited by BSA. A progressive reduction of the total and specific IgE, the latter until its total negativization, has been observed in the following three-year period. CONCLUSION: We report a case of IgE-mediated urticaria-angioedema due to BSA hypersensitivity, possibly induced by a subclinical sensitivity to dog and cat epithelium. The exclusion diet in patients allergic to these foods may be a progressive loss of clinical allergy.

↩

[148] - Perez A, Sanchez I, Vicente M, Baeza ML, Rodriguez JJ, Marañón F, et al. Allergy to mammal's meat. J Allergy Clin Immunol 2000;105(1 part 2):S139

↩

[149] - Touraine F, Principaud Perrier M, Brianchon C, Sagot L, Boumediene A, Sainte Laudy J, et al. Particularités de l'allergie alimentaire au porc. Rev Fr Allergol Immunol Clin 2006;46:388-391

L'allergie alimentaire au porc est rare. Cependant, nous en rapportons 13 cas, concernant surtout l'allergie aux rognons. Les réactions peuvent être sévères. Les sensibilisations croisées sont nombreuses avec d'autres mammifères. Une meilleure connaissance des allergènes en cause est nécessaire pour mieux identifier les risques chez ces patients.

↩

[150] - Vereda A, Cuesta J, Barderas M, de la Cuesta F, Pastor C, Vivanco F, et al. Beef allergy. EAACI 25th Congress, Vienna, 10-14 June, 2006, Poster n°1529

Background: Although beef meat is widely consumed in Western diets, beef allergy is rarely reported. The aim of the study was to describe a case of beef allergy and to identify the allergens. Method:A 16-month-old male, with atopic dermatitis and several food allergies (egg, fish and legumes), was studied. At the age of 7 months, he suffered labial angioedema and perioral erythema after the ingestion of scarcely cooked beef. He tolerated well done beef, as well as other meats and cow's milk. Skin tests, oral challenge and specific IgE determination were performed. Meat allergens were studied by SDS-PAGE, IgE-immunoblotting, inhibition assays and mass spectrometry. Results: Prick tests were positive to egg, fish, legumes, bovine serum albumin (BSA),bovine gamma globulin (BGG) and cow epithelium, and negative to the remaining milk proteins. Prick-prick tests were positive to raw and cooked beef, pork and lamb, and negative to chicken meat. Oral challenge test with raw beef meat elicited a positive response, with perioral wheals and erithema, and labial angioedema. However, the oral challenge was negative with cooked beef. Specific IgE was positive to BSA, cow's epithelium and milk, beef, pork and lamb meat. SDS-PAGE and immunoblotting with the beef extract revealed some prominent IgE-binding protein bands at >130, 67, 60 and 25 kDa, which were common to other meats (pork, rabbit, lamb), as well as to cow's epithelium and milk. IgE binding was decreased by heating the beef meat extract. Inhibition assays demonstrated cross-reactivity among the different meats, mainly between beef and lamb. BSA, b-enolase and creatin kinase were identified by mass spectrometry as allergens in the beef meat extract. Conclusions: We present a child with beef allergy, also sensitized to cow‚s milk and other meats. The responsible allergens are heat-labile, and could correspond to BSA and IGG. We also identified two proteins (b-enolase and creatin kinase), which have not been previously described as allergens.

↩

[151] - Palacios Benito R, Alvarez-Lovel MC, Martinez-Cocera C, Del Castillo Paya MM, Romanillos RA. Allergy to meat. Allergy 2002;57:858-859

↩

[152] - Pétrus M, Rival L, Abbal M. Une observation très particulière d'intolérance aux viandes de bœuf, de poulet, de porc, chez un nourrisson de 10 mois. Rev Fr Allergol Immunol Clin 2004;44:407-410

Les auteurs rapportent l'observation d'un nourrisson de dix mois, présentant des réactions d'intolérance digestive (vomissements, diarrhée), dans les deux heures suivant l'absorption de viande de poulet, de boeuf ou de porc. Les prick-tests, les tests natifs, labiaux, les IgE spécifiques étaient négatifs. Les patch-tests, lus à 24 et 72 heures, le test de transformation blastique, le test d'histaminolibération sont positifs. Le test de provocation oral à la viande de poulet reproduit la symptomatologie après absorption de 13 grammes de viande. L'oeuf de poule, le lait de vache et le poisson sont bien supportés. La suppression des viandes incriminées permet la guérison des symptômes. Les auteurs évoquent un mécanisme non IgE-dépendant.

↩

[153] - Guerrier G, Noiret A, Bellon G. Viande de boeuf ou lait de vache, même prudence: sensibilisation possible à la sérumalbumine bovine chez deux enfants. Rev Fr Allergol Immunol Clin 2001;41:396-400

Les auteurs rapportent deux observations de sensibilisation possible à la sérumalbumine bovine chez des enfants âgés de cinq et quatre ans. Celle-ci est associée à une intolérance au lait de vache (oedème des paupières et douleurs abdominales) chez le premier, à une intolérance à la viande de boeuf peu cuite chez le second (urticaire généralisée et oedème de la face). Les profils biologiques des deux enfants sont identiques, caractérisés par la présence d'IgE spécifiques vis-à-vis du lait de vache total, de la viande de boeuf et de la sérumalbumine bovine. Il n'existe pas d'IgE spécifiques dirigées contre les fractions « classiques » du lait de vache, alpha-lactalbumine, bêta-lactoglobuline et caséine. Chez les deux sujets, les prick-tests sont négatifs pour le lait et ses fractions. Le prick-test est positif pour la viande de boeuf uniquement chez l'enfant intolérant à cet aliment. Il est difficile d'expliquer cette dissociation séméiologique en présence d'une vraisemblable sensibilisation commune à la sérumalbumine bovine. La sensibilisation à la sérumalbumine bovine est rare, surtout quand elle est isolée et, en pratique, il faut s'assurer que la recherche d'IgE vis-à-vis du lait total (Rast) comporte bien, entre autres, celle d'IgE spécifiques vis-à-vis de cette protéine. Elle explique chez nos deux sujets la positivité du Rast à la fois au lait de vache total et à la viande de boeuf, mais l'exclusion d'un seul de ces deux aliments est justifiée chez chacun deux.

↩

[154] - Fiocchi A, De Chiara A, Isoardi P, Terracciano L, Bouygue GR, Arrigoni S. The need for beef challenges in children with adverse reactions to bovine proteins (ARBP). EAACI 22th Congress, Paris, 7-11 June, 2003, Poster n°621

Background: Children with cow's milk allergy (CMA) are often put on a permanent avoidance diet for beef until many outgrow their CMA in their third year or later. We prospectively enrolled patients who reported for assessment of CMA inclusive of double blind, placebo-controlled food challenge (DBPCFC) and compared outcomes with age above or under three years to attempt answering the question: "Is a DBPCFC needed to assess beef allergy (BA) in children with CMA?" Methods: 23 patients (9 females, 14 males, age range 0.66 to 12.16, median 3.59 years) with CMA underwent DBPCFC with cow's milk and beef (outcome measures) between 1st November 2000 and 30th January 2003. In this small sample, the chi-square test of the dependency of age under or above three years was considered to answer the research question ( = 0.05; v = 2). A 2x3 setup was used to compare expected (in 0,000) and observed frequencies using age (>3y) at DBPCFC with beef as the two rank categories and CMA, beef allergy or both conditions as column variables. RESULTS: Out of 46 DBPCFC procedures, 23 were carried out with cow's milk (23+) and 23 with beef (6+). The critical value of the chi-square distribution is chi-square0.05 = 5.991 and the chi-square test for the dependency of age <3y and positive DBPCFC is 40.386 and thus supports the research question in this sample. The relationship was strongest (more than three times the expected frequencies) with age <3y and DBPCFC with beef or with both beef and cow's milk, with the observed frequencies for DBPCFC with cow's milk more than twice the expected outcome. The relationship between age >3y and positive DBPCFC with beef was the least strong (by 3 orders of magnitude), indicating that children outgrow beef allergy even when CMA persists. CONCLUSIONS: The data suggest a DBPCFC with beef in children with CMA <3y is clinically supported. DBPCFC under the supervision of a paediatric allergist in a hospital setting, ideally after an elimination diet, maybe easier to carry out before issues the introduction of domestically cooked beef. At issue is not merely the ARBP workup but nutritional and management questions that suggest qualitative improvements.

↩

[155] - Martelli A, De Chiara A, Corvo M, Restani P, Fiocchi A. Beef allergy in children with cow's milk allergy; cow's milk allergy in children with beef allergy. Ann Allergy Asthma Immunol 2002;89(6 Suppl. 1):38-43

OBJECTIVE: To review the literature on the prevalence of beef allergy in children allergic to cow's milk and to report a series of patients with beef allergy evaluated for cow's milk allergy. DATA SOURCES: A MEDLINE search for cow's milk allergy and beef allergy was conducted. Also included in this report is a clinical evaluation of both these entities in a population of children with atopic dermatitis. STUDY SELECTION: Data from the literature were summarized. Recruited patients with beef allergy were evaluated on the basis of history, serology, skin prick tests, and double-blind, placebo-controlled food challenge (entry criterion), and presented between 1992 and 2000. RESULTS: In the literature, between 13 and 20% of children with cow's milk allergy also have beef allergy. In our personal series of patients, 28 children (18 boys and 10 girls) diagnosed with beef allergy underwent skin prick tests and double-blind, placebo-controlled food challenge, which showed that 26 (92.9%) were allergic to cow's milk. Two children nonallergic to cow's milk were the only ones who were not sensitized to bovine serum albumin. CONCLUSIONS: Most children with beef allergy are also allergic to cow's milk and should avoid the consumption of dairy products. Sensitization to bovine serum albumin is a marker of cow's milk allergy in children with beef allergy. Elimination of beef from the diet of children with cow's milk allergy should be evaluated on an individual basis after diagnostic workup.

↩

[156] - Werfel SJ, Cooke SK, Sampson HA. Clinical reactivity to beef in children allergic to cow's milk. J Allergy Clin Immunol 1997;99:293-300

↩

[157] - Kanny G, De Hauteclocque C, Moneret-Vautrin DA. Food anaphylaxis to bovine serum albumin. J Allergy Clin Immunol 1998;101:137-139

↩

[158] - Vereda A, Cuesta J, Barderas M, de la Cuesta F, Pastor C, Vivanco F, et al. Beef allergy. EAACI 25th Congress, Vienna, 10-14 June, 2006, Poster n°1529

Background: Although beef meat is widely consumed in Western diets, beef allergy is rarely reported. The aim of the study was to describe a case of beef allergy and to identify the allergens. Method:A 16-month-old male, with atopic dermatitis and several food allergies (egg, fish and legumes), was studied. At the age of 7 months, he suffered labial angioedema and perioral erythema after the ingestion of scarcely cooked beef. He tolerated well done beef, as well as other meats and cow's milk. Skin tests, oral challenge and specific IgE determination were performed. Meat allergens were studied by SDS-PAGE, IgE-immunoblotting, inhibition assays and mass spectrometry. Results: Prick tests were positive to egg, fish, legumes, bovine serum albumin (BSA),bovine gamma globulin (BGG) and cow epithelium, and negative to the remaining milk proteins. Prick-prick tests were positive to raw and cooked beef, pork and lamb, and negative to chicken meat. Oral challenge test with raw beef meat elicited a positive response, with perioral wheals and erithema, and labial angioedema. However, the oral challenge was negative with cooked beef. Specific IgE was positive to BSA, cow's epithelium and milk, beef, pork and lamb meat. SDS-PAGE and immunoblotting with the beef extract revealed some prominent IgE-binding protein bands at >130, 67, 60 and 25 kDa, which were common to other meats (pork, rabbit, lamb), as well as to cow's epithelium and milk. IgE binding was decreased by heating the beef meat extract. Inhibition assays demonstrated cross-reactivity among the different meats, mainly between beef and lamb. BSA, b-enolase and creatin kinase were identified by mass spectrometry as allergens in the beef meat extract. Conclusions: We present a child with beef allergy, also sensitized to cow‚s milk and other meats. The responsible allergens are heat-labile, and could correspond to BSA and IGG. We also identified two proteins (b-enolase and creatin kinase), which have not been previously described as allergens.

↩

[159] - Fiocchi A, De Chiara A, Isoardi P, Terracciano L, Bouygue GR, Arrigoni S. The need for beef challenges in children with adverse reactions to bovine proteins (ARBP). EAACI 22th Congress, Paris, 7-11 June, 2003, Poster n°621

Background: Children with cow's milk allergy (CMA) are often put on a permanent avoidance diet for beef until many outgrow their CMA in their third year or later. We prospectively enrolled patients who reported for assessment of CMA inclusive of double blind, placebo-controlled food challenge (DBPCFC) and compared outcomes with age above or under three years to attempt answering the question: "Is a DBPCFC needed to assess beef allergy (BA) in children with CMA?" Methods: 23 patients (9 females, 14 males, age range 0.66 to 12.16, median 3.59 years) with CMA underwent DBPCFC with cow's milk and beef (outcome measures) between 1st November 2000 and 30th January 2003. In this small sample, the chi-square test of the dependency of age under or above three years was considered to answer the research question ( = 0.05; v = 2). A 2x3 setup was used to compare expected (in 0,000) and observed frequencies using age (>3y) at DBPCFC with beef as the two rank categories and CMA, beef allergy or both conditions as column variables. RESULTS: Out of 46 DBPCFC procedures, 23 were carried out with cow's milk (23+) and 23 with beef (6+). The critical value of the chi-square distribution is chi-square0.05 = 5.991 and the chi-square test for the dependency of age <3y and positive DBPCFC is 40.386 and thus supports the research question in this sample. The relationship was strongest (more than three times the expected frequencies) with age <3y and DBPCFC with beef or with both beef and cow's milk, with the observed frequencies for DBPCFC with cow's milk more than twice the expected outcome. The relationship between age >3y and positive DBPCFC with beef was the least strong (by 3 orders of magnitude), indicating that children outgrow beef allergy even when CMA persists. CONCLUSIONS: The data suggest a DBPCFC with beef in children with CMA <3y is clinically supported. DBPCFC under the supervision of a paediatric allergist in a hospital setting, ideally after an elimination diet, maybe easier to carry out before issues the introduction of domestically cooked beef. At issue is not merely the ARBP workup but nutritional and management questions that suggest qualitative improvements.

