Graines : généralités

[1] - Helm RM. Allergy to plant seed proteins. J New Seeds 2001;3(3):37-60

Allergenicity is defined as the ability of proteins and other agents to sensitize genetically predisposed individuals to develop IgE antibodies, which bind to mast cells and basophils through the Fc portion of the IgE antibody. Upon subsequent exposures to the same protein, the proteins (allergens) bind to and cross-link cell bound IgE stimulating the release of mediators (histamine) that lead to an allergic reaction (immediate hypersensitivity). Seed proteins represent one important class of proteins that can induce a variety of allergic syndromes. Aerosolized particles released during pollination, harvest, transport and storage of grains and seed crops can cause inhalant allergy in susceptible individuals. Increased use of cereal grains, legumes and nuts in the diet has been suggested to contribute to the rise in the prevalence of food allergies. Plant biotechnology affords unique opportunities to identify individual components of seeds or seed products that may cause allergies and to remove or alter allergens from the food source, so that the food can be consumed safely by allergic individuals. These topics are highlighted to provide insight into the risks and benefits attributed to seed proteins. 100 ref

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

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[3] - Malandain H, Lavaud F. Allergénicité des protéines de défense végétale. Rev Fr Allergol Immunol Clin 2004;44:469-475

La synthèse de protéines de défense fait partie des réponses biochimiques que les plantes ont développées pour lutter contre leurs ennemis naturels et contre les stress environnementaux. De nombreuses protéines de défense végétale sont allergisantes : chitinases, protéines de transfert lipidique LTP, protéines Bet v 1-like. Cet article rappelle les principales familles de protéines de défense végétale, leur impact allergique et l'effet de certains procédés agricoles ou technoalimentaires sur l'allergénicité des aliments végétaux.

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[4] - Guéguen J, Lemarié J. Composition, structure et propriétés physicochimiques des protéines de légumineuses et d'oléagineux. in "Protéines végétales", Godon B., Lavoisier Technique et Documentation, Paris 1996, pp.81-118

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[5] - Malandain H. Familles moléculaires des principaux aliments végétaux allergisants. Alim'Inter 2003;8:78-84

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[6] - Frémont S, Sanchez C, Errahali Y, Mouécoucou J, Metche M, Méjean L, et al. Allergénicité alimentaire: importance des interactions protéines-lipides et protéines-polysaccharides. Alim'Inter 2003;8:35-41

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[7] - Grimshaw KEC, King RM, Nordlee JA, Hefle SL, Warner JO, Hourihane JOB. Presentation of allergen in different food preparations affects the nature of the allergic reaction – a case series. Clin Exp Allergy 2003;33:1581-1585

BACKGROUND: Characterization of fatal and non-fatal reactions to food indicates that the majority of reactions are due to the ingestion of prepared foods rather than the non-processed allergen. In an ongoing study that used a double-blind placebo-controlled food challenge to investigate peanut allergy and clinical symptoms, the observed reaction severity in four of the first six subjects was greater than anticipated. We hypothesized that this was due to differences in the composition of the challenge vehicle . OBJECTIVE: The aim was to investigate whether the severity of observed challenge reactions would be repeated on re-challenge with a lower fat challenge vehicle . METHODS: Peanut-allergic subjects were re-challenged with a lower fat recipe after reacting more severely than was anticipated to an initial peanut challenge. Similar challenge vehicle recipes were used, the only difference being the lower fat content (22.9% compared with 31.5%). The peanut content of the two recipes was analysed using RAST inhibition studies and ELISA tests . RESULTS: Three of four subjects reacted to much smaller doses of peanut protein on re-challenge (mean dose equivalence - 23 times less peanut) with the lower fat recipe. RAST inhibition showed that neither recipe altered epitope recognition. The higher fat recipe required twice as much peanut to cause 50% inhibition. ELISA detected far lower levels of peanut in the higher fat recipe (220 000 parts per million (p.p.m.)) than in the lower fat recipe (990 000 p.p.m.) . CONCLUSION: The fat content of a challenge vehicle has a profound effect on the reaction experienced after allergen ingestion. This is another factor to be considered in assessing the risk of certain foods to food-allergic consumers and adds another dimension to clinical, research and regulatory practice.

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[8] - van Odijk J, Bengtsson U. The fat content may affect the reaction pattern in double blind placebo controlled food challenges for hazelnut. Allergy 2007;62(suppl. 83):105

Background: Few studies have been performed regarding how nutrient composition, for example the fat content, may affect the outcome of the allergic reaction. To test the allergenicity of products with different fat contents, patients with a lower risk of severe reactions, for example birch pollen allergic patients with oral allergy syndrome to hazelnuts, may be involved. The aim was to study if the fat content in blinded food challenges to hazelnut affects the reaction pattern in birch pollen allergic patients with reported oral allergy syndrome to hazelnut. A secondary aim was to develop 2 recipes with different fat content that was documented blind by panels using a triangle test. METHODS: Two recipes containing the same amount of hazelnut but different content of fat were developed and tested on a panel of 24 subjects with triangle tests. The fat recipe contained 28.5 % of fat and the low-fat recipe 8.5 % of fat. The recipes were tested on separate blinded food challenges on 15 patients with documented birch pollen allergy and a history of oral allergy syndrome to hazelnuts. Onset and severity of symptoms were tested using a stopwatch and a VAS-scale. RESULTS: Both recipes were regarded equal regarding taste and texture as tested by the taste panels. All 15 subjects reacted to hazelnut challenge within 7.5 minutes as expected with itching in the oral cavity and swollen feeling of tongue and lips (oral allergy syndrome), regardless of fat content. All reactions terminated within 25 minutes. Twelve out of 15 subjects reacted with a shorter onset of symptoms when challenged with the low-fat recipe (p< 0.03). For 2 subjects, the onset was shorter for the fat recipe, and one subjects reacted within the same time range for both recipes (difference less than 5 seconds). There was a wider range of reactions reported by VAS scale to the fat recipe compared to non-fat recipe. There was no correlation between severity of symptoms (measured by VAS scale) and specific IgE level to birch or hazelnut. There seems to be a delayed reaction pattern to high fat hazelnut challenges in birch pollen allergic patients. This result is in line with earlier studies on peanut challenges and may reflect the role of food composition in allergic reactions.

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[9] - Frémont S, Errahali Y, Bignol M, Metche M, Nicolas JP. What about the Allergenicity of Vegetable Oils ? Internet Symp Food Allergens 2002;4(2):111-118

Cases of allergy to peanut, sunflower seed, soybean and sesame seed oils have been reported in the literature, although some authors have claimed that these oils are not allergenic. The aim of this article is to review this subject, to describe the processing methods to which the seeds are subjected during the extraction of their oil, to recall that oils do not consist solely of triglycerides and to describe the findings of our studies. The allergenicity of oils is a frequent subject of controversy and the bibliography constantly produces contradictory examples. This can be explained by the variability of the processes used in industry, and by the conditions under which proteins are extracted in the laboratory.

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[10] - Bessot JC. Allergènes végétaux non polliniques. Rev Fr Allergol Immunol Clin 2003;43:40-52

L'inventaire des allergènes végétaux non polliniques s'est considérablement élargi au cours des 12 dernières années. Ces allergènes, initialement répertoriés dans l'environnement professionnel peuvent aussi être rencontrés dans l'environnement domestique. Certains d'entre eux se comportent à la fois comme des pneumallergènes ou des trophallergènes. Dans cette revue générale, seront envisagés la prévalence, les mécanismes, les aspects cliniques, la démarche diagnostique des allergies aux gommes végétales, aux graines, aux racines, aux feuilles et aux plantes d'intérieur. Le rôle des allergènes du latex, des bois, des farines, des enzymes végétales ne sera pas traité ici. Les gommes végétales (arabique, karaya, guar, psyllium...) provoquent des rhinites ou des asthmes IgE médiés, bien que leurs allergènes soient des polysaccharides. La colophane fait partie des 5 allergènes le plus souvent responsables d'asthmes professionnels en Grande-Bretagne. Parmi les graines, le rôle des graines provenant de céréales, du café, du ricin, du soja sera privilégié. Parmi les racines, certaines plantes médicinales (sanyak, bahna, salsepareille...) ont une importance croissante. Le henné, le tabac, le thé, le lycopode sont aussi des sources d'allergènes. Des allergies IgE dépendantes ont été décrites pour le ficus, mais aussi pour d'autres plantes d'appartement. Certaines étiologies, se limitant actuellement à un ou quelques cas publiés, peuvent annoncer des pathologies allergiques émergentes.