↩

[160] - Fiocchi A, Restani P, Bouygue GR, Martelli A. Beef allergy in adults and children. Allergy 2005;60:126

↩

[161] - Martinez Alonso JC, Dominguez Ortega FJ, Fuentes Gonzalo MJ. Angioedema por sensibilización a carne de gallina. Allergol Immunopathol (Madr) 2003;31:50-52

BACKGROUND: Egg is the most frequent cause of food allergy in children. The bird-egg syndrome, found in a group of patients sensitized to egg through bird proteins, was infrequent in children. We report a patient with former history of hypersensitivity to egg who developed episodes of angioedema after ingestion of hen meat. METHODS: Prick testing with egg and their different antigenic protein fractions, alpha-livetin and chicken meat was performed. Antigens of hen meat were used for the skin prick test and prick-by-prick. Serum-specific IgE was identified with use of the CAP techniques and SDS-PAGE Immunoblotting. RESULTS: Prick test was positive with egg yolk, alpha-livetin and chicken meat. A prick-by-prick test with hen meat resulted positive in our patient, but the same test in four controls patients were negative. Serum specific IgE was positive for egg yolk and hen meat. CONCLUSION: Allergy reactions to hen meat are exceptional. We report a case of children with allergy to egg proteins and hen meat that suggest an IgE mediated hypersensitivity reaction. Skin test reveal sensitivity to egg yolk and alpha-livetin, but this pattern of sensitization was infrequent in children.

↩

[162] - Kanny G. Allergie à la viande de dinde. Alim'Inter 1997;2(7):14

↩

[163] - Escudero C, Cuesta J, Bartolomé B, de Miguel J, Compés E, de las Heras M, et al. Avian meat as a hidden allergen: double blind, placebo controlled, oral challenge study. EAACI 22th Congress, Paris, 7-11 June, 2003, Poster n°139

Chicken meat is a fundamental food in our diets. However, the food allergy to this food has been scantly documented and generally, into the context of the „bird-egg syndrome‰. Case report: 22-year-old man without personal history of atopy and family history of hay fever. He was refereed oral syndrome after the ingestion of frankfurter and foie gras that contains small amounts of avian meats. Moreover, he experienced oral syndrome, nausea, vomits and abdominal pain immediately after the ingestion of cooked chicken meat. He developed similar symptoms after the ingestion of turkey, duck, quail, partridge and pheasant meats. He could eat egg and mammalian meats, and he hadn‚t exposed to birds. He experiences oral itching after the ingestion of chickpea, kidney bean and lentil. The causative role of avian meats in the anaphylactic response of the patient was investigated by immunologic and double blind, placebo controlled, oral challenge tests (DBPCOC). Skin prick tests (SPT) were performed with a panel of foods. We obtained positive responses with chicken meat. SPT with raw chicken and turkey meats, performed by the prick-prick method, were positive. SPT with egg (egg white, egg yolk, ovalbumin, ovomucoid, conalbumin, and lysozyme), chicken albumin and feathers mixture were negative. Specific IgE were determined by CAP System (Pharmacia, Sweden). Specific IgE determinations to avian meats were positive (chicken 2.95; turkey 0.96 kU/L). Oral challenge with frankfurter that contains chicken meat was positive. DBPCOC with an accumulative dose of 3 gr. of chicken meat reproduced the symptoms. Placebo was prepared with green vegetable puree and cooked cow meat. Conclusion: Small amounts of poultry meat may be present in frankfurters and other foodstuffs and cause anaphylactic reactions in sensitised patients. We could demonstrate by means of skin tests, IgE determinations and DBPCOC that chicken meat caused anaphylaxis in the patient through an IgE-dependent mechanism. Crossreactive among various avian meats is clinically suggestive.

↩

[164] - Halloy JL. Allergie aux viandes d'oiseaux. Alim'Inter 2005;10:289-291

↩

[165] - Fontaine JF, Lavaud F, Sabouraud-Leclerc D, Perdu D, Prévost A. Allergie alimentaire à la viande de poulet et de dinde: à propos de 2 observations. Rev Fr Allergol Immunol Clin 1997;37:397

↩

[166] - Cahen YD, Fritsch R, Wüthrich B. Food allergy with monovalent sensitivity to poultry meat. Clin Exp Allergy 1998;28:1026-1030

BACKGROUND: Allergy to poultry meat is only rarely covered in science. The few reports are usually related to patients allergic to eggs or bird feathers. OBJECTIVE: Two patients with a clear history of monovalent, ingestive allergy to chicken and turkey meat, without other food allergies, were analysed. The relevant allergens were to be identified by immunoblotting. METHODS: Both patients were evaluated with skin tests and specific IgE determination (CAP). Allergens were identified by SDS-PAGE and immunoblotting. Cross-reactivity of chicken and turkey meat was examined by IgE inhibition experiments. RESULTS: Skin tests and specific IgE were positive for chicken and turkey in both patients. Cross-reactivities to other poultry meats were documented for duck and goose meat. No sensitization to egg components or poultry feathers could be found. Allergenic proteins of poultry meat were detected at molecular weights of 21, 23 and 50 kDa (distinct bands) and 13, 27 and 33kDa (faint bands). An additional band at 91 kDa for turkey, can probably not be considered a distinct allergenic epitope. Immunoblot inhibition confirmed cross-reactivity of chicken and turkey meat allergens. CONCLUSION: Food allergy to poultry meat is a distinct disorder with crossreactivity among chicken, turkey and other poultries. The relevant allergens were identified by immunoblotting. Associated food allergy to egg-components is unlikely as the patients were able to tolerate egg and eggs products.

↩

[167] - Liccardi G, Szepfalusi Z, Noschese P, D'Amato M. The significance of chicken meat allergy without sensitization to egg proteins. Ann Allergy Asthma Immunol 2000;85:84

↩

[168] - Martinez Alonso JC, Dominguez Ortega FJ, Fuentes Gonzalo MJ. Angioedema por sensibilización a carne de gallina. Allergol Immunopathol (Madr) 2003;31:50-52

BACKGROUND: Egg is the most frequent cause of food allergy in children. The bird-egg syndrome, found in a group of patients sensitized to egg through bird proteins, was infrequent in children. We report a patient with former history of hypersensitivity to egg who developed episodes of angioedema after ingestion of hen meat. METHODS: Prick testing with egg and their different antigenic protein fractions, alpha-livetin and chicken meat was performed. Antigens of hen meat were used for the skin prick test and prick-by-prick. Serum-specific IgE was identified with use of the CAP techniques and SDS-PAGE Immunoblotting. RESULTS: Prick test was positive with egg yolk, alpha-livetin and chicken meat. A prick-by-prick test with hen meat resulted positive in our patient, but the same test in four controls patients were negative. Serum specific IgE was positive for egg yolk and hen meat. CONCLUSION: Allergy reactions to hen meat are exceptional. We report a case of children with allergy to egg proteins and hen meat that suggest an IgE mediated hypersensitivity reaction. Skin test reveal sensitivity to egg yolk and alpha-livetin, but this pattern of sensitization was infrequent in children.

↩

[169] - Sokolova A, Costa AC, Santos MC, Bartolomé B, Pereira Barbosa M. Severe allergy to poultry meat without sensitisation to egg proteins with concomitant Leguminosae allergy. Case report. Allergol Immunopathol (Madr) 2009;37:168-171

↩

[170] - Zacharisen MC. Severe allergy to chicken meat. WMJ 2006;105:50-52

INTRODUCTION: While allergic reactions to poultry products in the form of feathers and eggs are common, allergic reactions to chicken meat are rare. Despite the popularity of chicken in today's healthy diet, severe reactions after ingesting chicken meat are rarely described. This report describes a patient who developed chicken meat anaphylaxis without experiencing allergy to eggs or feathers. METHODS: A carefully obtained history from a 41-year-old male suggested chicken meat as the cause of his symptoms. He developed abdominal cramping, generalized urticaria, and chest tightness after ingestion of chicken meat. Percutaneous allergy skin testing with commercial chicken and turkey extract and freshly cooked chicken utilizing the prick-prick test was performed. RESULTS: Skin testing was positive with all extracts of chicken and turkey in the patient, and negative in 4 healthy adult controls. Skin tests with feather and egg extract were negative. CONCLUSION: This is the third report of severe allergy to chicken meat in the absence of egg allergy. Physicians should be aware of the presence of chicken allergy without concomitant feather or egg allergy, particularly in adults.

↩

[171] - Liccardi G, Szepfalusi Z, Noschese P, Nentwich I, D'Amato M, D'Amato G. Allergy to chicken meat without sensitization to egg proteins: A case report. J Allergy Clin Immunol 1997;100:577-579

↩

[172] - Kelso JM, Cockrell G, Helm RM, Burks AW. Common allergens in avian meats. J Allergy Clin Immunol 1999;104:202-204

BACKGROUND: Reports of allergy to bird meats are uncommon, and most have been in patients with "bird-egg syndrome." OBJECTIVE: We sought to evaluate 3 patients who reported allergic reactions to several avian meats, but who denied allergic reactions to eating eggs. The patients required yellow fever vaccine for entry into the military. METHODS: Patients were skin tested with commercial extracts of chicken, turkey, and egg, as well as with crude extracts made from dove and quail meat, and with yellow fever vaccine. Immunoblots for IgE antibody were performed by using the same materials used for skin testing plus extracts of duck and goose meat. RESULTS: Skin tests were positive in all 3 patients to chicken, turkey, dove, quail, and yellow fever vaccine and negative to egg. This included some positive skin test responses to bird meats the patients denied ever having eaten. The vaccine was administered in graded doses. Immunoblots revealed IgE binding to several proteins of similar molecular weights in all of the avian meats but not to egg or yellow fever vaccine. Again, this included IgE antibody to some bird meats the patients denied ever having eaten. CONCLUSION: Patients allergic to one bird meat may be allergic to others, including game birds, probably because of cross-reacting allergens. Such patients may have to exercise caution even when eating bird meats they have not previously ingested. The relationship of this allergy to yellow fever vaccine, if any, remains to be determined

↩

[173] - Martorell Aragones A, Bone Calvo J, Garcia Ara MC, Nevot Falco S, Plaza Martin AM, (Food Allergy Committee of the Spanish Society of Pediatric Clinical Immunology and Allergy) Allergy to egg proteins. Allergol Immunopathol (Madr) 2001;29:72-95

↩

[174] - Martinez Alonso JC, Dominguez Ortega FJ, Fuentes Gonzalo MJ. Angioedema por sensibilización a carne de gallina. Allergol Immunopathol (Madr) 2003;31:50-52

BACKGROUND: Egg is the most frequent cause of food allergy in children. The bird-egg syndrome, found in a group of patients sensitized to egg through bird proteins, was infrequent in children. We report a patient with former history of hypersensitivity to egg who developed episodes of angioedema after ingestion of hen meat. METHODS: Prick testing with egg and their different antigenic protein fractions, alpha-livetin and chicken meat was performed. Antigens of hen meat were used for the skin prick test and prick-by-prick. Serum-specific IgE was identified with use of the CAP techniques and SDS-PAGE Immunoblotting. RESULTS: Prick test was positive with egg yolk, alpha-livetin and chicken meat. A prick-by-prick test with hen meat resulted positive in our patient, but the same test in four controls patients were negative. Serum specific IgE was positive for egg yolk and hen meat. CONCLUSION: Allergy reactions to hen meat are exceptional. We report a case of children with allergy to egg proteins and hen meat that suggest an IgE mediated hypersensitivity reaction. Skin test reveal sensitivity to egg yolk and alpha-livetin, but this pattern of sensitization was infrequent in children.

↩

[175] - Lemerdy P, Moneret-Vautrin DA, Rancé F, Kanny G, Parisot L. Prévalence des allergies alimentaires chez l'enfant et l'adulte. Alim'Inter 2003;8:5-8

↩

[176] - Allergie à la viande de porc. Alim'Inter 2000;5(23):3-4

↩

[177] - Llaster R, Polo F, Delahoz F, Guillaumet B. Alimentary allergy to pork: crossreactivity among pork kidney and pork and lamb gut. Clin Exp Allergy 1998;28:1021-1025

BACKGROUND: A patient suffered from anaphylaxis after the ingestion of pork gut and kidney, but she tolerated pork meat. Clinical symptoms were also triggered upon intake of lamb gut. OBJECTIVE: To demonstrate an IgE-mediated hypersensitivity and identify the pork proteins involved. And also, to study the possible cross-allergenicity among proteins from lamb gut and pork. METHODS AND RESULTS: The patient had strong positive skin-prick test responses to pork kidney, gut and liver, and lamb gut and kidney. RAST technique showed specific IgE to pork kidney, gut and meat. Immunoblotting after SDS-PAGE disclosed the presence of four prominent IgE-binding polypeptides in pork kidney (200, 90, 57, and 47 kDa), two in gut (57 and 27 kDa), and three in meat (51, 40, and 28-30 kDa), apart from other weaker radiostained bands in each extract. The binding of IgE to 200 and 90 kDa allergens from pork kidney was inhibited by gut from pork and lamb in immunoblotting inhibition assays. No inhibition was produced by pork meat. CONCLUSIONS: A mechanism of IgE-mediated hypersensitivity has been demonstrated in this case of anaphylaxis provoked by pork products. Four main allergens were detected in pork kidney, two of which (200 and 90 kDa) share allergenic epitopes with proteins from pork and lamb gut. On the other hand, pork meat does not seem to have allergenic epitopes in common with pork kidney.

↩

[178] - Lepp U, Pauli G, Wittkowski M, Becker WM. Anaphylactic shock after ingestion of pork kidney: case reports and western blot studies. 8th International Symposium on Problems of Food Allergy, Venice 2001, March 11-13

Food allergies to pork kidney are rare. We report of two patients with allergic reactions after ingestion of pork kidney. Utilizing Western-blots we tried to identify important allergens. Clinical cases: The first patient is a 55 year old French female with two episodes of anaphylactic reaction approximately two hours after eating cooked pork kidney. The symptoms were urticaria and edema and, severe anaphylaxis with hypotension and bronchospasm, respectively. She had no other respiratory allergy. Skin Prick Test (SPT) was negative to a crude kidney extract, but positive in case of a cooked kidney extract. Moreover Patch Tests were also positive at 48 hours with cooked kidney. All other SPT were negative, especially for cat and dog extracts. In the second case we report of a 52 years old German female with a known allergy to wasp sting, ampicillin and sulfonamides. She reported an anaphylactic reaction 6 h after ingestion of pork kidney. SPT were only positive to vespula-venom, not to pork kidney in any preparation. Specific IgE was found against venom, cat, dog. However nasal provocation testing with a cat extract reveals no symptoms. Open challenge under clinical conditions confirmed pork kidney as causing allergen as the patient showed an anaphylactic reaction 6 h after ingestion. Serum IgE was measured with 406 and 70 kU/L, respectively. Specific IgE-antibodies against pork meat could be found in both patients (0,723 kU/l and 4,49 kU/l) without any symptoms after eating pork meat. Both patients' Western blotting with an extract of crude pork kidney showed an IgE-binding in the range between 10 and 98 kD. Cooking the kidney does not abolish IgE-reactivity, but bands get more diffuse, which might be a sign of denaturising. Comparing this binding patterns with that of pork meat, kidney proteins lower than 14 kD seems to be crucial. Conclusions: 1) There are anaphylactic reactions against pork kidney. 2) This reactions may be delayed (2 and 6 hours, respectively). 3) Both patients show specific IgE-antibodies without any symptoms. 4) Proteins in the molecular weight of lower than 14Kd may represent the causing allergen.

↩

[179] - Llaster R, Polo F, Delahoz F, Guillaumet B. Alimentary allergy to pork: crossreactivity among pork kidney and pork and lamb gut. Clin Exp Allergy 1998;28:1021-1025

BACKGROUND: A patient suffered from anaphylaxis after the ingestion of pork gut and kidney, but she tolerated pork meat. Clinical symptoms were also triggered upon intake of lamb gut. OBJECTIVE: To demonstrate an IgE-mediated hypersensitivity and identify the pork proteins involved. And also, to study the possible cross-allergenicity among proteins from lamb gut and pork. METHODS AND RESULTS: The patient had strong positive skin-prick test responses to pork kidney, gut and liver, and lamb gut and kidney. RAST technique showed specific IgE to pork kidney, gut and meat. Immunoblotting after SDS-PAGE disclosed the presence of four prominent IgE-binding polypeptides in pork kidney (200, 90, 57, and 47 kDa), two in gut (57 and 27 kDa), and three in meat (51, 40, and 28-30 kDa), apart from other weaker radiostained bands in each extract. The binding of IgE to 200 and 90 kDa allergens from pork kidney was inhibited by gut from pork and lamb in immunoblotting inhibition assays. No inhibition was produced by pork meat. CONCLUSIONS: A mechanism of IgE-mediated hypersensitivity has been demonstrated in this case of anaphylaxis provoked by pork products. Four main allergens were detected in pork kidney, two of which (200 and 90 kDa) share allergenic epitopes with proteins from pork and lamb gut. On the other hand, pork meat does not seem to have allergenic epitopes in common with pork kidney.

↩

[180] - Touraine F, Principaud Perrier M, Brianchon C, Sagot L, Boumediene A, Sainte Laudy J, et al. Particularités de l'allergie alimentaire au porc. Rev Fr Allergol Immunol Clin 2006;46:388-391

L'allergie alimentaire au porc est rare. Cependant, nous en rapportons 13 cas, concernant surtout l'allergie aux rognons. Les réactions peuvent être sévères. Les sensibilisations croisées sont nombreuses avec d'autres mammifères. Une meilleure connaissance des allergènes en cause est nécessaire pour mieux identifier les risques chez ces patients.

↩

[181] - Morisset M, Frémont S. Quel type de viande est à risque dans un syndrome porc-chat ?. Alim'Inter 2000;5(25):22

↩

[182] - Paschke A, Besler M. Stability of bovine allergens during food processing. Ann Allergy Asthma Immunol 2002;89(6 Suppl. 1):16-20

OBJECTIVE: The primary objective of this review was to summarize reported findings about the influence of various food manufacturing processes on the potential alteration of bovine allergens in cow's milk, beef, and related food products. DATA SOURCES: This review was based on literature research in two German databases. STUDY SELECTION: The expert opinion of the authors was used to select the relevant data for the review. RESULTS: Changes in allergenic activity during food processing are attributable to inactivation or destruction of epitope structures, formation of new epitopes, or improved access of previously hidden epitopes. The allergenic potency of food could be altered by several food manufacturing procedures--such as mechanical, purification, thermal, biochemical, and chemical processes. The main processing steps studied by investigators were heating (dry heating, boiling, or cooking) and enzymatic digestion. A review of the available literature on the alteration of bovine allergens in cow's milk, meat, and related food products revealed reduction (but not elimination) of allergenicity by heating of cow's milk for 10 minutes. Although homogenization did not change the allergenic potency of cow's milk, it decreased the allergenicity of beef, as did freeze-drying. Digestion studies showed varied results. CONCLUSIONS: The allergenicity of some food products decreased during certain processing steps, but the results of other investigations differed. Therefore, more systematic research on the influence of food processing on allergenicity should be undertaken.

↩

[183] - Fiocchi A, Bouygue GR, Sarratud T, Terracciano L, Martelli A, Restani P. Clinical tolerance of processed foods. Ann Allergy Asthma Immunol 2004;93(5 Suppl. 3):S38-S46

OBJECTIVE: To review the effects of technological processing on selected foods of relevance to childhood allergy from the viewpoints of reduced allergenicity, contamination of processed foods by allergens introduced during processing, and ad hoc technologies to produce reduced hypoallergenic products. DATA SOURCES: We searched the literature (PubMed/MEDLINE) for articles published between January 1994 and April 2004 using the following keywords: food allergy AND process* OR heat* OR cooking OR toleran*. STUDY SELECTION: We drew on our collective clinical and biological experience to restrict retrieved studies to those of more frequent relevance to a hospital allergy practice. RESULTS: Comparatively few clinical studies address the modification of allergenicity of food through cooking or processing. Dairy foods are largely unaffected by processing and may be contaminated by, or themselves become, hidden allergens. Hypoallergenic formulas based on milk, soy, or rice and homogenized beef are successful applications of allergenicity reduction via technological processing. Egg, fish, condiments, and vegetables all carry heat-resistant allergens and should also be considered contaminants. Cereals and bakery products are generally well tolerated, but their allergenicity may be enhanced by processing; the case of rice is still open. Peanut allergens are stable, and the evidence is scant that thermal processing affects the allergenicity of soybean and soy hydrolysates. The debate is ongoing about the tolerance of vegetable oils. CONCLUSIONS: It is too early to systematize clinical studies based on single procedures. Processing affects antigenicity, but this does not always translate into safety recommendations. Industrial processing is liable to contamination, and monitoring and labeling are industry priorities. Clinicians should evaluate foods by as complete a workup as possible before recommending processed foods.

↩

[184] - Besler M, Steinhart H, Paschke A. Stability of food allergens and allergenicity of processed foods. J Chromatogr B Biomed Appl 2001;756:207-228

The allergenicity of food could be altered by several processing procedures. For various foods of animal and plant origin the available literature on this alteration is described. Investigations on hidden allergens in food products are also dealt with. [References: 160

↩

[185] - Kanny G, De Hauteclocque C, Moneret-Vautrin DA. Food anaphylaxis to bovine serum albumin. J Allergy Clin Immunol 1998;101:137-139

↩

[186] - Ayuso R, Lehrer SB, Tanaka L, Ibanez MD, Pascual C, Burks AW, et al. IgE antibody response to vertebrate meat proteins including tropomyosin. Ann Allergy Asthma Immunol 1999;83:399-405

Although meat is a main source of proteins in western diets, little information is available regarding allergy to vertebrate meats or the allergens implicated in these reactions. OBJECTIVE: To evaluate the in vitro IgE antibody response to different vertebrate meats in suspected meat-allergic subjects, as well as the possible role of tropomyosin in meat allergy and to analyze the cross-reactivity between vertebrate meats and the effect of heating on the IgE-binding to meat proteins. METHODS: Fifty-seven sera from suspected meat-allergic subjects were tested by grid blot to extracts of beef, lamb, pork, venison, chicken, and turkey and to four mammalian tropomyosins of different origins. RESULTS: Meat-allergic subjects have IgE antibodies to proteins in different mammalian meats (43/57 subjects); cross-reactivity with avian meat was limited: less than 50% (19/43) of meat positive sera reacted to chicken. In contrast, most of the poultry-positive sera also reacted to different mammalian meats. In general, there was stronger IgE reactivity to raw meats in comparison to cooked meats; an exception was six cases in which IgE reactivity to cooked poultry was stronger. Weak IgE reactivity to tropomyosin was detected in only 2/57 sera tested. CONCLUSIONS: Suspected meat-allergic subjects have serum IgE directed to meat proteins. In vitro cross-reactivity among mammalian meats appears to be important, while cross-reactivity to poultry is limited indicating mammalian-specific proteins. Although cooking in general denatures meat proteins rendering them less allergenic, in some cases the process of cooking may result in the formation of new allergenic moieties. The muscle protein tropomyosin is not an important vertebrate meat allergen.

↩

[187] - Ayuso R, Lehrer SB, Lopez M, Reese G, Ibanez RM, Martin-Esteban M, et al. Identification of bovine IgG as a major cross-reactive vertebrate meat allergen. Allergy 2000;55:348-354

Although beef is a main source of protein in Western diets, very little has been published on allergic reactions to beef or the main allergens implicated in these reactions. The aim was to evaluate the IgE antibody response to beef in suspected meat-allergic subjects and assess cross-reactivity of beef with other vertebrate meats. METHODS: Fifty-seven sera from suspected meat-allergic subjects were tested by grid blot for specific IgE antibodies to vertebrate meats (beef, lamb, pork, venison, and chicken), and the patterns of recognition of meat proteins were assessed by immunoblot studies. RESULTS: A 160-kDa band, identified as bovine IgG, was detected in raw beef in 83% (10/12) of beef-allergic subjects but in only 24% of the beef-tolerant subjects. IgE reactivity to a band of similar mol. mass was detected also in lamb and venison, but rarely in pork or chicken. Complete inhibition of the IgE reactivity to the bovine IgG was obtained with lamb, venison, and milk. IgE reactivity to this band also completely disappeared when beef or lamb extracts were separated under reducing conditions, indicating conformational epitopes. CONCLUSIONS: Bovine IgG appears to be a major cross-reacting meat allergen that could predict beef allergy. Further studies with oral IgG challenges should be performed to document the conclusion that in vitro reactivity correlates with clinical hypersensitivity. The role of bovine IgG in other bovine products such as milk, dander, or hair must also be studied, and the hypothesis that it is a cross-reacting allergen with other mammalian products validated.

↩

[188] - Werfel SJ, Cooke SK, Sampson HA. Clinical reactivity to beef in children allergic to cow's milk. J Allergy Clin Immunol 1997;99:293-300

↩

[189] - Fiocchi A, Bouygue GR, Sarratud T, Terracciano L, Martelli A, Restani P. Clinical tolerance of processed foods. Ann Allergy Asthma Immunol 2004;93(5 Suppl. 3):S38-S46

OBJECTIVE: To review the effects of technological processing on selected foods of relevance to childhood allergy from the viewpoints of reduced allergenicity, contamination of processed foods by allergens introduced during processing, and ad hoc technologies to produce reduced hypoallergenic products. DATA SOURCES: We searched the literature (PubMed/MEDLINE) for articles published between January 1994 and April 2004 using the following keywords: food allergy AND process* OR heat* OR cooking OR toleran*. STUDY SELECTION: We drew on our collective clinical and biological experience to restrict retrieved studies to those of more frequent relevance to a hospital allergy practice. RESULTS: Comparatively few clinical studies address the modification of allergenicity of food through cooking or processing. Dairy foods are largely unaffected by processing and may be contaminated by, or themselves become, hidden allergens. Hypoallergenic formulas based on milk, soy, or rice and homogenized beef are successful applications of allergenicity reduction via technological processing. Egg, fish, condiments, and vegetables all carry heat-resistant allergens and should also be considered contaminants. Cereals and bakery products are generally well tolerated, but their allergenicity may be enhanced by processing; the case of rice is still open. Peanut allergens are stable, and the evidence is scant that thermal processing affects the allergenicity of soybean and soy hydrolysates. The debate is ongoing about the tolerance of vegetable oils. CONCLUSIONS: It is too early to systematize clinical studies based on single procedures. Processing affects antigenicity, but this does not always translate into safety recommendations. Industrial processing is liable to contamination, and monitoring and labeling are industry priorities. Clinicians should evaluate foods by as complete a workup as possible before recommending processed foods.