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[11] - Moneret-Vautrin DA, Morisset M, Lemerdy P, Croizier A, Kanny G. Food allergy and IgE sensitization caused by spices: CICBAA data (based on 589 cases of food allergy). Allerg Immunol (Paris) 2002;34:135-140

BACKGROUND: Spices originate in various botanical families: Apiaceae, Lamiaceae, Lauraceae, Leguminosae, Liliaceae, Myristicaceae, Myrtaceae, Piperaceae, Solanaceae, Zingiberaceae.... METHODOLOGY: Prick-tests to native spices have been carried out in patients suspected of food allergies to spices. The CICBAA data bank includes 589 cases of food allergies, a part of which has benefited from investigations for spices. Data about the rate of sensitization and food allergy are available. RESULTS: Frequent sensitization to Apiaceae is observed: coriander, caraway, fennel, celery: 32% of prick-tests in children, 23% of prick-tests in adults. Sensitization to Liliaceae: garlic, onion, chive, is observed in 4.6% of prick-tests in children, 7.7% of prick-tests in adults. Rare cases of sensitization to paprika and saffron are recorded. Prick-tests to nutmeg, ginger and clove are currently negative. 10 food allergies related to the mugwort-celery-spices syndrome are reported: coriander: 1, caraway: 2, fennel: 3, garlic: 3, onion: 1. Food allergy to spices is unfrequent: 2% of the totality of food allergies. However, only adults are allergic to spices and allergy to spices accounts for 6.4% of food allergies in adults. Tiny amount of proteins are usually ingested. Patients at risk of spice allergy are young adults sensitized to mugwort and birch allergens, sharing cross-sensitization with various food vegetal allergens. The clinical suspicion raises from frequent post-prandial systemic reactions. Other allergens of vegetal origin have to be cleared. Diagnosis can be established by DBPCFC using powdered spices in capsules. [References: 22]

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[12] - Schöll I, Jensen-Jarolim E. Allergenic Potency of Spices: Hot, Medium Hot, or Very Hot. Int Arch Allergy Immunol 2004;135:247-261

Spices are the most attractive ingredients to confer an authentic taste to food. As they are derived from plants, they harbour allergenic potency and can induce symptoms ranging from mild local to severe systemic reactions. Due to the content of pharmacologically active substances of spices, the diagnosis of allergy and the differentiation from intolerance reactions may be difficult. Association with inhalative allergies via IgE cross-reactivity, but also direct gastrointestinal sensitization plays a role. This article is a botanical and allergological overview of the most important spices and molecules responsible for eliciting IgE-mediated reactions or cross-reactions. As no curative treatments are known at present, strict avoidance is recommended and, therefore, accurate labelling of pre-packed food is necessary.

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[13] - Zana H, Moneret-Vautrin DA, Guérin L, Kanny G, Leduc V. Allergie alimentaire aux graines de courge africaine. Rev Fr Allergol Immunol Clin 2005;45:275

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[14] - Stadtmauer G, Beyer K, Bardina L, Sicherer SH. Anaphylaxis to ingestion of hempseed (Cannabis sativa). J Allergy Clin Immunol 2003;112:216-217

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[15] - Chu E, Umetsu DT, Loewy EG. Tangerine seeds, but not tangerine fruit, as a cause of anaphylaxis. ACAAI Annual Meeting, San Antonio, 15-20 Nov. 2002, Poster n° P116

We report a 4.5 year old male who presented with anaphylaxis, with generalized urticaria as well as wheezing several hours after ingestion of a tangerine with seeds. The reactions required treatment with diphenhydramine as well as aerosolized albuterol with subsequent improvement of symptoms. Previous ingestions of seedless tangerines had not resulted in any allergic reactions, however, this was the first exposure for this child to tangerines with seeds. Specifically, the child chewed and then swallowed the tangerine seeds. Past medical history was not significant for asthma or allergic rhinitis, but was notable for well-controlled atopic dermatitis as well as a history of previous anaphylaxis to cashews and almonds confirmed by positive skin prick testing. Skin prick testing was performed and showed an extremely positive response to extract of tangerine seed (4+, had to be wiped off due to severity of reaction as seen in figure) with negative response to the tangerine fruit itself. Skin prick tests were also positive to cashew (4+), almond (4+), but negative for peanut. This represents the first report of a systemic reaction after oral ingestion of tangerine seeds, but not tangerine fruit, presumably caused by hypersensitivity to seed antigens. Figure Legend Right upper quadrant-Control, Left upper quadrant-Histamine, Right lower quadrant-Tangerine Juice, Left lower quadrant-Tangerine Seed Extract.

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[16] - Glaspole IN, de Leon MP, Rolland JM, O'Hehir RE. Anaphylaxis to lemon soap: citrus seed and peanut allergen cross-reactivity. Ann Allergy Asthma Immunol 2007;98:286-289

BACKGROUND: Many individuals allergic to peanuts have multiple allergen sensitivity. OBJECTIVE: To report the first case, to our knowledge, of a peanut allergic patient who exhibited cosensitivity to citrus seeds and who had experienced anaphylaxis to lemon soap. METHODS: Extracts of peanut and seeds from different varieties of citrus fruit (orange, lemon, and mandarin) were prepared and resolved with 14% sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Direct and inhibition immunoblotting of the patient's serum on the extracts was used to examine the pattern of IgE reactivity and the presence of cross-reactive allergens. RESULTS: Numerous IgE reactive proteins were demonstrated in each citrus seed extract and the peanut extract. Complete IgE cross-reactivity was demonstrated among the different citrus seed extracts. Partial cross-reactivity was demonstrated between the peanut and orange seed extracts. CONCLUSIONS: Citrus seeds contain numerous IgE reactive proteins that are completely cross-reactive among orange, lemon, and mandarin. When peanut allergy coexists with citrus seed allergy, IgE cross-reactivity between peanut and citrus seed proteins can be demonstrated, suggesting a basis to this cosensitivity.

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[17] - Rodríguez B, Rodríguez A, de Barrio M, Tornero P, Baeza ML. Asthma Induced by Canary Food Mix. Allergy Asthma Proc 2003;24:265-268

A 42-year-old woman reported immediate rhinoconjunctivitis, asthma, and contact urticaria while handling bird food. Skin-prick tests were positive to Lolium, Cynodon, Phragmites, Cupressus sempervirens, Cupressus arizonica, Chenopodium, sunflower pollen and seed, mugwort, chamomile, Chrysanthemum, Taraxacum, canary seed, and black seed (Guizotia abyssinica). The patient's serum-specific immunoglobulin (IgE) to Taraxacum, black seed, and canary seed was positive. Enzyme-linked immunosorbent assay inhibition studies revealed a 97 and 27% IgE-binding inhibition of whole canary food IgE by black seed and Taraxacum pollen, respectively. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis immunoblotting showed two IgE-binding protein bands of 11 and 44 kDa in the G. abyssinica extract. These two bands were totally inhibited by sunflower seed, mugwort, and Taraxacum extracts. Specific bronchial challenge with black seed extract was positive. The patient was able to feed her canary with birdseeds after she removed black seeds. We report a case of asthma caused by black seed (G. abyssinica) used as canary food in a patient previously allergic to pollen (olea europaea, grass, and mugwort) and sunflower seeds.

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[18] - Fritsch R, Ebner H, Kraft D, Ebner C. Food allergy to pumpkin seed: characterization of allergens. Allergy 1997;52:335-337

In recent years, pumpkinseed has become increasingly popular as a foodstuff. Here we report the occurrence of allergic reactions (itching and swelling of oral mucosa, and asthma) to this member of the Cucurbitaceae family. We investigated three patients suffering from symptoms after ingestion of roasted pumpkinseed. All the patients fished for sport and used pressed pumpkinseed flour as bait. Sera were tested by the immunoblot technique for IgE reactivity with proteins of pumpkinseed extract. The immunoblot revealed pumpkinseed allergens of 13, 14, 36, 48, 77, and 87 kDa. Inhibition experiments with recombinant birch profilin were performed: IgE binding to the 14-kDa allergen was completely blocked by preincubation of the sera with recombinant birch profilin. In conclusion, type I allergy to pumpkinseed is rare, and the patients' histories suggest inhalation of pumpkinseed flour during fishing to be the relevant route of sensitization, leading to food allergy to pumpkinseed.