↩

[190] - Kanny G, De Hauteclocque C, Moneret-Vautrin DA. Food anaphylaxis to bovine serum albumin. J Allergy Clin Immunol 1998;101:137-139

↩

[191] - Fiocchi A, Restani P, Riva E, Mirri GP, Santini I, Bernardo L, et al. Heat treatment modifies the allergenicity of beef and bovine serum albumin. Allergy 1998;53:798-802

The effect of heat on the allergenicity of beef and bovine serum albumin was investigated among 10 toddlers skin prick test (SPT)-positive to raw and cooked beef. The meat-allergy diagnosis was confirmed during double-blind, placebo-controlled food challenge (DBPCFC) with 180 g of beef cooked for 5 min at 100 degrees C. SPT with homogenized and freeze-dried beef, and heated and unheated bovine serum albumin were performed. Both heated and unheated bovine serum albumin, homogenized beef, and freeze-dried beef were used in trial DBPCFC. All children were SPT-positive to unheated bovine serum albumin. Seven were positive to heated bovine serum albumin, one to freeze-dried beef, and none to homogenized beef. DBPCFCs were negative for homogenized beef and freeze-dried beef, positive for unheated bovine serum albumin in five patients, and positive for heated albumin in four children. We conclude that heating reduces sensitization to beef and bovine serum albumin but does not abolish reactivity to albumin under home conditions. However, industrially heat-treated and sterilized homogenized beef and freeze-dried beef may be suitable substitutes in beef-allergic children's diets.

↩

[192] - Werfel SJ, Cooke SK, Sampson HA. Clinical reactivity to beef in children allergic to cow's milk. J Allergy Clin Immunol 1997;99:293-300

↩

[193] - Vereda A, Cuesta J, Barderas M, de la Cuesta F, Pastor C, Vivanco F, et al. Beef allergy. EAACI 25th Congress, Vienna, 10-14 June, 2006, Poster n°1529

Background: Although beef meat is widely consumed in Western diets, beef allergy is rarely reported. The aim of the study was to describe a case of beef allergy and to identify the allergens. Method:A 16-month-old male, with atopic dermatitis and several food allergies (egg, fish and legumes), was studied. At the age of 7 months, he suffered labial angioedema and perioral erythema after the ingestion of scarcely cooked beef. He tolerated well done beef, as well as other meats and cow's milk. Skin tests, oral challenge and specific IgE determination were performed. Meat allergens were studied by SDS-PAGE, IgE-immunoblotting, inhibition assays and mass spectrometry. Results: Prick tests were positive to egg, fish, legumes, bovine serum albumin (BSA),bovine gamma globulin (BGG) and cow epithelium, and negative to the remaining milk proteins. Prick-prick tests were positive to raw and cooked beef, pork and lamb, and negative to chicken meat. Oral challenge test with raw beef meat elicited a positive response, with perioral wheals and erithema, and labial angioedema. However, the oral challenge was negative with cooked beef. Specific IgE was positive to BSA, cow's epithelium and milk, beef, pork and lamb meat. SDS-PAGE and immunoblotting with the beef extract revealed some prominent IgE-binding protein bands at >130, 67, 60 and 25 kDa, which were common to other meats (pork, rabbit, lamb), as well as to cow's epithelium and milk. IgE binding was decreased by heating the beef meat extract. Inhibition assays demonstrated cross-reactivity among the different meats, mainly between beef and lamb. BSA, b-enolase and creatin kinase were identified by mass spectrometry as allergens in the beef meat extract. Conclusions: We present a child with beef allergy, also sensitized to cow‚s milk and other meats. The responsible allergens are heat-labile, and could correspond to BSA and IGG. We also identified two proteins (b-enolase and creatin kinase), which have not been previously described as allergens.

↩

[194] - Ayuso R, Lehrer SB, Lopez M, Reese G, Ibanez RM, Martin-Esteban M, et al. Identification of bovine IgG as a major cross-reactive vertebrate meat allergen. Allergy 2000;55:348-354

Although beef is a main source of protein in Western diets, very little has been published on allergic reactions to beef or the main allergens implicated in these reactions. The aim was to evaluate the IgE antibody response to beef in suspected meat-allergic subjects and assess cross-reactivity of beef with other vertebrate meats. METHODS: Fifty-seven sera from suspected meat-allergic subjects were tested by grid blot for specific IgE antibodies to vertebrate meats (beef, lamb, pork, venison, and chicken), and the patterns of recognition of meat proteins were assessed by immunoblot studies. RESULTS: A 160-kDa band, identified as bovine IgG, was detected in raw beef in 83% (10/12) of beef-allergic subjects but in only 24% of the beef-tolerant subjects. IgE reactivity to a band of similar mol. mass was detected also in lamb and venison, but rarely in pork or chicken. Complete inhibition of the IgE reactivity to the bovine IgG was obtained with lamb, venison, and milk. IgE reactivity to this band also completely disappeared when beef or lamb extracts were separated under reducing conditions, indicating conformational epitopes. CONCLUSIONS: Bovine IgG appears to be a major cross-reacting meat allergen that could predict beef allergy. Further studies with oral IgG challenges should be performed to document the conclusion that in vitro reactivity correlates with clinical hypersensitivity. The role of bovine IgG in other bovine products such as milk, dander, or hair must also be studied, and the hypothesis that it is a cross-reacting allergen with other mammalian products validated.

↩

[195] - Vicente-Serrano J, Caballero ML, Rodriguez-Pérez R, Carretero P, Pérez R, Blanco JG, et al. Sensitization to serum albumins in children allergic to cow’s milk and epithelia. Pediatr Allergy Immunol 2007;18:503-507

Patients with persistent milk allergy and specific immunoglobulin E (IgE) to bovine serum albumin (BSA) have a greater risk of rhinoconjunctivitis and asthma because of animal dander. To prove the cross-reactivity between serum albumin (SA) of different mammals in milk, meat, and epithelia and determine if heat treatment of meats decrease the allergenicity of albumins. The study was performed using SDS-PAGE and IgE-immunoblotting using sera from eight patients sensitized to milk, BSA, and animal danders. Sera from non-allergic and only animal dander allergic subjects served as a control. With one exception, all patients' sera recognized SA in different meats (beef, lamb, deer, and pork), epithelia (dog, cat, and cow), and cow's milk. Some patients even were only sensitized to SA in meat and epithelia. Danders' allergic only recognized other proteins in epithelia but not SA. No patients reacted to SA from heated meat extracts. Serum albumin is an important allergen involved in milk, meat, and epithelia allergy. The first contact with SA was through cow's milk and patients developed sensitization to epithelia SA even without direct contact with animals. Patients with both BSA and cow's milk allergy must avoid raw meats and furry pets.

↩

[196] - Restani P, Fiocchi A, Beretta B, Velona T, Giovannini M, Galli CL. Effects of structure modifications on IgE binding properties of serum albumins. Int Arch Allergy Immunol 1998;117:113-119

BACKGROUND: Bovine serum albumin (BSA) is one of the most widely studied proteins its structure is well-known and its antigenic characteristics have been described in studies performed in in vitro and animal models. The aim of our work was to evaluate the role of BSA conformation in its antigenicity (recognition by circulating IgEs from allergic children). METHODS: This study was performed using electrophoresis associated with the immunoblotting technique, where sera from children sensitized to BSA (as shown by double-blind placebo-controlled food challenge) were used. RESULTS AND DISCUSSION: Heat treatment and chemical denaturation (SDS treatment) are not able to decrease the BSA capability to bind circulating IgEs. Only by reducing treatment with 2-mercaptoethanol is it possible to modify but not to eliminate the antigenicity of this protein. The reactivity to other serum albumins from different animal species was also investigated and in this study we show a direct correlation between the number of IgE-mediated responses observed in immunoblotting and the percentage of sequence identity (phylogenetic similarity) of serum albumins. CONCLUSION: Data obtained in this research indicate that serum albumin antigenicity is only partially correlated to its native three-dimensional structure.

↩

[197] - Werfel SJ, Cooke SK, Sampson HA. Clinical reactivity to beef in children allergic to cow's milk. J Allergy Clin Immunol 1997;99:293-300

↩

[198] - Ayuso R, Lehrer SB, Lopez M, Reese G, Ibanez RM, Martin-Esteban M, et al. Identification of bovine IgG as a major cross-reactive vertebrate meat allergen. Allergy 2000;55:348-354

Although beef is a main source of protein in Western diets, very little has been published on allergic reactions to beef or the main allergens implicated in these reactions. The aim was to evaluate the IgE antibody response to beef in suspected meat-allergic subjects and assess cross-reactivity of beef with other vertebrate meats. METHODS: Fifty-seven sera from suspected meat-allergic subjects were tested by grid blot for specific IgE antibodies to vertebrate meats (beef, lamb, pork, venison, and chicken), and the patterns of recognition of meat proteins were assessed by immunoblot studies. RESULTS: A 160-kDa band, identified as bovine IgG, was detected in raw beef in 83% (10/12) of beef-allergic subjects but in only 24% of the beef-tolerant subjects. IgE reactivity to a band of similar mol. mass was detected also in lamb and venison, but rarely in pork or chicken. Complete inhibition of the IgE reactivity to the bovine IgG was obtained with lamb, venison, and milk. IgE reactivity to this band also completely disappeared when beef or lamb extracts were separated under reducing conditions, indicating conformational epitopes. CONCLUSIONS: Bovine IgG appears to be a major cross-reacting meat allergen that could predict beef allergy. Further studies with oral IgG challenges should be performed to document the conclusion that in vitro reactivity correlates with clinical hypersensitivity. The role of bovine IgG in other bovine products such as milk, dander, or hair must also be studied, and the hypothesis that it is a cross-reacting allergen with other mammalian products validated.

↩

[199] - Fuentes MM, Palacios R, Garcés MM, Caballero ML, Moneo I. Isolation and characterization of a heat-resistant beef allergen: myoglobin. Allergy 2004;59:327-331

BACKGROUND: Meat allergy is rarely reported. Most of the described cases are sensitizations to bovine serum albumin . OBJECTIVE: The aim of the study was to describe a case of allergy to a new meat allergen and, after its characterization . METHODS: A 35-year-old nonatopic female with allergic episodes after ingestion of several types of meat was studied. Skin tests (prick and prick-to-prick); total and specific immunoglobulin E (IgE) determination; sodium dodecyl sulphate-polyacrylamide gel electrophoresis and specific IgE determination by immunoblotting under different conditions were performed. A 17-kDa allergen was semipurified by ethanol fractionation and its amino-terminal sequence was determined. The existence of specific IgE directed to this protein was studied by immunoblot in 80 atopic patients . RESULTS: The patient showed specific IgE antibodies to a 17-kDa protein. During the isolation of this allergen it was found that a 70-90% (vol/vol) ethanol concentration was able to purify the protein. The characterization revealed that it was a heat-resistant protein without disulfide bonds. N-terminal amino acid sequence (16 residues) showed identity with myoglobin. The study of specific IgE to this allergen among atopic patients showed that it was recognized by about 1% of the subjects . CONCLUSIONS: We describe a case of meat allergy caused by myoglobin. This is the first described case of monosensitization to this protein.

↩

[200] - Ayuso R, Lehrer SB, Tanaka L, Ibanez MD, Pascual C, Burks AW, et al. IgE antibody response to vertebrate meat proteins including tropomyosin. Ann Allergy Asthma Immunol 1999;83:399-405

Although meat is a main source of proteins in western diets, little information is available regarding allergy to vertebrate meats or the allergens implicated in these reactions. OBJECTIVE: To evaluate the in vitro IgE antibody response to different vertebrate meats in suspected meat-allergic subjects, as well as the possible role of tropomyosin in meat allergy and to analyze the cross-reactivity between vertebrate meats and the effect of heating on the IgE-binding to meat proteins. METHODS: Fifty-seven sera from suspected meat-allergic subjects were tested by grid blot to extracts of beef, lamb, pork, venison, chicken, and turkey and to four mammalian tropomyosins of different origins. RESULTS: Meat-allergic subjects have IgE antibodies to proteins in different mammalian meats (43/57 subjects); cross-reactivity with avian meat was limited: less than 50% (19/43) of meat positive sera reacted to chicken. In contrast, most of the poultry-positive sera also reacted to different mammalian meats. In general, there was stronger IgE reactivity to raw meats in comparison to cooked meats; an exception was six cases in which IgE reactivity to cooked poultry was stronger. Weak IgE reactivity to tropomyosin was detected in only 2/57 sera tested. CONCLUSIONS: Suspected meat-allergic subjects have serum IgE directed to meat proteins. In vitro cross-reactivity among mammalian meats appears to be important, while cross-reactivity to poultry is limited indicating mammalian-specific proteins. Although cooking in general denatures meat proteins rendering them less allergenic, in some cases the process of cooking may result in the formation of new allergenic moieties. The muscle protein tropomyosin is not an important vertebrate meat allergen.