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[19] - Sanchez Machin I, Garcia Robaina JC, de la Torre Morin F. Anaphylaxis due to the ingestion of cardamom (Elettaria cardamomum) present in biscuits and German bread. EAACI 22th Congress, Paris, 7-11 June, 2003, Poster n°697

Background: Allergic symptoms caused by spices are infrequent, and account only for 2% of food allergies. Adverse reactions have been reported to several spices, although only a few cases have been reported where cardamom was the offending agent causing allergic contact dermatitis. Cardamom belongs to Zingiberaceae botanical family along with ginger and Indian saffron (Curcuma domestica). Cardamom is a popular traditional flavouring agent for coffee, sweets and baked goods, particularly in Arabic countries. Besides having some pharmacological properties, such as antiinflammatory, analgesic and antispasmodic activity, extracts of cardamom are capable of enhancing the cutaneous penetration of drugs, such as indomethacin, prednisolone. Material and Methods: We present a 41year old man with no family or personal history of allergic reactions, who in the past year experienced 6 episodes of scalp, genital area, palms and soles pruritus, urticaria, facial angioedema, throat swelling and general malaise 15 to 30 minutes following the ingestion of wholemeal biscuits and home-made German-style bread. Emergency treatment was required in all these episodes. Skin prick tests were conducted with mites, pollens, moulds, animal danders, cereals and additives. The patient tolerates the ingestion all type of cereals. A further battery of tests was conducted with seeds, nuts and spices, including cardamom. Results: All skin tests were negative except the prick by prick with raw cardamom, which showed a positive immediate response with a wheal size of 9 x 6 mm. Specific IgE to cereals were negative. The patient remains symptom free since avoiding the ingestion of foods containing cardamom. Conclusions: We present a case of anaphylaxis due to sensitisation to, and ingestion of cardamom. Due to the severity of the clinical manifestations, the patient was not challenged with this spices. To the best of our knowledge, this is the first reported case of cardamom sensitivity inducing severe generalised symptoms. Cardamom should be included in the list of "hidden" food allergens.

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[20] - Helm RM. Allergy to plant seed proteins. J New Seeds 2001;3(3):37-60

Allergenicity is defined as the ability of proteins and other agents to sensitize genetically predisposed individuals to develop IgE antibodies, which bind to mast cells and basophils through the Fc portion of the IgE antibody. Upon subsequent exposures to the same protein, the proteins (allergens) bind to and cross-link cell bound IgE stimulating the release of mediators (histamine) that lead to an allergic reaction (immediate hypersensitivity). Seed proteins represent one important class of proteins that can induce a variety of allergic syndromes. Aerosolized particles released during pollination, harvest, transport and storage of grains and seed crops can cause inhalant allergy in susceptible individuals. Increased use of cereal grains, legumes and nuts in the diet has been suggested to contribute to the rise in the prevalence of food allergies. Plant biotechnology affords unique opportunities to identify individual components of seeds or seed products that may cause allergies and to remove or alter allergens from the food source, so that the food can be consumed safely by allergic individuals. These topics are highlighted to provide insight into the risks and benefits attributed to seed proteins. 100 ref

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[21] - Crespo JF, Rodriguez J. Food allergy in adulthood. Allergy 2003;58:98-113

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[22] - Rodriguez J, Poza P, Crespo JF. Follow-Up of Immunological Reactivity in 27 Patients Allergic to Nuts and Seeds. J Allergy Clin Immunol 2005;115(2 suppl.):S94

RATIONALE: There is limited information on the natural course of patients with positive skin testing and/or CAP FEIA to peanuts and/or tree nuts, but clinical tolerance. We evaluated if immunological reactivity to nuts developed into clinical reactivity over time METHODS: Twenty-seven patients (median= 25 yr.) with proven clinical allergy (DBPCFC procedure) to nuts [almond (AL), 3 patients; hazelnut (HN), 13; peanut (PN), 6; chestnut (ChN), 8; walnut (WN), 12; pistachio (P), 2; and sunflower seed (S), 6] were included in the study. Patients underwent skin prick testing and specific IgE determinations (CAP-FEIA) to other nuts with proven tolerance and, if positive, new clinical reactivity to nuts was assessed by phone interview, followed by oral provocations Median follow-up (months) was: AL, 51.5; HZ, 49.5; PN, 43; ChN, 38; WN, 65.5; P, 44.5; and S, 42 RESULTS: A total of 89 immunologic reactivities to nuts were detected (17 to AL, 7 to HZ, 17 to PN, 16 to ChN, 12 to WN, 10 to P, and 11 to S) After the follow- up period, 24 patients (80 immunologic reactions) could be contacted by telephone (89% participants). They reported intentional avoidance of 26 nuts (33%); ingestion with tolerance of 53 nuts (66%), and eating with symptoms to 1 nut (WN) (1%). A further clinical evaluation including DBPCFC confirmed one new case of clinical allergy to WN CONCLUSIONS: Patients clinically reactive to a nut have also an extensive immunologic reactivity to other nuts, which could be safely consumed, as new cases of clinical allergy seem to be infrequent

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[23] - Osterballe M, Hansen TK, Mortz CG, Bindslev-Jensen C. The clinical relevance of sensitization to pollen-related fruits and vegetables in unselected pollen-sensitized adults. Allergy 2005;60:218-225

BACKGROUND: Previous studies have described cross-reactivity between fresh fruits, vegetables and pollen. However, no data demonstrates the clinical relevance of sensitization to pollen-related fruits and vegetables in unselected pollen-sensitized adults with and without symptoms in the pollen season . OBJECTIVE: The aim of this study was to estimate the clinical relevance of sensitization to pollen-related fruits and vegetables in unselected pollen-sensitized adults and to examine the diagnostic value of skin-prick test (SPT), histamine release and specific IgE compared with the outcome of oral challenge . METHODS: In total, 936 unselected adults (female : male 479 : 457, median age 33.7 years) were examined for pollen sensitization and clinical cross-reactivity with pollen-related fruits and vegetables by questionnaire, SPT, histamine release, specific IgE and oral challenge . RESULTS: The prevalence of pollen sensitization was 23.8% (n = 223). The probability of a clinical reaction to pollen-related foods in the respective pollen-sensitized groups was: 24% (birch), 4% (grass), 10% (mugwort), 35% (birch + grass), 8% (grass + mugwort) and 52% (birch + grass + mugwort). The odds ratio of a clinical reaction to pollen-related fruits and vegetables in symptomatic pollen-sensitized adults was as high as four times (birch + grass) the odds ratio of a clinical reaction in asymptomatic pollen-sensitized adults . CONCLUSION: This study not only demonstrates a high prevalence of clinical reactions to fruits and vegetables in pollen-sensitized adults, but also a discrepancy between the prevalence of sensitization to fruits and vegetables and the clinical relevance in different pollen-sensitized groups with symptoms in the pollen season as a significant factor.

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[24] - Besler M, Hefle SL, Jensen-Jarolim E. Allergen data Collection: sunflower Seed (Helianthus annuus). Internet Symp Food Allergens 2001;3(2):103-114

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[25] - Mayaud-Marret C, Malod-Panisset A, Bidat E. L'allergie au tournesol et à son huile : rôles du contact, de l'ingestion et de l'inhalation. Rev Fr Allergol Immunol Clin 2006;46:92-94

Nous rapportons l'observation d'une fillette de cinq ans présentant une allergie alimentaire à l'huile de tournesol. Une sensibilisation est mise en évidence au niveau cutané pour l'huile et les graines de tournesol. Les IgE sériques spécifiques sont négatives. Le test de provocation par voie orale est positif pour 54 ml d'huile de tournesol. Elle réagit aussi à l'inhalation et au contact de graines de tournesol. Les signes cliniques sont variables : urticaire, érythème, vomissements, gêne respiratoire ou fatigue. Ils sont fonction de la voie de déclenchement : contact, ingestion et inhalation du (des) allergènes.

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[26] - Zitouni N, Errahali Y, Metche M, Kanny G, Moneret-Vautrin DA, Nicolas JP, et al. Influence of refining steps on trace allergenic protein content in sunflower oil. J Allergy Clin Immunol 2000;106:962-967

BACKGROUND: Although allergy to sunflower seed and oil is a relatively rare occurrence, several cases of sunflower seed allergy have been observed, and we have already described one case of anaphylaxis after eating sunflower oil and margarine. OBJECTIVE: The aim of our study was to determine and characterize the allergens from sunflower oil at the different steps of the refining process: crude pressed oil (step A), acidification and neutralization (step B), pregumming by centrifugation (step C), washing (step D), bleaching (step E), gumming by filtration (step F), and deodorization (step G). METHODS: A sample of oil from each step of the process (steps A to G) was heat extracted with PBS. The protein concentration of each extract was evaluated by using the micro-Bradford assay. Samples were run on SDS-PAGE. The immunoblot was performed with the serum of a patient sensitized to sunflower seed and oil. RESULTS: The extracts obtained after each step reveal a decrease in total protein concentration from 13.6 microg/mL to 0. 22 microg/mL. The result of SDS-PAGE shows 5 bands, from 67 kd to 145 kd, with the most abundant being the 67-kd protein. The amount of this protein decreases after each step of the process. It is, however, still present in trace amounts in the refined oil. The 67-kd protein, which is mainly present in the crude oil and slightly in the refined oil, has been shown to be allergenic. CONCLUSION: Because of the presence of allergenic proteins, refined sunflower oil may pose a threat to people highly sensitized to sunflower seeds.

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[27] - Asero R, Mistrello G, Roncarolo D, Amato S. Airborne allergy to sunflower seed. J Investig Allergol Clin Immunol 2004;14:244-246

BACKGROUND: There is increasing evidence that bird fanciers may develop airborne allergies to unusual allergens. OBJECTIVE: To detect the allergen source in a bird fancier with a history of asthma associated with bird cage cleaning activities and with contact with a Brazil parrot. METHODS: SPT with a large series of both airborne and food allergens were carried out. IgE reactivity to allergens causing wheal and flare reactions was confirmed by in-vitro investigations including ELISA/ELISA inhibition and immunoblot analysis. RESULTS: Strong skin reactivity to sunflower seed was observed. Immunoblot analysis showed IgE reactivity to low m.w. proteins, most probably 2S albumin, and ELISA inhibition studies showed the absence of cross-reactivity to mustard. CONCLUSION: Sunflower seed dust may sensitize patients via the respiratory tract. Differently from previously reported cases of sunflower seed allergy, no cross-reactivity to 2S albumin from botanically unrelated seeds was found.

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[28] - Palma-Carlos AG, Palma-Carlos ML, Tengarrinha F. Allergy to sunflower seeds. Eur Ann Allergy Clin Immunol 2005;37:183-186

A case of oral syndrome after eating sunflower seeds is reported. Sensitization has been probably through inhalant route when using these seeds to feed birds. Skin prick tests with a fresh macerate of sunflower seeds has been clearly positive (greater than histamine control) but commercial extracts have given borderline positivity and specific IgE to sunflower was strongly positive.

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[29] - de Lacoste de Laval A, Guérin L, Leduc V. Allergie aux pollen et graine de tournesol, réactions croisées ou cosensibilisation. Rev Fr Allergol Immunol Clin 2004;44:348

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[30] - Bousquet J, Dhivert H, Clauzel AM, Hewitt B, Michel FB. Occupational allergy to sunflower pollen. J Allergy Clin Immunol 1985;75:70-74

Although the sunflower belongs to the Compositeae family, allergy to sunflower pollen is not common. The occurrence of occupational allergy to this pollen species made it possible to characterize cross-reactive patterns of Compositeae pollens in a human experimental model. A 24-yr-old man developed rhinitis and conjunctivitis over 5 yr of exposure to sunflower pollens, and asthma developed during the fifth year. All respiratory and occular symptoms disappeared after he was removed from exposure, but he had a food allergic reaction while he was eating honey containing 30% sunflower pollens. The diagnosis of occupational allergy was based on history, skin prick tests and RAST to the pollen. Bronchial provocation tests performed after removal from exposure confirmed the sensitivity to sunflower pollens but there was no nonspecific hyperreactivity. It was found by RAST inhibition that sunflower pollen does not cross-react with other Compositeae pollens tested or with sunflower seed. The honey that elicited food intolerance was demonstrated to inhibit significantly sunflower pollen RAST

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[31] - Kanny G, Frémont S, Nicolas JP, Moneret-Vautrin DA. Food allergy to sunflower oil in a patient sensitized to mugwort pollen. Allergy 1994;49:561-564

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[32] - Moneret-Vautrin DA, Morisset M, Lemerdy P, Croizier A, Kanny G. Food allergy and IgE sensitization caused by spices: CICBAA data (based on 589 cases of food allergy). Allerg Immunol (Paris) 2002;34:135-140

BACKGROUND: Spices originate in various botanical families: Apiaceae, Lamiaceae, Lauraceae, Leguminosae, Liliaceae, Myristicaceae, Myrtaceae, Piperaceae, Solanaceae, Zingiberaceae.... METHODOLOGY: Prick-tests to native spices have been carried out in patients suspected of food allergies to spices. The CICBAA data bank includes 589 cases of food allergies, a part of which has benefited from investigations for spices. Data about the rate of sensitization and food allergy are available. RESULTS: Frequent sensitization to Apiaceae is observed: coriander, caraway, fennel, celery: 32% of prick-tests in children, 23% of prick-tests in adults. Sensitization to Liliaceae: garlic, onion, chive, is observed in 4.6% of prick-tests in children, 7.7% of prick-tests in adults. Rare cases of sensitization to paprika and saffron are recorded. Prick-tests to nutmeg, ginger and clove are currently negative. 10 food allergies related to the mugwort-celery-spices syndrome are reported: coriander: 1, caraway: 2, fennel: 3, garlic: 3, onion: 1. Food allergy to spices is unfrequent: 2% of the totality of food allergies. However, only adults are allergic to spices and allergy to spices accounts for 6.4% of food allergies in adults. Tiny amount of proteins are usually ingested. Patients at risk of spice allergy are young adults sensitized to mugwort and birch allergens, sharing cross-sensitization with various food vegetal allergens. The clinical suspicion raises from frequent post-prandial systemic reactions. Other allergens of vegetal origin have to be cleared. Diagnosis can be established by DBPCFC using powdered spices in capsules. [References: 22]

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[33] - de Lacoste de Laval A, Guérin L, Leduc V. Allergie aux pollen et graine de tournesol, réactions croisées ou cosensibilisation. Rev Fr Allergol Immunol Clin 2004;44:348

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[34] - Palma-Carlos AG, Palma-Carlos ML, Tengarrinha F. Allergy to sunflower seeds. Eur Ann Allergy Clin Immunol 2005;37:183-186

A case of oral syndrome after eating sunflower seeds is reported. Sensitization has been probably through inhalant route when using these seeds to feed birds. Skin prick tests with a fresh macerate of sunflower seeds has been clearly positive (greater than histamine control) but commercial extracts have given borderline positivity and specific IgE to sunflower was strongly positive.

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[35] - Lamilla Yerga AM, García Menaya JM, González Galán I, Jiménez Ferrera G, Cordobés Durán C, Mangas Santos RM. Food allergy with sunflower seeds. Allergy Clin Immunol Int 2005;17(Suppl. 1):364

Background: Sunflower (Helianthus annus) is a member of the Compositae family, frequently cultivated in Spain that is commonly consumed as toasted sunflower seeds or as sunflower oil. Few cases have been published reporting anaphylaxis after ingestion or inmunology contact urticaria. We report a case of an immediate systemic reaction after eating sunflower seeds. Clinical Report: A 17-year-old woman with seasonal rhinoconjunctivitis developed three episodes of angioedeme in face, lips and gums, immediately after eat sunflower seeds in the last six months. In the last episode she suffered cutaneous micropapular eruption in her neck and in the first episode she also presented dyspnea and generalized pruritus. In the three ocassions she was treated with methylprednisolone and dexclorpheniramine improving within 2-3 hours. Previously she had tolerated sunflower seeds. After the last episode she has avoided sunflower seeds. Actually she tolerates the rest of nuts. Methods and results: Skin prick test with common inhalants were positive to secale, lolium, poa, artemisia and dog epithelium, and were negative for the rest. Skin prick test with commkon commercial extracts of food were positive to sunflower seed and negative for the rest. Skin prick-prick with sunflower seed was positive. Serum total IgE was elevated (127 UI/ml) and serum specific IgE against sunflower seeds, almond, peanut and chestnut was negative. Conclusions: We report a case of a patient with immediate IgE-mediated systemic reactions due to sunflower seeds demonstrated by cutaneous tests.

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[36] - Axelsson IG, Ihre E, Zetterstrom O. Anaphylactic reactions to sunflower seed. Allergy 1994;49:517-520

We report on four patients sensitized to sunflower seed. Three of them developed anaphylaxis and one chronic bronchial asthma. All four patients reacted the first time sunflower seeds were ingested, and all had kept cage birds fed on sunflower seeds. Therefore, the route of sensitization was probably by inhalation of airborne sunflower seed allergens. Investigation of this type of hypersensitivity in 84 atopic patients showed that only three patients were RAST-positive, indicating that this allergy is fairly uncommon. On the other hand, when atopic persons are exposed to cage birds, the rate of sensitization is rather high, as indicated by the fact that in this category 79% were skin prick positive and 21% were unequivocably RAST positive to sunflower seed.