↩

[201] - Drouet M. Allergènes des viandes. Rev Fr Allergol 2009;49:160-165

L‚allergie aux viandes de vertébrés est passée en revue à partir des divers rapports et travaux de la littérature. Nous présentons les diverses allergies aux viandes et leurs particularités. Nous évoquons les allergies croisées démontrées ou simplement suspectées pour chacune d‚entre elles.

↩

[202] - Palacios Benito R, Alvarez-Lovel MC, Martinez-Cocera C, Del Castillo Paya MM, Romanillos RA. Allergy to meat. Allergy 2002;57:858-859

↩

[203] - Eigenmann PA. Anaphylaxis to cow's milk and beef meat proteins. Ann Allergy Asthma Immunol 2002;89(6 Suppl. 1):61-64

OBJECTIVE: This report summarizes a review of anaphylactic reactions to cow's milk and beef presented at a recent conference on adverse reactions to bovine proteins. DATA SOURCES: A review of pertinent PubMed (National Library of Medicine) articles was performed. Relevant publications were critically analyzed. STUDY SELECTION: The expert opinion of the author was used to select the relevant data for the review. RESULTS: Although cow's milk has been recognized for many years as one of the leading causes of food allergy, beef has only recently been identified as a cause of immunoglobulin (Ig)E-mediated reactions. Epidemiologic data indicate that the prevalence of cow's milk allergy is approximately 1 to 2%, but no definite data are available for beef allergy. Anaphylaxis to both foods has been well characterized in childhood; however, a subset of adult patients may become reactive to cow's milk and have the characteristic features of anaphylaxis. The diagnosis is primarily based on skin prick tests and measurement of cow's milk- or beef-specific IgE antibodies. In selected patients, a standardized food challenge might be necessary to determine the diagnosis. CONCLUSIONS: In the absence of a proactive treatment of food allergy, patients with anaphylaxis to cow's milk or beef must be instructed to avoid these foods in their diet. Although cow's milk allergy generally is associated with a good prognosis, with most young children spontaneously "outgrowing" the disease, current research is focusing on the prevention and the treatment of this condition.

↩

[204] - Kanny G. Allergie à la viande de dinde. Alim'Inter 1997;2(7):14

↩

[205] - Morisset M, Frémont S. Quel type de viande est à risque dans un syndrome porc-chat ?. Alim'Inter 2000;5(25):22

↩

[206] - Kanny G, De Hauteclocque C, Moneret-Vautrin DA. Food anaphylaxis to bovine serum albumin. J Allergy Clin Immunol 1998;101:137-139

↩

[207] - Guerrier G, Noiret A, Bellon G. Viande de boeuf ou lait de vache, même prudence: sensibilisation possible à la sérumalbumine bovine chez deux enfants. Rev Fr Allergol Immunol Clin 2001;41:396-400

Les auteurs rapportent deux observations de sensibilisation possible à la sérumalbumine bovine chez des enfants âgés de cinq et quatre ans. Celle-ci est associée à une intolérance au lait de vache (oedème des paupières et douleurs abdominales) chez le premier, à une intolérance à la viande de boeuf peu cuite chez le second (urticaire généralisée et oedème de la face). Les profils biologiques des deux enfants sont identiques, caractérisés par la présence d'IgE spécifiques vis-à-vis du lait de vache total, de la viande de boeuf et de la sérumalbumine bovine. Il n'existe pas d'IgE spécifiques dirigées contre les fractions « classiques » du lait de vache, alpha-lactalbumine, bêta-lactoglobuline et caséine. Chez les deux sujets, les prick-tests sont négatifs pour le lait et ses fractions. Le prick-test est positif pour la viande de boeuf uniquement chez l'enfant intolérant à cet aliment. Il est difficile d'expliquer cette dissociation séméiologique en présence d'une vraisemblable sensibilisation commune à la sérumalbumine bovine. La sensibilisation à la sérumalbumine bovine est rare, surtout quand elle est isolée et, en pratique, il faut s'assurer que la recherche d'IgE vis-à-vis du lait total (Rast) comporte bien, entre autres, celle d'IgE spécifiques vis-à-vis de cette protéine. Elle explique chez nos deux sujets la positivité du Rast à la fois au lait de vache total et à la viande de boeuf, mais l'exclusion d'un seul de ces deux aliments est justifiée chez chacun deux.

↩

[208] - Werfel SJ, Cooke SK, Sampson HA. Clinical reactivity to beef in children allergic to cow's milk. J Allergy Clin Immunol 1997;99:293-300

↩

[209] - Domínguez-Ortega J, Rodríguez-Jiménez B, Ledesma A, Kindelan C, González JM, Jiménez F. Selective Allergy to Raw Pork. J Investig Allergol Clin Immunol 2009;19:244-245

↩

[210] - Rico-Diaz A, Diaz Roman T, Costa-Dominguez M, Ledesma A. Cow milk and meat allergy in a patient with allergy to hamster can be mediated by sera albumin. Allergy 2009;64(Suppl. 90):234-235

Background: Pork meat is a common food in diet but the allergy to this is rare. Much of the allergies to meat have been produced by primary sensitization to animal aeroallergens. Thus, in patients with pork meat allergy, the sensitization has been produced by cat antigen. Sera albumin is a putative cross reactive antigen in response. We ought to know allergy mechanism in a poly-sensitive patient with allergy to dust mites, animal epithelia and a late debut of cow milk allergy. Methods: A 10 years old female with diagnostic of dust mites and animals epithelia allergy undergoes eczema, rhinitis and asthma. She was living with cats, dogs, and hamster. Since she was 14 years old, she had abdominals pains, vomits, diarrhea, oral itch, rash and facial urticaria, immediately after the ingestions of lacteous derivates, or fresh sausages. Cooked meat was always well tolerated. Skin Prick tests to aeroallergens, to commercial food extract including cow milk and to different meats were made. Prick-prick with cooked and uncooked meat and specific IgE to animal allergens were also determined. Western Blot (WB) test. An extract of beef meat at 10% (p/v) in phosphate buffers was obtained, and conveniently stored at -20°C until use. Commercial extracts of hamster and cat epithelia, pork and beef meat, were employed in a non reduced SDS PAGE assay and transferred to nitrocellulose membrane. The patient's serum was incubated with the nitrocellulose strips to detect proteins with affinity to serum IgE. Also, the patient's serum was incubated with extract of hamster or cow epithelium in other strips in a blocking WB assay. Results: Prick test. D Pteronyssinus 10mm, Hamster 8mm, Cat 5mm, Dog 5mm, Cow milk (-), casein (-), BLG (-), ALA 4mm, BSA 4mm, histamine (8mm). Prick-Prick. Pork meat 11mm, cooked pork meat (-), Beef meat 3mm, cooked beef meat (-). IgE to hamster > 100 KU/ l; pork meat 9,2 KU/l; BSA 0,38KU/l. WB: Several bands were observed: A 60Kd band in blots with beef meat, pork meat and hamster epithelium, suggesting IgE recognizing sera albumin, a 19Kd band on cat epithelium (Fel d1) and 15Kd band on hamster epithelium. An evident reduction in 60Kd band intensity was observed following inhibition of patient serum with hamster extract in blocking WB. That diminution of band was observed in pork meat but not in beef meat blot. Conclusion: Our results suggest a food allergy to cow milk and pork meat proteins probably in relation to primary sensitization of hamster.

↩

[211] - Asero R, Mistrello G, Falagiani P. Oral allergy syndrome from pork. Allergy 1997;52:684-686

↩

[212] - Besler M, Fiocchi A, Restani P. Allergen Data Collection: Pork (Sus scrofa). Internet Symp Food Allergens 2001;3(4):185-192

↩

[213] - Ayuso R, Lehrer SB, Lopez M, Reese G, Ibanez RM, Martin-Esteban M, et al. Identification of bovine IgG as a major cross-reactive vertebrate meat allergen. Allergy 2000;55:348-354

Although beef is a main source of protein in Western diets, very little has been published on allergic reactions to beef or the main allergens implicated in these reactions. The aim was to evaluate the IgE antibody response to beef in suspected meat-allergic subjects and assess cross-reactivity of beef with other vertebrate meats. METHODS: Fifty-seven sera from suspected meat-allergic subjects were tested by grid blot for specific IgE antibodies to vertebrate meats (beef, lamb, pork, venison, and chicken), and the patterns of recognition of meat proteins were assessed by immunoblot studies. RESULTS: A 160-kDa band, identified as bovine IgG, was detected in raw beef in 83% (10/12) of beef-allergic subjects but in only 24% of the beef-tolerant subjects. IgE reactivity to a band of similar mol. mass was detected also in lamb and venison, but rarely in pork or chicken. Complete inhibition of the IgE reactivity to the bovine IgG was obtained with lamb, venison, and milk. IgE reactivity to this band also completely disappeared when beef or lamb extracts were separated under reducing conditions, indicating conformational epitopes. CONCLUSIONS: Bovine IgG appears to be a major cross-reacting meat allergen that could predict beef allergy. Further studies with oral IgG challenges should be performed to document the conclusion that in vitro reactivity correlates with clinical hypersensitivity. The role of bovine IgG in other bovine products such as milk, dander, or hair must also be studied, and the hypothesis that it is a cross-reacting allergen with other mammalian products validated.

↩

[214] - Astwood JD, Leach JN, Fuchs RL. Stability of food allergens to digestion in vitro. Nat Biotechnol 1996;14:1269-1273

One of the concerns regarding the development of genetically modified foods is the introduction of allergenic molecules, predominantly proteins. Prospective testing for allergenic proteins from sources with no prior history of causing allergy is hampered by the absence of suitable techniques and models. Stability to digestion was tested as a candidate physicochemical property for use in distinguishing allergenic proteins from non-allergenic proteins. A simple model of gastric digestion was tested using some major food allergens (peanut Ara h2 and lectin, soybean [beta]-conglycinin subunits, SKTI and Gly m BD 30K, mustard Bra J IE, milk casein and [beta]-lactoglobulin, bovine serum albumin, and several egg proteins). Soybean [beta]-conglycinin was stable for 60 min; in comparison, a non-allergenic protein (spinach RUBISCO) was digested within 15 s. Data support the hypothesis that food allergens must be sufficiently stable to reach the intestinal mucosa where absorption and sensitization can occur. It is concluded that stability to digestion is an important parameter which distinguishes food allergens from non-allergens

↩

[215] - Ofori-Anti AO, Ariyarathna H, Chen L, Lee HL, Pramod SN, Goodman RE. Establishing objective detection limits for the pepsin digestion assay used in the assessment of genetically modified foods. Regul Toxicol Pharmacol 2008;52:94-103

RATIONALE: Guidelines for assessing the potential allergenicity of genetically modified (GM) organisms recommend testing the digestibility of the introduced protein by pepsin. Previous studies detailed the digestion procedure but have not described a simple objective measurement of the extent of digestion nor evaluated the impact of variation in pepsin activity. METHODS: Samples of eight proteins were digested by pepsin at pH 1.2 and 2.0 using standard conditions (10,000 U of pepsin activity per mg test protein) as well as 5000 and 20,000 units per mg of test protein. An independent digestion assay of hemoglobin was used to verify pepsin activity for each assay. Digestion was stopped in timed samples between 0.5 and 60 min. Digestion samples and undigested protein (10% and 100%) were separated by SDS-PAGE. Residual stained protein bands were measured by image analysis. RESULTS: The differences in pH and pepsin concentration only had minor effects on digestion of intermediately stable proteins: concanavalin A, ovalbumin, and lysozyme, but not on rapidly digested or stable proteins. CONCLUSIONS: Verification of pepsin activity and measurement of an objective endpoint of digestion (e.g. (90%) should provide more comparable results for the safety assessment of novel food proteins.

↩

[216] - Thomas K, Aalbers M, Bannon GA, Bartels M, Dearman RJ, Esdaile DJ, et al. A multi-laboratory evaluation of a common in vitro pepsin digestion assay protocol used in assessing the safety of novel proteins. Regul Toxicol Pharmacol 2004;39:87-98

Rationale. Evaluation of the potential allergenicity of proteins derived from genetically modified foods has involved a weight of evidence approach that incorporates an evaluation of protein digestibility in pepsin. Currently, there is no standardized protocol to assess the digestibility of proteins using simulated gastric fluid. Potential variations in assay parameters include: pH, pepsin purity, pepsin to target protein ratio, target protein purity, and method of detection. The objective was to assess the digestibility of a common set of proteins in nine independent laboratories to determine the reproducibility of the assay when performed using a common protocol. Methods. A single lot of each test protein and pepsin was obtained and distributed to each laboratory. The test proteins consisted of Ara h 2 (a peanut conglutin-like protein), beta-lactoglobulin, bovine serum albumin, concanavalin A, horseradish peroxidase, ovalbumin, ovomucoid, phosphinothricin acetyltransferase, ribulose diphosphate carboxylase, and soybean trypsin inhibitor. A ratio of 10U of pepsin activity/microg test protein was selected for all tests (3:1 pepsin to protein, w:w). Digestions were performed at pH 1.2 and 2.0, with sampling at 0.5, 2, 5, 10, 20, 30, and 60min. Protein digestibility was assessed from stained gels following SDS-PAGE of digestion samples and controls. Results. Results were relatively consistent across laboratories for the full-length proteins. The identification of proteolytic fragments was less consistent, being affected by different fixation and staining methods. Overall, assay pH did not influence the time to disappearance of the full-length protein or protein fragments, however, results across laboratories were more consistent at pH 1.2 (91% agreement) than pH 2.0 (77%). Conclusions. These data demonstrate that this common protocol for evaluating the in vitro digestibility of proteins is reproducible and yields consistent results when performed using the same proteins at different laboratories.