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[37] - Garcia Ortiz JC, Cosmes Martin P, Lopez-Asunsolo A. Allergy to foods in patients monosensitized to Artemisia pollen. Allergy 1996;51:927-931

It is known that patients with pollinosis may display clinical characteristics caused by allergy to certain fruits and vegetables, but subjects allergic to Artemisia seem to show particularly peculiar characteristics. The clinical features of 84 patients with rhinitis, asthma, urticaria, and/or anaphylaxis whose inhalant allergy was exclusively to Artemisia vulgaris were studied and compared with a control group of 50 patients monosensitized to grass pollen. The mean age for the beginning of symptoms was 30.2 years, and this was higher than in the control group (P < 0.05). We found the main incidence to be in women (70.2%). Some 42.3% had family history of atopia, lower than in the control group (P < 0.05), while the prevalence of asthma and urticaria was significantly higher (P < 0.05). Food hypersensitivity was reported by 23 patients (27.3%) allergic to Artemisia. The foods responsible (with respective numbers of cases) were honey (14), sunflower seeds (11), camomile (four), pistachio (three), hazelnut (two), lettuce (two), pollen (two), beer (two), almond (one), peanut (one), other nuts (one), carrot (one), and apple (one). None of the patients monosensitized to grass had food allergy. CAP inhibition experiments were carried out on a single patient. Results showed the existence of common antigenic epitopes in pistachio and Artemisia pollen for this patient. We concluded that mugwort hay fever can be associated with the Compositae family of foods, but that it is not normally associated with other foods.

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[38] - Garcia-Ortega P, Bartolome B, Enrique E, Gaig P, Richart C. Allergy to Diplotaxis erucoides pollen: occupational sensitization and cross-reactivity with other common pollens. Allergy 2001;56:679-683

BACKGROUND: Diplotaxis erucoides is a common weed of the Brassicaceae family widespread in southern and central Europe. METHODS: A total of 410 consecutive patients referred for allergy study of rhinoconjunctivitis and/or asthma were skin tested with D. erucoides pollen, 14 proving positive. A purified D. erucoides pollen extract was prepared to perform quantitative skin tests, provocation tests, immunoblotting, and EIA inhibition in the 14 sensitized patients. RESULTS: Three patients, directly involved in viniculture, had rhinoconjunctivitis related to D. erucoides pollen. No D. erucoides-related symptoms were observed in most patients, who were also sensitized to Artemisia pollen. RAST was positive in 12/14 patients and nasal provocation tests in 9/12. The molecular masses of the most prevalent IgE-binding proteins ranged from 26 to 27.5 and from 31 to 34 kDa. D. erucoides pollen inhibited the IgE-binding of other sensitizing pollens in the three viniculture workers, whereas both Artemisia and D. erucoides pollen produced similar heterologous inhibition in the pooled serum of the remaining, nonclinically affected, D. erucoides-sensitized patients. CONCLUSION: D. erucoides pollen may be an important prevalent aeroallergen, particularly in rural areas. It may act as an occupational allergen in vineyard workers, in whom it seems to be the primary sensitizing agent, playing a secondary cross-reactive role in other sensitized patients.

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[39] - Garcia Ortiz JC, Cosmes Martin P, Lopez-Asunsolo A. Melon sensitivity shares allergens with Plantago and grass pollens. Allergy 1995;50:269-273

Possible associations between allergy to pollen and that to food allergens were studied in 262 patients sensitized to pollen. Forty-four patients (16.7%) showed some allergic symptoms after testing with fruits and vegetables, melon being the food most frequently involved (24 patients), followed by sunflower seed (12 patients). Skin testing was done by the prick method with natural fruit or vegetable, and also with commercial food extracts. We found in our region that the distribution of sensitivity to pollens in the group of patients with allergy to fruits or vegetables does not coincide with the prevalence in pollen-allergic subjects in general, since in the first group--subjects allergic to food--there was a major prevalence of allergy to Plantago (P < 0.01). In particular, in the group of subjects allergic to melon, the prevalence of sensitivity to grass and especially to Plantago was larger than in pollen-allergic subjects in general (P < 0.05 and P < 0.001, respectively). The use of fresh food produced better results than commercial extracts. A positive skin test to fresh melon closely correlated with positive CAP results. CAP inhibition experiments were carried out, and we found that Dactylis and Plantago extracts inhibited the binding of the melon-positive pool to solid-phase melon. The results suggest the existence of common antigenic epitopes in melon and Plantago pollen, and in melon and grass pollen.

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[40] - Osterballe M, Hansen TK, Mortz CG, Bindslev-Jensen C. The clinical relevance of sensitization to pollen-related fruits and vegetables in unselected pollen-sensitized adults. Allergy 2005;60:218-225

BACKGROUND: Previous studies have described cross-reactivity between fresh fruits, vegetables and pollen. However, no data demonstrates the clinical relevance of sensitization to pollen-related fruits and vegetables in unselected pollen-sensitized adults with and without symptoms in the pollen season . OBJECTIVE: The aim of this study was to estimate the clinical relevance of sensitization to pollen-related fruits and vegetables in unselected pollen-sensitized adults and to examine the diagnostic value of skin-prick test (SPT), histamine release and specific IgE compared with the outcome of oral challenge . METHODS: In total, 936 unselected adults (female : male 479 : 457, median age 33.7 years) were examined for pollen sensitization and clinical cross-reactivity with pollen-related fruits and vegetables by questionnaire, SPT, histamine release, specific IgE and oral challenge . RESULTS: The prevalence of pollen sensitization was 23.8% (n = 223). The probability of a clinical reaction to pollen-related foods in the respective pollen-sensitized groups was: 24% (birch), 4% (grass), 10% (mugwort), 35% (birch + grass), 8% (grass + mugwort) and 52% (birch + grass + mugwort). The odds ratio of a clinical reaction to pollen-related fruits and vegetables in symptomatic pollen-sensitized adults was as high as four times (birch + grass) the odds ratio of a clinical reaction in asymptomatic pollen-sensitized adults . CONCLUSION: This study not only demonstrates a high prevalence of clinical reactions to fruits and vegetables in pollen-sensitized adults, but also a discrepancy between the prevalence of sensitization to fruits and vegetables and the clinical relevance in different pollen-sensitized groups with symptoms in the pollen season as a significant factor.

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[41] - Asero R, Mistrello G, Roncarolo D, Amato S. Airborne allergy to sunflower seed. J Investig Allergol Clin Immunol 2004;14:244-246

BACKGROUND: There is increasing evidence that bird fanciers may develop airborne allergies to unusual allergens. OBJECTIVE: To detect the allergen source in a bird fancier with a history of asthma associated with bird cage cleaning activities and with contact with a Brazil parrot. METHODS: SPT with a large series of both airborne and food allergens were carried out. IgE reactivity to allergens causing wheal and flare reactions was confirmed by in-vitro investigations including ELISA/ELISA inhibition and immunoblot analysis. RESULTS: Strong skin reactivity to sunflower seed was observed. Immunoblot analysis showed IgE reactivity to low m.w. proteins, most probably 2S albumin, and ELISA inhibition studies showed the absence of cross-reactivity to mustard. CONCLUSION: Sunflower seed dust may sensitize patients via the respiratory tract. Differently from previously reported cases of sunflower seed allergy, no cross-reactivity to 2S albumin from botanically unrelated seeds was found.

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[42] - Do MY, Kim HM, Choi SY, Lee EK, Park JW, Hong CS. Identification of specific IgE binding proteins: Sunflower seed anaphylaxis. Allergy Clin Immunol Int 2005;17(Suppl. 1):364

Background: Sunflower () taxonomically belongs to the Compositae family which includes ragweed, mugwort and chrysanthemum. Its seeds are used as an ingredient in margarine, cooking, salad oils, and a bread condiment. Sunflower seed can cause anaphylaxis after ingestion in some susceptible individuals. But, there are few studies about its allergens. Methods: We experienced one sunflower seed anaphylaxis patient and evaluated its allergenicity by ELISA, and 2-dimensional PAGE immunoblots. Crossallergenicity among sunflower seeds, cottonseeds and castor beans were also determined by ELISA inhibitions. Results: The patients showed positive skin response (mean wheal size; 12 mm) to the extract of sunflower seed in prick test but negative responses to ragweed, mugwort and chrysanthemum. Sunflower seed specific IgE was specifically inhibited by the extract of sunflower seeds (maximum inhibition of 91%) but not with cottonseeds and castor beans. IgE of the patient's serum bound to proteins with molecular weights to 9, 12, 14, 18 kD. Our study suggests that 9, 14, 18 kD protein maybe candidate major allergen of sunflower seed.

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[43] - Comstock SS, Kath C, Teuber SS. Sunflower Seed Food Allergy as a Co-allergy With Peanut. J Allergy Clin Immunol 2007;119(1 suppl):S116

RATIONALE: Sunflower seed allergens are not well-described. Because sunflower seed butter may be consumed as an alternative to peanut butter by peanut-allergic individuals or those trying to avoid sensitization to peanut, issues of co-allergy are important. METHOD: Volunteers with self-reported severe nut and/or seed allergies were recruited. Subjects were interviewed and asked if they had ever eaten the following foods and if they had any symptoms upon ingestion: different tree nuts, peanut, sunflower seeds, pumpkin, or sesame seeds. Sera donated by some subjects were used in IgE immunoblots against raw sunflower seed extract and sunflower butter extract. RESULTS: In our population of seed or nut-allergic individuals, co-allergy to peanut and sunflower seed was reported by 20 of 210 patients with peanut allergy (9.5%). Sera from patients with sunflower and peanut allergy showed IgE binding to multiple sunflower polypeptide bands in both the seed and butter extracts. The roasted sunflower butter extract contained more high molecular weight polypeptides in a Coomassie-stained gel. Much, but not all, of the IgE reactivity was absorbed out by preincubation of sera with perennial ryegrass pollen extract. 31 patients with peanut allergy, but no known sunflower seed allergy were also screened (some of whom had never eaten sunflower seeds), and 9 showed IgE binding to sunflower proteins. CONCLUSIONS: Some patients with peanut allergy are clinically allergic to both peanut and sunflower by self-report. Also, a percentage of patients with peanut allergy have sunflower seed-reactive IgE that may not be clinically relevant.

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[44] - Asero R, Mistrello G, Roncarolo D, Amato S. Allergenic similarities of 2S albumins. Allergy 2002;57:61-62

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[45] - Kelly JD, Hlywka JJ, Hefle SL. Identification of sunflower seed IgE-binding proteins. Int Arch Allergy Immunol 2000;121:19-24

Sunflower seed can cause severe anaphylactic reactions in some susceptible individuals. It is conceivable that the 2S sunflower seed protein is an allergen based on its high degree of homology (34%) with the allergenic mature 2S albumin protein of the Brazil nut. The first step in determining the allergenicity of sunflower seed proteins is to identify IgE-binding proteins. METHODS: Sera from sunflower seed-sensitive individuals were evaluated by radioallergosorbent test (RAST), isoelectric focusing (IEF) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis immunoblotting with sunflower seed proteins. RESULTS: Positive RAST scores (>2) were observed in 3 individuals and immunoblotting demonstrated IgE-binding to 2-7 distinct proteins ranging in size from 10 to 50 kD. Two out of 3 sera recognized two proteins between 16 and 17 kD. The lower molecular weight protein (16 kD) approximates to the prepo region of the precursor methionine-rich 2S albumin protein found in sunflower seed (SFA-8/SSA). IEF followed by immunoblotting demonstrated several IgE-binding proteins, including two proteins with isoelectric points of 5.97 and 5.3, respectively, which are consistent with the mature and immature forms of the SFA-8/SSA region. CONCLUSIONS: Sunflower seed contains several IgE-binding proteins, including regions of the high-methionine 2S albumin SFA-8/SSA.

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[46] - Kelly JD, Hefle SL. 2S methionine-rich protein (SSA) from sunflower seed is an IgE-binding protein. Allergy 2000;55:556-559

BACKGROUND: Sunflower seed contains 2S albumins that in other crops have been associated with allergenicity. The sunflower seed methionine-rich 2S albumin (SSA) may be an IgE-binding protein responsible for anaphylactic reactions in some sunflower seed-sensitive subjects. The objective was to demonstrate that SSA is an IgE-binding protein. METHODS: SSA was purified and the amino-acid sequence determined. The degree of purity of SSA was evaluated by silver staining, and its IgE-binding capacity by immunoblotting with serum from a subject with a convincing clinical history of anaphylaxis to sunflower seed. RESULTS: The amino-acid sequence confirmed that the purified protein was the mature form of the methionine-rich storage protein SSA from sunflower seed (Helianthus annuus). The SSA was specifically recognized by IgE from the serum of the sunflower seed-allergic subject. CONCLUSIONS: SSA is an IgE-binding protein, and subjects allergic to sunflower seed whose IgE binds to SSA are at risk of developing allergic reactions if they consume SSA.

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[47] - Papageorgiou PS, Shewry PR, Fido RJ, Papadopoulos NG, Tassios IK, Tatham AS. Identification of Lipid Transfer Protein (LTP) as a major sunflower seed food allergen in sunflower seed-induced systemic reactions. EAACI 22th Congress, Paris, 7-11 June, 2003, Poster n°197, p.63

Background: Sunflower seeds (SS) have been reported to cause severe anaphylactic reactions to some susceptible individuals. Several IgE binding proteins have been detected in SS and a 2S methionine-rich SS albumin (SSA) has been recently suggested as the responsible allergen causing anaphylactic reactions. The aim of our study was to identify clinically relevant SS allergens in 6 patients with severe allergic reactions to SS but no pollen allergy. Methods: 6 patients aged 6-12 years with severe systemic allergic reaction to the ingestion of SS underwent skin prick testing (SPT) with isotonic solutions of the purified major protein fractions of SS: lipid transfer proteins (LTP), N-terminal albumins, C-terminal albumins, SFA8 methionine-rich albumins and total albumins at concentrations of 0.01-10.0 mg/ml as well as histamine and normal saline. Their sera were evaluated for specific IgE to SS by FEIA, Pharmacia CAP System and by IgE immunoblotting using the purified SS protein fractions. Results: Serum specific IgE to sunflower seed was positive in all patients (>1KUA/L). Five of 6 patients were SPT positive to the LTP fraction and less reactive/non- reactive to other albumin fractions and by immunoblotting the LTP was identified as the major binding protein in the same 5/6 patients. To a lesser extent N- and C-type 2S albumins were recognized in the immunoblot of some patients but without eliciting a SPT reaction. Pooled sera of 3 atopic, non-allergic to SS gave negative FEIA and immunoblotting results. Conclusion: IgE staining to LTP and the positive SPT reactions to the LTP fraction of purified protein fractions of SS in 5/6 patients with systemic anaphylactic reaction to the ingestion of SS, indicate that in these patients the major allergen is the LTP.

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[48] - Akkerdaas J, Fernandez-Rivas M, Zuidmeer L, Hefle S, Aalberse R, van Ree R. IgE binding profiles to several food LTPs of Spanish patients with apple ingestion related symptoms. Allergy Clin Immunol Int 2005;17(Suppl. 1):338-339

Background Fruit allergic individuals from the Mediterranean area are predominantly sensitized by the non-specific lipid transfer protein (nsLTP). It seems that peach LTP is the most likely sensitizing allergen, however other factors (pollen related, genetic) can not be excluded yet. Objective It was our aim to identify IgE binding profiles to different natural (n) and recombinant (r) purified LTPs and to study the pair wise correlation between amino acid sequence identity and LTP specific IgE titers. Methods Serum and clinical data (after ingestion of 6 different foods) was obtained from Spanish apple allergic patients (n=19), as was proven by SPT/ DBPCFC. Seven different LTPs (rApple, rPeach, nGrape, rStrawberry, nSunflower, nHazelnut and nMaize, also analyzed for sequence homology) were applied in RAST to determine specific-IgE titers. Results Clinical symptoms after apple ingestion ranged from no- to severe systemic reactions like anaphylaxis. LTP Sequence homologies ranged from 81% (apple/peach) to 44% (hazelnut/maize). Highest correlation observed for IgE binding:0.989 (apple:peach). Lowest correlation: 0.228 (maize/grape). RAST highest/lowest mean score: apple 6.4/maize 0.4 IU/ml respectively. Conclusion Since most patients were selected on having a true apple allergy and the amino acid sequence homology between apple and peach LTP is 81%, an IgE binding-correlation of 0.989 was to be expected. Elucidation of IgE crossreactivity patterns between the LTPs applied might predict clinical symptoms. The intriguing question remains: How do we identify the sensitizing LTP and how do we prevent the development of (severe) food allergy as result of the induction of IgE against LTP?