↩

[217] - Beretta B, Conti A, Fiocchi A, Gaiaschi A, Galli CL, Giuffrida MG, et al. Antigenic Determinants of Bovine Serum Albumin. Int Arch Allergy Immunol 2001;126:188-195

Background: Bovine serum albumin (BSA) is one of the most widely studied proteins; its structure is well known and its antigenic characteristics have been described in several papers. The aim of this research was the identification of the BSA antigenic determinants. Methods: This study was performed using limited proteolysis and an immunoblotting technique, in which a commercial murine antibody and sera from children sensitized to BSA were used. Results: Findings suggest amino acids (aa) 524-598 as an epitopic area for human species. The most critical sequence seems to be aa 524-542, even if it must be included in a longer fragment to be recognized by antibodies. Murine IgG antibodies also recognize fragments contained in the first half (NH2-terminal portion) of BSA. Conclusions: The results presented in this study indicate that the epitopic sites of an antigenic protein can be different when different species are considered, so that data obtained with antibodies from animal species cannot be directly extrapolated to the behavior of human IgEs.

↩

[218] - Besler M, Fiocchi A, Restani P. Allergen Data Collection: Beef (Bos domesticus). Internet Symp Food Allergens 2001;3(4):171-184

↩

[219] - Fiocchi A, Restani P, Riva E, Restelli AR, Biasucci G, Galli CL, et al. Meat allergy: II--Effects of food processing and enzymatic digestion on the allergenicity of bovine and ovine meats. J Am Coll Nutr 1995;14:245-250

OBJECTIVES: This study was designed to evaluate whether peptic treatment of BSA and OSA affects their allergenicity and to evaluate the effect of technological treatments of meat for infant feeding on the allergenicity of these proteins. SUBJECTS: Twelve children (8 males and 14 females) suffering from atopic dermatitis (AD), aged 12 months to 4.33 years (mean age 2.21 +/- 1.05 years). STUDY DESIGN AND METHODS: Children suffering from atopic dermatitis (AD), (AD), clinically reactive and SPT-positive to beef, underwent skin prick testing (SPT) and radioallergosorbent test (RAST) with BSA and OSA, before and after peptic treatment. They were tested also with commercially available homogenized bovine meat (HBM) and with freeze-dried bovine (FDBM) and ovine (FDOM) meats. Peptic digestion of BSA and OSA was carried out in a Dubnoff's water bath containing 0.05 mg/ml of pepsin. SPT and RAST were performed for 1 mg/ml of BSA and OSA digested 5 minutes, 2 hours and 4 hours with pepsin; homogenized bovine meat, and FDBM and FDOM. SPT results were expressed as diameters (in mm) of the wheal obtained after SPT; a diameter > or = 3 mm was considered as positive. RAST was considered positive for IgE values 5 > UI/ml. RESULTS: SPT to native BSA and OSA were positive in all patients. Only 2 of the 12 children were SPT-positive to HBM, FDBM, and FDOM. After digestion, SPTs and were positive as follows: for BSA, 4/12 after 5 minutes peptic treatment, 2/12 after 2 hours and 2/12 after 4 hours; for OSA, 3/12 after 5 minutes peptic treatment, none after 2 and 4 hours. None of RASTs was positive after peptic attack. CONCLUSIONS: Both proteolytic digestion and technological treatment reduced the allergenic potential of meat products.

↩

[220] - Fiocchi A, Restani P, Riva E, Restelli AR, Biasucci G, Galli CL, et al. Meat allergy: II--Effects of food processing and enzymatic digestion on the allergenicity of bovine and ovine meats. J Am Coll Nutr 1995;14:245-250

OBJECTIVES: This study was designed to evaluate whether peptic treatment of BSA and OSA affects their allergenicity and to evaluate the effect of technological treatments of meat for infant feeding on the allergenicity of these proteins. SUBJECTS: Twelve children (8 males and 14 females) suffering from atopic dermatitis (AD), aged 12 months to 4.33 years (mean age 2.21 +/- 1.05 years). STUDY DESIGN AND METHODS: Children suffering from atopic dermatitis (AD), (AD), clinically reactive and SPT-positive to beef, underwent skin prick testing (SPT) and radioallergosorbent test (RAST) with BSA and OSA, before and after peptic treatment. They were tested also with commercially available homogenized bovine meat (HBM) and with freeze-dried bovine (FDBM) and ovine (FDOM) meats. Peptic digestion of BSA and OSA was carried out in a Dubnoff's water bath containing 0.05 mg/ml of pepsin. SPT and RAST were performed for 1 mg/ml of BSA and OSA digested 5 minutes, 2 hours and 4 hours with pepsin; homogenized bovine meat, and FDBM and FDOM. SPT results were expressed as diameters (in mm) of the wheal obtained after SPT; a diameter > or = 3 mm was considered as positive. RAST was considered positive for IgE values 5 > UI/ml. RESULTS: SPT to native BSA and OSA were positive in all patients. Only 2 of the 12 children were SPT-positive to HBM, FDBM, and FDOM. After digestion, SPTs and were positive as follows: for BSA, 4/12 after 5 minutes peptic treatment, 2/12 after 2 hours and 2/12 after 4 hours; for OSA, 3/12 after 5 minutes peptic treatment, none after 2 and 4 hours. None of RASTs was positive after peptic attack. CONCLUSIONS: Both proteolytic digestion and technological treatment reduced the allergenic potential of meat products.

↩

[221] - Quirce S, Marañón F, Umpierrez A, De las Heras M, Fernández-Caldas E, Sastre J. Chicken serum albumin (Gal d 5) is a partially heat-labile inhalant and food allergen implicated in the bird-egg syndrome. Allergy 2001;56:754-762

BACKGROUND: Chicken serum albumin (alpha-livetin) has been implicated as the causative allergen of the bird-egg syndrome. However, the clinical relevance of sensitization to this allergen has not been confirmed by specific challenge tests and environmental sampling. We investigated whether chicken albumin can be detected in air samples collected in a home with birds, and whether sensitization to this protein may cause respiratory and food allergy symptoms. The heat resistance of chicken albumin and the possible cross-reactivity with conalbumin were also investigated . METHODS: We studied eight patients with food allergy to egg yolk who also suffered from respiratory symptoms (rhinitis and/or asthma) caused by exposure to birds. Sensitization to egg yolk and bird antigens was investigated by skin and serologic tests. Hypersensitivity to chicken albumin was confirmed by specific bronchial, conjunctival, and oral provocation tests . RESULTS: All patients had positive skin tests and serum IgE against egg yolk, chicken serum, chicken meat, bird feathers, and chicken albumin. The presence of airborne chicken albumin in the domestic environment was confirmed. Specific bronchial challenge to chicken albumin elicited early asthmatic responses in six patients with asthma. An oral challenge with chicken albumin provoked digestive and systemic allergic symptoms in the two patients challenged. IgE reactivity to chicken albumin was reduced by 88% after heating at 90 degrees C for 30 min. ELISA inhibition demonstrated only partial cross-reactivity between chicken albumin and conalbumin . CONCLUSION: Chicken albumin (Gal d 5) is a partially heat-labile allergen that may cause both respiratory and food-allergy symptoms in patients with the bird-egg syndrome.

↩

[222] - Kanny G, De Hauteclocque C, Moneret-Vautrin DA. Food anaphylaxis to bovine serum albumin. J Allergy Clin Immunol 1998;101:137-139

↩

[223] - Ayuso R, Lehrer SB, Tanaka L, Ibanez MD, Pascual C, Burks AW, et al. IgE antibody response to vertebrate meat proteins including tropomyosin. Ann Allergy Asthma Immunol 1999;83:399-405

Although meat is a main source of proteins in western diets, little information is available regarding allergy to vertebrate meats or the allergens implicated in these reactions. OBJECTIVE: To evaluate the in vitro IgE antibody response to different vertebrate meats in suspected meat-allergic subjects, as well as the possible role of tropomyosin in meat allergy and to analyze the cross-reactivity between vertebrate meats and the effect of heating on the IgE-binding to meat proteins. METHODS: Fifty-seven sera from suspected meat-allergic subjects were tested by grid blot to extracts of beef, lamb, pork, venison, chicken, and turkey and to four mammalian tropomyosins of different origins. RESULTS: Meat-allergic subjects have IgE antibodies to proteins in different mammalian meats (43/57 subjects); cross-reactivity with avian meat was limited: less than 50% (19/43) of meat positive sera reacted to chicken. In contrast, most of the poultry-positive sera also reacted to different mammalian meats. In general, there was stronger IgE reactivity to raw meats in comparison to cooked meats; an exception was six cases in which IgE reactivity to cooked poultry was stronger. Weak IgE reactivity to tropomyosin was detected in only 2/57 sera tested. CONCLUSIONS: Suspected meat-allergic subjects have serum IgE directed to meat proteins. In vitro cross-reactivity among mammalian meats appears to be important, while cross-reactivity to poultry is limited indicating mammalian-specific proteins. Although cooking in general denatures meat proteins rendering them less allergenic, in some cases the process of cooking may result in the formation of new allergenic moieties. The muscle protein tropomyosin is not an important vertebrate meat allergen.

↩

[224] - Moneret-Vautrin DA, Lemerdy P. Allergie à la viande de canard. Alim'Inter 2007;12:67-68

↩

[225] - Liccardi G, Szepfalusi Z, Noschese P, Nentwich I, D'Amato M, D'Amato G. Allergy to chicken meat without sensitization to egg proteins: A case report. J Allergy Clin Immunol 1997;100:577-579

↩

[226] - Sokolova A, Costa AC, Santos MC, Bartolomé B, Pereira Barbosa M. Severe allergy to poultry meat without sensitisation to egg proteins with concomitant Leguminosae allergy. Case report. Allergol Immunopathol (Madr) 2009;37:168-171

↩

[227] - Zacharisen MC. Severe allergy to chicken meat. WMJ 2006;105:50-52

INTRODUCTION: While allergic reactions to poultry products in the form of feathers and eggs are common, allergic reactions to chicken meat are rare. Despite the popularity of chicken in today's healthy diet, severe reactions after ingesting chicken meat are rarely described. This report describes a patient who developed chicken meat anaphylaxis without experiencing allergy to eggs or feathers. METHODS: A carefully obtained history from a 41-year-old male suggested chicken meat as the cause of his symptoms. He developed abdominal cramping, generalized urticaria, and chest tightness after ingestion of chicken meat. Percutaneous allergy skin testing with commercial chicken and turkey extract and freshly cooked chicken utilizing the prick-prick test was performed. RESULTS: Skin testing was positive with all extracts of chicken and turkey in the patient, and negative in 4 healthy adult controls. Skin tests with feather and egg extract were negative. CONCLUSION: This is the third report of severe allergy to chicken meat in the absence of egg allergy. Physicians should be aware of the presence of chicken allergy without concomitant feather or egg allergy, particularly in adults.

↩

[228] - Fiocchi A, Restani P, Riva E, Mirri GP, Santini I, Bernardo L, et al. Heat treatment modifies the allergenicity of beef and bovine serum albumin. Allergy 1998;53:798-802

The effect of heat on the allergenicity of beef and bovine serum albumin was investigated among 10 toddlers skin prick test (SPT)-positive to raw and cooked beef. The meat-allergy diagnosis was confirmed during double-blind, placebo-controlled food challenge (DBPCFC) with 180 g of beef cooked for 5 min at 100 degrees C. SPT with homogenized and freeze-dried beef, and heated and unheated bovine serum albumin were performed. Both heated and unheated bovine serum albumin, homogenized beef, and freeze-dried beef were used in trial DBPCFC. All children were SPT-positive to unheated bovine serum albumin. Seven were positive to heated bovine serum albumin, one to freeze-dried beef, and none to homogenized beef. DBPCFCs were negative for homogenized beef and freeze-dried beef, positive for unheated bovine serum albumin in five patients, and positive for heated albumin in four children. We conclude that heating reduces sensitization to beef and bovine serum albumin but does not abolish reactivity to albumin under home conditions. However, industrially heat-treated and sterilized homogenized beef and freeze-dried beef may be suitable substitutes in beef-allergic children's diets.

↩

[229] - Donnay C, Barderas R, Kopferschmitt-Kubler MC, Pauli G, de Blay F. Sensitization to pig albumin and gamma-globulin responsible for occupational respiratory allergy. Allergy 2006;61:143-144

↩

[230] - San-Juan S, Lezaun A, Caballero ML, Moneo I. Occupational allergy to raw beef due to cross-reactivity with dog epithelium. Allergy 2005;60:839-840

↩

[231] - Labrecque M, Coté J, Cartier A, Lemière C, Malo JL. Occupational asthma due to pork antigens. Allergy 2004;59:893-894

↩

[232] - Hilger C, Swiontek K, Hentges F, de Blay F, Pauli G. Cross-sensitization to hemoglobin in a case of respiratory allergy to pork and food allergy to chicken meat. 3rd International Symposium on Molecular Allergology, Salzburg, April 18-20, 2008, Poster n°48

↩

[233] - Blaumeiser M, De Blay F, Wagner A, Gonzalez M, Pauli G, Cantineau A. Cutaneous, respiratory and gastrointestinal allergy to bovine serum albumin in a cook. Rev Fr Allergol Immunol Clin 1996;36:54-56

↩

[234] - Leduc V, Demeulemester C, Polack B, Guizard C, Le Guern L, Peltre G. Immunochemical detection of egg-white antigens and allergens in meat products. Allergy 1999;54:464-472

BACKGROUND: The purpose of this study was to detect antigens and allergens in egg-white byproduct ingredients and after their incorporation in processed pork meat pastes. Commercially prepared foods may have potentially allergenic ingredients (egg, milk, soybean, wheat, and peanut) added in processing. Since allergic patients may react to unidentified ingredients, it is important to assess the allergenic potency of these food proteins added during processing. Egg white was chosen as an experimental model, since egg is one of the most prevalent allergens in food hypersensitivity. METHODS: Experimental pork meat pastes containing egg white underwent pasteurization and sterilization. Ingredients derived from egg-white or paste extracts were isoelectrofocused and then blotted onto cyanogen bromide-activated nitrocellulose membranes. Egg-white antigens were identified in ingredients and in meat products with rabbit anti-egg-white antiserum by isoelectric focusing immunoblotting. Allergens were identified with sera from sensitized patients. A sensitive ELISA test was developed to detect egg-white proteins in raw, pasteurized, and sterilized meat products. RESULTS: Antigens and allergens in four egg-white byproducts were detected. Egg-white antigens were detectable in all ingredients and meat pastes by ELISA. Allergens were detected in ingredients and in raw and pasteurized products by immunoprint techniques and ELISA. CONCLUSIONS: Masked egg-white allergens are recognized by human serum IgE after pasteurization. Egg-white antigens are detectable in sterilized meat by ELISA techniques. Ingestion of processed foods could entail a risk of allergic reactions for sensitized consumers.