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[49] - Comstock SS, Kath C, Teuber SS. Sunflower Seed Food Allergy as a Co-allergy With Peanut. J Allergy Clin Immunol 2007;119(1 suppl):S116

RATIONALE: Sunflower seed allergens are not well-described. Because sunflower seed butter may be consumed as an alternative to peanut butter by peanut-allergic individuals or those trying to avoid sensitization to peanut, issues of co-allergy are important. METHOD: Volunteers with self-reported severe nut and/or seed allergies were recruited. Subjects were interviewed and asked if they had ever eaten the following foods and if they had any symptoms upon ingestion: different tree nuts, peanut, sunflower seeds, pumpkin, or sesame seeds. Sera donated by some subjects were used in IgE immunoblots against raw sunflower seed extract and sunflower butter extract. RESULTS: In our population of seed or nut-allergic individuals, co-allergy to peanut and sunflower seed was reported by 20 of 210 patients with peanut allergy (9.5%). Sera from patients with sunflower and peanut allergy showed IgE binding to multiple sunflower polypeptide bands in both the seed and butter extracts. The roasted sunflower butter extract contained more high molecular weight polypeptides in a Coomassie-stained gel. Much, but not all, of the IgE reactivity was absorbed out by preincubation of sera with perennial ryegrass pollen extract. 31 patients with peanut allergy, but no known sunflower seed allergy were also screened (some of whom had never eaten sunflower seeds), and 9 showed IgE binding to sunflower proteins. CONCLUSIONS: Some patients with peanut allergy are clinically allergic to both peanut and sunflower by self-report. Also, a percentage of patients with peanut allergy have sunflower seed-reactive IgE that may not be clinically relevant.

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[50] - Kelly JD, Hlywka JJ, Hefle SL. Identification of sunflower seed IgE-binding proteins. Int Arch Allergy Immunol 2000;121:19-24

Sunflower seed can cause severe anaphylactic reactions in some susceptible individuals. It is conceivable that the 2S sunflower seed protein is an allergen based on its high degree of homology (34%) with the allergenic mature 2S albumin protein of the Brazil nut. The first step in determining the allergenicity of sunflower seed proteins is to identify IgE-binding proteins. METHODS: Sera from sunflower seed-sensitive individuals were evaluated by radioallergosorbent test (RAST), isoelectric focusing (IEF) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis immunoblotting with sunflower seed proteins. RESULTS: Positive RAST scores (>2) were observed in 3 individuals and immunoblotting demonstrated IgE-binding to 2-7 distinct proteins ranging in size from 10 to 50 kD. Two out of 3 sera recognized two proteins between 16 and 17 kD. The lower molecular weight protein (16 kD) approximates to the prepo region of the precursor methionine-rich 2S albumin protein found in sunflower seed (SFA-8/SSA). IEF followed by immunoblotting demonstrated several IgE-binding proteins, including two proteins with isoelectric points of 5.97 and 5.3, respectively, which are consistent with the mature and immature forms of the SFA-8/SSA region. CONCLUSIONS: Sunflower seed contains several IgE-binding proteins, including regions of the high-methionine 2S albumin SFA-8/SSA.

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[51] - Murtagh GJ, Dumoulin M, Archer DB, Alcocer MJ. Stability of recombinant 2 S albumin allergens in vitro. Biochem Soc Trans 2002;30:913-915

Two well known 2 S albumins, Ber e 1 from brazil nut and sunflower 2 S albumin 8 (SFA-8), have been expressed in a eukaryotic system and purified. Analysis of recombinant versions of Ber e 1 and SFA-8 revealed them to be significantly more resistant to digestion by pepsin than BSA, and to be stable for up to 30 min in simulated gastric fluid. Unfolding monitored by CD indicated that both proteins were also very resistant to denaturation induced by heat and low pH. These results suggest that, although the ability of 2 S albumins to reach the circulatory system may be a prerequisite for the allergenicity of this group of proteins, stability is just one of a number of characteristics that provoke a selective immune response

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[52] - Burnett GR, Wickham M, Fillery-Travis A, Robertson JA, Belton PS, Gilbert SM, et al. Interaction between protein allergens and model gastric emulsions. Biochem Soc Trans 2002;30:916-918

The observed resistance to pepsinolysis of known food allergens has been suggested as a predictor of their allergenic risk. Consequently, resistance to pepsinolysis has become incorporated into decision tree assessment for potential allergenic risk posed by novel foods. However, existing methods take little account of the interaction between food structure and physiological conditions existing during digestion in vivo. Here we show that a range of protein allergens can adsorb to model stomach emulsions, providing a further means of resisting digestion. We also show that raising the pH and the addition of bile salts to a model stomach emulsion, thereby mimicking the duodenal environment, has the effect of desorbing the adsorbed protein.

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[53] - Egorov TA, Odintsova TI, Musolyamov AKh, Fido R, Tatham AS, Shewry PR. Disulphide structure of a sunflower seed albumin: conserved and variant disulphide bonds in the cereal prolamin superfamily. FEBS Lett 1996;396:285-288

Disulphide mapping of a methionine-rich 2S albumin from sunflower seeds showed four intra-chain disulphide bonds which are homologous with those in a related heterodimeric albumin from lupin seeds (conglutin delta). Similar conserved disulphide bonds are also present in alpha-gliadin and gamma-gliadin storage proteins of wheat, but a lower level of conservation is present in a further related group of proteins, the cereal inhibitors of alpha-amylase and trypsin. These differences may relate to the different functions of the proteins.

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[54] - Pantoja-Uceda D, Shewry PR, Bruix M, Tatham AS, Santoro J, Rico M. Solution structure of a methionine-rich 2S albumin from sunflower seeds: relationship to its allergenic and emulsifying properties. Biochemistry 2004;43:6976-6986

The three-dimensional structure in aqueous solution of SFA-8, a 2S albumin 103-residue protein from seeds of sunflower (Helianthus anuus L.), has been determined by NMR methods. An almost complete (1)H resonance assignment was accomplished from analysis of two-dimensional (2D) COSY and 2D TOCSY spectra, and the structure was computed by using restrained molecular dynamics on the basis of 1393 upper limit distance constraints derived from NOE cross-correlation intensities measured in 2D NOESY spectra. In contrast with most other 2S albumins, SFA-8 consists of a single polypeptide chain without any cleavage in the segment of residues 30-46. The computed structures exhibited an rmsd radius of 0.52 A for the backbone structural core (residues 11-30 and 46-101) and 1.01 A for the side chain heavy atoms. The resulting structure consists of five amphipathic helices arranged in a right-handed superhelix, a folding motif first observed in nonspecific lipid transfer (nsLTP) proteins, and common to other 2S albumins. In contrast to nsLTP proteins, neither SFA-8 nor RicC3 (a 2S albumin from castor bean) has an internal cavity that is able to host a lipid molecule, which results from an exchange in the pairing of disulfide bridges in the CXC segment. Both 2S albumins and nonspecific lipid transfer proteins belong to the prolamin superfamily, which includes a number of important food allergens. Differences in the extension and solvent exposition of the so-called "hypervariable loop" (which connects helices III and IV) in SFA-8 and RicC3 may be responsible for the different allergenic properties of the two proteins. SFA-8 has been shown to form highly stable emulsions with oil/water mixtures. We propose that these properties may be determined partly by a hydrophobic patch at the surface of the protein which consists of five methionines that partially hide the Trp76 residue. The flexibility of the loop which contains Trp76 and the hydrophobicity of the whole environment may favor a conformational change, by which the Trp76 side chain may become inserted into the oil phase.

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[55] - Asero R, Mistrello G, Roncarolo D, Amato S. Allergenic similarities of 2S albumins. Allergy 2002;57:61-62

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[56] - Parra FM, Cuevas M, Lezaun A, Alonso MD, Beristain AM, Losada E. Pistachio nut hypersensitivity: identification of pistachio nut allergens. Clin Exp Allergy 1993;23:996-1001

Type I hypersensitivity to pistachio nut antigens was demonstrated in three patients by means of immediate skin-test reactivity, specific IgE determination by a fluoroimmunoassay (CAP), CAP-inhibition and leucocyte histamine release. Sensitization to other dried fruits and pollens was observed in the patients. The CAP-inhibition studies revealed significant crossreactivity between pistachio and cashew nut belonging to the Anacardiaceae family, and between pistachio nut and other dried fruits belonging to taxonomically unrelated botanical families. No relevant crossallergenicity was observed between pistachio nut and Lolium and Olea pollens. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of a pistachio nut extract followed by immunoblotting analysis identified four IgE-binding bands with molecular weights of 34, 41, 52 and 60 kD.