↩

[235] - Belloque J, Garcia MC, Torre M, Marina ML. Analysis of soybean proteins in meat products: a review. Crit Rev Food Sci Nutr 2002;42:507-532

The use of soyabean proteins as meat extenders has spread significantly due to the interesting nutritional and functional properties that are present in soyabean proteins. Together with these, health and economical reasons are the major causes for the addition of soyabean proteins to meat products. Nevertheless, despite the good properties associated to soyabean proteins, there are many countries in which the addition of these proteins is forbidden or in which the addition of soyabean proteins is allowed up to a certain extent. Thus, the need of analytical methods enabling the detection of added soyabean proteins in meat products is obvious. Microscopic, electrophoretic, immunologic, and chromatographic methods are the most widely used for this purpose. However, the detection of soyabean proteins in meat products presents difficulties related to the composition (meat species, meat quality, soyabean protein source, presence of other non-meat proteins, etc.) and the processing of the meat products, and, although these analytical methods have tried to overcome all these difficulties, there is still not a method enabling quantitative assessment of soyabean proteins in all kinds of meat products.

↩

[236] - Armentia A, Martin-Gil FJ, Pascual C, Martin-Esteban M, Callejo A, Martinez C. Anisakis simplex allergy after eating chicken meat. J Investig Allergol Clin Immunol 2006;16:258-263

BACKGROUND: Allergic reactions to food can be produced by contaminants that induce sensitization. Among these, Anisakis simplex can cause seafood infestation, and allergic symptoms (urticaria-angioedema, anaphylaxis, and asthma) can follow the eating or handling of affected fish. Although seafood is the principal source of human infections by this parasite, we have found allergic symptoms in 8 patients previously diagnosed as having A simplex sensitization after they ate chicken meat. Chicken feed usually has a high proportion of fishmeal, which might possibly be contaminated by this nematode. OBJECTIVE: The aim of our study was to determine whether parasite proteins present in chicken meat could be responsible for the symptoms reported by these subjects. METHODS: We carried out in vivo tests (prick, bronchial challenge, and double-blind placebo-controlled challenge with meat chicken) in these 8 patients. We performed immunoblotting using the sera from the 8 patients and controls in order to detect A simplex sensitization. We also investigated the presence of A simplex proteins in sera from chickens fed with fishmeal and in other sera from chickens fed only with cereals. We excluded sensitization to other chicken nematodes by serologic methods. RESULTS: All 8 patients presented positive prick and challenges to A simplex. When we used serum from chickens fed with fishmeal as the antigen in blotting, patients 3, 4, 5, 6, 7, and 8 recognized a band of 16 kd, also obtained when using pools of fish-shellfish and A simplex larva. No detection was observed with sera from chickens fed with only cereals. CONCLUSION: We provide evidence, based on in vivo and in vitro tests, that subjects highly sensitized to A simplex can detect the presence of Anisakis species allergens in chicken meat.

↩

[237] - Bobolea ID, Barranco P, Pedrosa M, Quirce S. Allergy To Dry Fermented Sausage: A Case Report. J Allergy Clin Immunol 2009;123:S249

RATIONALE: Adding moulds to typical foods such as dry sausages or French cheese in order to enrich the flavour is common in Central and Southern Europe. Occupational respiratory allergy in food industry workers is well documented, but food allergy to moulds is uncommon. METHODS:We report the case of a 24-year old male, diagnosed with allergic rhinoconjunctivitis and asthma. During the last year he had experienced two episodes of facial angioedema immediately after ingestion of a dry sausage, tolerating any other meat products .We performed skin prick tests (SPTs) to aeroallergens, meats and other foods, prick-prick with the outer skin and the meat of the suspected sausage, total and specific IgE, a microbiological analysis and culture of the sausage‚s skin, and a mucosal open provocation (a brief contact of the outer skin with the lower lip). RESULTS: SPTs were positive to grass pollen, dust mites and moulds (Alternaria, Penicillium, Mucor spp), and negative to the food allergens tested. The prick-prick was positive with the sausage skin (7 mm) and negative with the meat. Specific IgE (CAP kU/L) results: Alternaria alternata 58, Mucor racemosus 2.67, and Penicillium notatum 3.03. Penicillium and Mucor spp colonies grew in the skin cultures. The mucosal provocation yielded positive: in 5 minutes the patient developed angioedema of the lips, tongue and uvula, symptoms that subsided within 2 hours after treatment with antihistamines and systemic corticosteroids. CONCLUSIONS: We demonstrated an IgE-mediated allergy to the isolated moulds as the responsible mechanism for this unusual type of food allergy.

↩

[238] - Morisset M, Parisot L, Kanny G, Moneret-Vautrin DA. Food allergy to moulds: two cases observed after dry fermented sausage ingestion. Allergy 2003;58:1203-1204

↩

[239] - Bidat E. Allergie alimentaire à Penicillium, une allergie fréquente ? Alim'Inter 2002;7:24-25

↩

[240] - Guillet MH, Kauffmann-Lacroix C, Dromer F, Larsen C, Guillet G. Urticaire et choc anaphylactique par allergie alimentaire à Penicillium italicum. Rev Fr Allergol Immunol Clin 2003;43:520-523

Un malade aux antécédents de crises d'asthme dans les rayons de fromagerie développe trois épisodes d'urticaire et de choc anaphylactique par allergie alimentaire à une moisissure contaminant la peau et la chair de saucisse et la tomme de Savoie. Les seuls tests cutanés positifs concernent la peau de la saucisse ainsi que la chair et la tomme de Savoie sur lesquels est identifié Penicillium italicum. Les tests sanguins confirment la sensibilisation à Penicillium au taux de 6,36 KU/l. Le complément de bilan allergologique ne montrait pas d'autres allergies à d'autres fromages ni à la pénicilline. La responsabilité de cette moisissure est vraisemblablement sous estimée en cas de présomption d'allergie aux saucisses et fromage quand il s'agit d'allergie alimentaire alors qu'elle est généralement prise en compte en cas de manifestations respiratoires.

↩

[241] - Cahen YD, Fritsch R, Wüthrich B. Food allergy with monovalent sensitivity to poultry meat. Clin Exp Allergy 1998;28:1026-1030

BACKGROUND: Allergy to poultry meat is only rarely covered in science. The few reports are usually related to patients allergic to eggs or bird feathers. OBJECTIVE: Two patients with a clear history of monovalent, ingestive allergy to chicken and turkey meat, without other food allergies, were analysed. The relevant allergens were to be identified by immunoblotting. METHODS: Both patients were evaluated with skin tests and specific IgE determination (CAP). Allergens were identified by SDS-PAGE and immunoblotting. Cross-reactivity of chicken and turkey meat was examined by IgE inhibition experiments. RESULTS: Skin tests and specific IgE were positive for chicken and turkey in both patients. Cross-reactivities to other poultry meats were documented for duck and goose meat. No sensitization to egg components or poultry feathers could be found. Allergenic proteins of poultry meat were detected at molecular weights of 21, 23 and 50 kDa (distinct bands) and 13, 27 and 33kDa (faint bands). An additional band at 91 kDa for turkey, can probably not be considered a distinct allergenic epitope. Immunoblot inhibition confirmed cross-reactivity of chicken and turkey meat allergens. CONCLUSION: Food allergy to poultry meat is a distinct disorder with crossreactivity among chicken, turkey and other poultries. The relevant allergens were identified by immunoblotting. Associated food allergy to egg-components is unlikely as the patients were able to tolerate egg and eggs products.

↩

[242] - Escudero C, Cuesta J, Bartolomé B, de Miguel J, Compés E, de las Heras M, et al. Avian meat as a hidden allergen: double blind, placebo controlled, oral challenge study. EAACI 22th Congress, Paris, 7-11 June, 2003, Poster n°139

Chicken meat is a fundamental food in our diets. However, the food allergy to this food has been scantly documented and generally, into the context of the „bird-egg syndrome‰. Case report: 22-year-old man without personal history of atopy and family history of hay fever. He was refereed oral syndrome after the ingestion of frankfurter and foie gras that contains small amounts of avian meats. Moreover, he experienced oral syndrome, nausea, vomits and abdominal pain immediately after the ingestion of cooked chicken meat. He developed similar symptoms after the ingestion of turkey, duck, quail, partridge and pheasant meats. He could eat egg and mammalian meats, and he hadn‚t exposed to birds. He experiences oral itching after the ingestion of chickpea, kidney bean and lentil. The causative role of avian meats in the anaphylactic response of the patient was investigated by immunologic and double blind, placebo controlled, oral challenge tests (DBPCOC). Skin prick tests (SPT) were performed with a panel of foods. We obtained positive responses with chicken meat. SPT with raw chicken and turkey meats, performed by the prick-prick method, were positive. SPT with egg (egg white, egg yolk, ovalbumin, ovomucoid, conalbumin, and lysozyme), chicken albumin and feathers mixture were negative. Specific IgE were determined by CAP System (Pharmacia, Sweden). Specific IgE determinations to avian meats were positive (chicken 2.95; turkey 0.96 kU/L). Oral challenge with frankfurter that contains chicken meat was positive. DBPCOC with an accumulative dose of 3 gr. of chicken meat reproduced the symptoms. Placebo was prepared with green vegetable puree and cooked cow meat. Conclusion: Small amounts of poultry meat may be present in frankfurters and other foodstuffs and cause anaphylactic reactions in sensitised patients. We could demonstrate by means of skin tests, IgE determinations and DBPCOC that chicken meat caused anaphylaxis in the patient through an IgE-dependent mechanism. Crossreactive among various avian meats is clinically suggestive.

↩

[243] - Restani P, Ballabio C, Tripodi S, Fiocchi A. Meat allergy. Curr Opin Allergy Clin Immunol 2009;9:265-269

PURPOSE OF REVIEW: This review summarizes the scientific evidence on meat allergy, an unusual disorder, whose prevalence in some European countries (such as Italy) may be increasing. RECENT FINDINGS: Data reported in this review underline some interesting points: in meats rarely consumed, such as kangaroo, whale and seal, the main allergens are only partially correlated to those detected in beef or other usually consumed meats; cross-reactivity and cross-contamination are critical aspects, which should be seriously considered by allergologists. SUMMARY: Meat allergy is normally outgrown during the first years of life, so that it is rare in adults. Beef among mammals and chicken among birds are most frequently involved. The major allergens are serum albumins and immunoglobulins, but there are a few reports of allergies to muscle proteins (actin, myosin and tropomyosin). As meat allergenicity can be reduced by various treatments (heat, homogenization and freeze-drying), the consumption of meat derivatives by children allergic to meat proteins is often permitted. Cross-reactivity has been described between different meats, between meat and milk or eggs and between meat and animal dander. There are some reports of cross-contamination associated with the inadequate cleaning of industrial or butchers' equipment. All these aspects may have serious implications for clinical practice.

↩

[244] - Médicaments à base de porc ou de bœuf. Alim'Inter 2007;12:89-90

↩

[245] - Fiocchi A, Bouygue GR, Restani P, Bonvini G, Startari R, Terracciano L. Accuracy of skin prick tests in IgE-mediated adverse reactions to bovine proteins. Ann Allergy Asthma Immunol 2002;89(6 Suppl. 1):26-32

OBJECTIVES: To review the recent literature on the diagnostic accuracy of skin prick tests (SPTs) in pediatric food allergy, focusing on adverse reactions to milk and beef. To present data about the test performance characteristics of beef extracts used in SPTs among children with atopic dermatitis (AD) reporting immediate hypersensitivity to beef. DATA SOURCES: MEDLINE search using the following algorithm ["skin prick test" AND "food allergy" OR allergen; 1997-2002; English; all children]. Prospective sensitivity study of SPTs in 34 patients. STUDY SELECTION: Thirty-four children with AD (median age 2.29 years) were consecutively recruited between 1992 and 2000 because of immediate reactions to beef. On double-blind, placebo-controlled food challenges (entry criterion), 20 of the patients reacted to beef and 14 did not. Cut-off points for skin prick test wheal positivity was selected by receiving-operator characteristic analysis for fresh and commercial beef allergens. Sensitivity and specificity of skin tests and indices of reproducibility were calculated. RESULTS: In the literature, the positive predictive accuracies of skin prick tests vary between 69 and 100% and the negative predictive accuracies between 20 to 86% for cow's milk. In our series, SPTs with commercial beef extracts were highly diagnostic (100% sensitivity; 10% false positive rate) and SPTs with fresh beef were highly specific (100%), albeit with a false-positive rate of 21.42%. CONCLUSIONS: From the literature, we conclude that the diagnostic accuracy of SPTs with milk should be reappraised in the workup of cow's milk allergy. Carrying out commercial and fresh food SPTs at the same time substantially reduces costs and diagnostic work. Oral provocation is necessary in 20.68% of children with AD who have immediate symptoms to beef. Greater allergen standardization and streamlining of the workup of cow's milk allergy are desirable future goals

↩

[246] - Werfel SJ, Cooke SK, Sampson HA. Clinical reactivity to beef in children allergic to cow's milk. J Allergy Clin Immunol 1997;99:293-300

↩

[247] - Moneret-Vautrin DA, Lemerdy P. Allergie à la viande de canard. Alim'Inter 2007;12:67-68

↩

[248] - Fritsche P, Theler B, Ballmer B. Meat allergy in Switzerland. Allergy 2007;62(suppl. 83):356-357

Background: A study published in 1996 reported an incidence of meat allergy of 8.2% among patients with IgE-dependent food allergies. Objective: The aim of this study was to investigate the clinical characteristics of meat allergy and to validate the routine diagnostic tools. Methods: We have recruited within the framework of the EU-project REDALL patients with a positive case history of meat allergy. Definitive inclusion criteria were either a history of an anaphylactic reaction to meat or a positive titrated double-blind placebo-controlled food challenge with the incriminated meat. Sensitisation to meat was assessed in all patients by prick-prick-testing with native meats and in vitro determination of specific IgE to pork, beef and chicken (CAP-FEIA). Results: From 2/2003 to 6/2005 we have identified twelve patients with a positive case history of a meat allergy to either chicken (n=6), beef (n=5), pork (n=6), horse (n=1), sheep (n=1), bunch (n=1), turkey (n=1), veal (n=1), duck (n=1) or lamb (n=2), respectively. The mean age of those patients was 30.8 years (range 2 to 55). Meat allergy associated symptoms as reported by the patients ranged from contact urticaria of the oral mucosa (OAS) to anaphylactic reactions. Of these twelve patients only six could be definitively included into the study either on the basis of a case history of an anaphylactic reaction (n=3) or a positive DBPCFC (n=3). Skin testing with the responsible meat was positive in three out of six patients, and in vitro determination of specific IgE in three out of five patients. Under DBPCFC two patients responded with either urticaria or dysphagia and nausea at 2.6g and 26.4g of chicken, respectively and another patient with urticara after ingestion of 0.9g beef. Conclusion: Meat allergy seems to be an uncommen food allergy in Switzerland. Meat induced symptoms range from OAS to severe anaphylactic reactions. The routine-diagnostic tools, i.e. skin testing and in vitro determination of specific IgE had a low sensitivity among our patients.

↩

[249] - Martelli A, De Chiara A, Corvo M, Restani P, Fiocchi A. Beef allergy in children with cow's milk allergy; cow's milk allergy in children with beef allergy. Ann Allergy Asthma Immunol 2002;89(6 Suppl. 1):38-43

OBJECTIVE: To review the literature on the prevalence of beef allergy in children allergic to cow's milk and to report a series of patients with beef allergy evaluated for cow's milk allergy. DATA SOURCES: A MEDLINE search for cow's milk allergy and beef allergy was conducted. Also included in this report is a clinical evaluation of both these entities in a population of children with atopic dermatitis. STUDY SELECTION: Data from the literature were summarized. Recruited patients with beef allergy were evaluated on the basis of history, serology, skin prick tests, and double-blind, placebo-controlled food challenge (entry criterion), and presented between 1992 and 2000. RESULTS: In the literature, between 13 and 20% of children with cow's milk allergy also have beef allergy. In our personal series of patients, 28 children (18 boys and 10 girls) diagnosed with beef allergy underwent skin prick tests and double-blind, placebo-controlled food challenge, which showed that 26 (92.9%) were allergic to cow's milk. Two children nonallergic to cow's milk were the only ones who were not sensitized to bovine serum albumin. CONCLUSIONS: Most children with beef allergy are also allergic to cow's milk and should avoid the consumption of dairy products. Sensitization to bovine serum albumin is a marker of cow's milk allergy in children with beef allergy. Elimination of beef from the diet of children with cow's milk allergy should be evaluated on an individual basis after diagnostic workup.

↩

[250] - Restani P, Ballabio C, Tripodi S, Fiocchi A. Meat allergy. Curr Opin Allergy Clin Immunol 2009;9:265-269

PURPOSE OF REVIEW: This review summarizes the scientific evidence on meat allergy, an unusual disorder, whose prevalence in some European countries (such as Italy) may be increasing. RECENT FINDINGS: Data reported in this review underline some interesting points: in meats rarely consumed, such as kangaroo, whale and seal, the main allergens are only partially correlated to those detected in beef or other usually consumed meats; cross-reactivity and cross-contamination are critical aspects, which should be seriously considered by allergologists. SUMMARY: Meat allergy is normally outgrown during the first years of life, so that it is rare in adults. Beef among mammals and chicken among birds are most frequently involved. The major allergens are serum albumins and immunoglobulins, but there are a few reports of allergies to muscle proteins (actin, myosin and tropomyosin). As meat allergenicity can be reduced by various treatments (heat, homogenization and freeze-drying), the consumption of meat derivatives by children allergic to meat proteins is often permitted. Cross-reactivity has been described between different meats, between meat and milk or eggs and between meat and animal dander. There are some reports of cross-contamination associated with the inadequate cleaning of industrial or butchers' equipment. All these aspects may have serious implications for clinical practice.

↩

[251] - Malandain H, Giroux F, Cano Y. The influence of carbohydrate structures present in common allergen sources on specific IgE results. Eur Ann Allergy Clin Immunol 2007;39:216-220

BACKGROUND: Cross-reactive carbohydrate determinants (CCD) are well known interferants in specific IgE assays (sIgE). Glyco-epitopes are not restricted to CCD and extracts used to prepare in vitro tests contain many other glycoproteins able to bind glycan-specific IgE. The overall amounts of IgE-bindable glycan structures in allergen sources are unknown . OBJECTIVE: We aimed at quantifying the influence of N-glycan structures on IgE reactivity to commonly tested allergen sources . METHODS: IgE reactivity to 51 allergen extracts, one purified natural allergen and 10 recombinant allergens was measured on Phadia UniCAP system using 2 sera demonstrating significant levels of glycan-related IgE reactivity. Immobilized bromelain and horseradish peroxidase (HRP) were used to capture N-glycan-specific IgE from these sera. Residual IgE reactivity was measured for 42 allergen sources and 4 recombinant/purified allergens . RESULTS: An obviously excessive number of positive CAP-results were obtained with both sera, especially for plant-based allergen sources. Capture of glycan-specific IgE led to a decrease of serum IgE ractivity, variable among allergen sources and between sera. Among others, peanut results were proven largely interfered by the presence of glycan-specific IgE. Unexpectedly some allergen sources showed a slight influence of glycan-related reactivity, such as cockroach, mosquito, mussel, shrimp and domestic mites . CONCLUSION: In patients sensitized to pollens or to Hymenoptera venoms sIgE results should be interpreted with caution. One cannot substract the result of a glyco-reporter test (bromelain and/or HRP) in order to compute glycan-free slgE results for common allergen sources like peanuts. As long as the demonstration of a significant role for glycan structures in clinical allergic reactions is lacking, a simple pre-treatment able to discard glycan-specific IgE from serum would be useful to improve accuracy of in vitro diagnostic tests.

↩

[252] - Hilger C, Grigioni F, Thill L, Mertens L, Hentges F. Severe IgE-mediated anaphylaxis following consumption of fried frog legs: definition of a alpha-parvalbumin as the allergen in cause. Allergy 2002;57:1053-1058

BACKGROUND: IgE-mediated allergic reactions to bullfrog and edible frog have been reported. The implicated allergens have not been defined so far. The frog material and the patient's serum from a case of severe food-induced anaphylaxis were used to define the implicated allergen at the protein and DNA level . METHODS: Immunoblotting techniques and N-terminal protein microsequencing were used to define the allergen recognized by the patient's serum. Back translation from the identified protein sequence was used to design degenerated primers to amplify the allergen's cDNA by polymerase chain reaction (PCR). We defined the nucleotide sequence of the allergen from the frog of Indonesian origin that was consumed by the patient, and the homologous cDNA from Rana esculenta . RESULTS: Protein microsequencing revealed that the implicated frog allergen belonged to the parvalbumin family. cDNAs coding for alpha- and beta-parvalbumin of R. esculenta and Rana species were cloned. Recombinant proteins were expressed in Escherichia coli. The patient's serum IgE antibodies recognized parvalbumin prepared from frog muscle and recombinant alpha-parvalbumin from R. species but not from R. esculenta. Recombinant beta-parvalbumin was not recognized by the IgE antibodies . CONCLUSION: This work defines at the protein and DNA levels alpha-parvalbumin as the allergen implicated in a case of IgE-mediated anaphylaxis to frog muscle. It also shows that a protein belonging to the parvalbumin family is implicated in type I allergies outside the fish species.

↩

[253] - Romano C, Ferrara AM, Cislaghi C, Falagiani P. Food allergy to frog. Allergy 2000;55:584-585

↩

[254] - Romano C, Ferrara AM, Cislaghi C, Falagiani P. Food allergy to frog. Allergy 2000;55:584-585

↩

[255] - Ma Y, Breiteneder H, Fernandez-Rivas M, Hoffmann-Sommergruber K. Cross-reactivity of codfish and edible frog parvalbumins: cloning and expression. EAACI 25th Congress, Vienna, 10-14 June, 2006, Poster n°521

Background: Fish is a valuable part of human nutrition. However, fish allergy is very well documented affecting children as well as adults. Parvalbumin, the major allergen, has been found in many species of fish, shellfish, and frog. There are two distinct phylogenetic lineages of parvalbumins, alpha and beta, and so far most allergic reactions are caused by the beta parvalbumins. Most of the fish species described as allergenic express only beta parvalbumin. The aim of this study was to establish cDNAs encoding parvalbumin and subsequently to generate recombinant proteins, which could allow the study of molecular cross-reactivity between codfish and edible frog parvalbumins and between alpha and beta parvalbumins. Methods: Total RNA was isolated from codfish (Gadus morhua) and edible frog (Rana macrodon), respectively. Five µg each were used for cDNA synthesis. Gene-specific primers were designed according to the published N-terminal sequences of parvalbumin, RT-PCR performed and the PCR products cloned, sequenced and subcloned into the E. coli expression vector pET-17b. Results: Two full length clones coding for b-type parvalbumins were obtained from codfish. In addition, one clone coding for a- and b-parvalbumin from frog was obtained, respectively. The difference of the deduced b-parvalbumin amino acid sequences among codfish and frog is in the range of 35-38%. The amino acid sequence identity between b-parvalbumins from codfish is 71%, and between a- and b-parvalbumins from frog is 52%. Conclusions: The cloning of two distinct parvalbumin cDNAs from codfish and frog demonstrates the presence of at least two b variants in codfish and at least one a and one b variant in frog. Parvalbumins, are major cross-reactive allergens among different fish and frog species with high sequence identities and may share IgE binding epitopes.

↩

[256] - Hilger C, Thill L, Grigioni F, Lehners C, Falagiani P, Ferrara A, et al. IgE antibodies of fish allergic patients cross-react with frog parvalbumin. Allergy 2004;59:653-660

BACKGROUND: The major allergens in fish are parvalbumins. Important immunoglobulin (Ig)E cross-recognition of parvalbumins from different fish species has been shown. Recently frog parvalbumin alpha has been found to be responsible for a case of IgE-mediated anaphylaxis triggered by the ingestion of frog meat. The aim of this study was to investigate whether IgE antibodies of fish allergic persons cross-react with frog parvalbumin and to appreciate its clinical relevance . METHODS: The sera of 15 fish allergic patients and one fish and frog allergic patient were tested by IgE-immunoblotting against frog muscle extract. Sera were tested against recombinant parvalbumin alpha and beta from Rana esculenta. Skin prick tests were performed in selected patients with recombinant frog parvalbumin. Ca(2+) depletion experiments and inhibition studies with purified cod and frog recombinant parvalbumin were done to characterize the cross-reactive pattern . RESULTS: Fourteen of the sera tested had IgE antibodies recognizing low molecular weight components in frog muscle extract. Calcium depletion experiments or inhibition of patient sera with purified cod parvalbumin led to a significant or complete decrease in IgE binding. When tested against recombinant parvalbumins, three of 13 sera reacted with alpha parvalbumin and 11 of 12 reacted with beta parvalbumin from R. esculenta. Skin prick tests performed with recombinant frog parvalbumin were positive in fish allergic patients. Inhibition studies showed that a fish and frog allergic patient was primarily sensitized to fish parvalbumin . CONCLUSION: Cod parvalbumin, a major cross-reactive allergen among different fish species, shares IgE binding epitopes with frog parvalbumin. This in vitro cross-reactivity seems to be also clinically relevant. Parvalbumins probably represent a new family of cross-reactive allergens.

↩

[257] - Boyle RJ, Russo VC, Andaloro E, Mehr SM, Tang MLK. Anaphylaxis to kangaroo meat – identification of a new marsupial allergen. Allergy 2007;62:209-210

↩

[258] - Bourne HC, Restani P, Moutzouris M, Katelaris CH. An unusual pattern of meat allergy. Allergy 2005;60:706-707

↩