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[57] - Comstock SS, Kath C, Teuber SS. Sunflower Seed Food Allergy as a Co-allergy With Peanut. J Allergy Clin Immunol 2007;119(1 suppl):S116

RATIONALE: Sunflower seed allergens are not well-described. Because sunflower seed butter may be consumed as an alternative to peanut butter by peanut-allergic individuals or those trying to avoid sensitization to peanut, issues of co-allergy are important. METHOD: Volunteers with self-reported severe nut and/or seed allergies were recruited. Subjects were interviewed and asked if they had ever eaten the following foods and if they had any symptoms upon ingestion: different tree nuts, peanut, sunflower seeds, pumpkin, or sesame seeds. Sera donated by some subjects were used in IgE immunoblots against raw sunflower seed extract and sunflower butter extract. RESULTS: In our population of seed or nut-allergic individuals, co-allergy to peanut and sunflower seed was reported by 20 of 210 patients with peanut allergy (9.5%). Sera from patients with sunflower and peanut allergy showed IgE binding to multiple sunflower polypeptide bands in both the seed and butter extracts. The roasted sunflower butter extract contained more high molecular weight polypeptides in a Coomassie-stained gel. Much, but not all, of the IgE reactivity was absorbed out by preincubation of sera with perennial ryegrass pollen extract. 31 patients with peanut allergy, but no known sunflower seed allergy were also screened (some of whom had never eaten sunflower seeds), and 9 showed IgE binding to sunflower proteins. CONCLUSIONS: Some patients with peanut allergy are clinically allergic to both peanut and sunflower by self-report. Also, a percentage of patients with peanut allergy have sunflower seed-reactive IgE that may not be clinically relevant.

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[58] - Jansen A, Vermeulen A, Dieges PH, Van Toorenenbergen AW. Allergy to pine nuts in a bird fancier. Allergy 1996;51:741-744

A patient is described with the bird-egg syndrome who experienced an anaphylactic reaction after eating some of her parrot's food (pine nuts: Pinus pinea). Specific IgE against this nut and another pine nut (P. cembra) was demonstrated by RAST. Cross-reactivity between these botanically related seeds was shown by RAST inhibition. Besides avian antigens, bird food antigens should be taken into consideration when symptoms of allergy occur on exposure to birds.

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[59] - Quercia O, Rafanelli S, Marsigli L, Foschi FG, Stefanini GF. Unexpected anaphylaxis to cashew nut. Allergy 1999;54:895-897

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[60] - Ibañez MD, Lombardero M, Martinez san Ireneo M, Muñoz MC. Anaphylaxis induced by pine nuts in two young girls. Pediatr Allergy Immunol 2003;14:317-319

BACKGROUND: The aetiology of food allergy remains unclear. Although failure to develop or breakdown in oral tolerance has been proposed, the existence of physiologic sensitization routes other than the gastrointestinal tract cannot be excluded. OBJECTIVE: The purpose of this study is to clarify whether or not exposure to allergen through the skin can promote food allergy. METHODS: BALB/c mice were shaved on the back, and a patch impregnated with 100 micro g of ovalbumin (OVA) was applied to the dorsal skin for a 1-week period and then removed. After three courses of sensitization, OVA-specific antibodies in sera were measured, and then mice were orally challenged with 50 mg of OVA. Anaphylactic symptoms, plasma histamine levels, and histology of intestines and lungs after oral challenge were examined. RESULTS: Epicutaneous (EC) sensitization of mice to OVA induced a high level of OVA-specific IgE. Subsequent oral challenge with OVA resulted in symptoms of systemic anaphylaxis with elevated levels of plasma histamine as well as histological changes in both intestines and lungs. In the presence of anti-IL-4 antibodies, EC sensitization failed to provoke an IgE response, but still induced a Th2-predominant cellular immune response in lungs after oral challenge. CONCLUSION: We demonstrated for the first time that food allergy can be induced by allergen exposure through the skin. Our results identify a novel role of EC sensitization in the pathogenesis of food allergy.

↩

[61] - Mazeyrat R, Paupe J. Choc anaphylactique au pignon de pin. Rev Fr Allergol Immunol Clin 1999;39:139-140

↩

[62] - Beyer AV, Gall H, Peter RU. Anaphylaxis to pine nuts. Allergy 1998;53:1227

↩

[63] - Micheau P, Juchet A, Rancé F, Brémont F, Dutau G. Allergie au pignon de pin. Rev Fr Allergol Immunol Clin 2001;41:348

↩

[64] - van de Scheur MR, Bruynzeel DP. Acute anaphylaxis after pine nut skin testing. Ann Allergy Asthma Immunol 2004;92:93

↩

[65] - Rubira N, Botey J, Eseverri JL, Marin A. Allergy to pine nuts in children. Allerg Immunol (Paris) 1998;30:212-216

BACKGROUND: Allergy to nuts is a common and well-known disease. Despite the fact that pine nut is a widely eaten food, only nine cases have been described in literature. OBJECTIVE: To describe four paediatric patients suffering from allergy reaction on ingestion of pine nuts and compare them with cases described in literature, taking into account clinical symptoms, epidemiological and diagnostic methods. METHODS: The immuno-allergic study was carried out with skin tests (prick tests) using a commercial and native extract, and specific IgE serum test. An oral provocation test was performed in one case. RESULTS: Ages ranged from 12 months to 6 years. All patients had a personal history of atopy. Symptoms on ingesting pine nut were severe systemic reactions in three cases. Two of the children had allergic reactions to other nuts. In all cases, both the skin test and the specific IgE serum test were positive. The oral provocation was positive in the case for which it was performed. CONCLUSIONS: A typical clinical reaction of immediate hypersensitivity to this nut took place in all four children. The skin tests and in vitro studies confirm an IgE-mediated response. We currently have a commercial prick test for pine nut for the diagnosis, which has proven its sensitivity and specificity. In our region, due to the large consumption, the rate of allergic reactions to pine nuts would probably be greater and earlier on in life than in other areas. [References: 21]

↩

[66] - Moneret-Vautrin DA, Blain H, Kanny G, Bloch Y. Anaphylaxis to walnuts and pine nuts induced by ACE. Allergy 1998;53:1233-1234

↩

[67] - Subba Rao PV, Rajagopal D, Ganesh KA. B- and T-cell epitopes of tropomyosin, the major shrimp allergen. Allergy 1998;53(suppl. 46):44-47

The major crustacean allergen characterized from different species of shrimp is the muscle protein tropomyosin. Two shared epitopes corresponding to 47-63 and 150-158 of the deduced amino-acid sequence of the brown shrimp, M. ensis, were identified as IgE-binding B-cell epitopes. A 21-mer peptide spanning the amino-acid residues 261-281 was identified as a putative T-cell epitope capable of reducing ongoing tropomyosin-specific IgG and IgE responses in a mouse model. These observations suggest that peptide immunotherapy may also be effective in the treatment of food hypersensitivity.

↩

[68] - de las Marinas D, Vila L, Sanz ML. Allergy to pine nuts. Allergy 1998;53:220-222

↩

[69] - Añó MA, Maselli JP, Sanz ML, Fernández-Benítez M. Allergy to pine nut. Allergol Immunopathol (Madr) 2002;30:104-108

↩

[70] - Ibañez MD, Lombardero M, Martinez san Ireneo M, Muñoz MC. Anaphylaxis induced by pine nuts in two young girls. Pediatr Allergy Immunol 2003;14:317-319

BACKGROUND: The aetiology of food allergy remains unclear. Although failure to develop or breakdown in oral tolerance has been proposed, the existence of physiologic sensitization routes other than the gastrointestinal tract cannot be excluded. OBJECTIVE: The purpose of this study is to clarify whether or not exposure to allergen through the skin can promote food allergy. METHODS: BALB/c mice were shaved on the back, and a patch impregnated with 100 micro g of ovalbumin (OVA) was applied to the dorsal skin for a 1-week period and then removed. After three courses of sensitization, OVA-specific antibodies in sera were measured, and then mice were orally challenged with 50 mg of OVA. Anaphylactic symptoms, plasma histamine levels, and histology of intestines and lungs after oral challenge were examined. RESULTS: Epicutaneous (EC) sensitization of mice to OVA induced a high level of OVA-specific IgE. Subsequent oral challenge with OVA resulted in symptoms of systemic anaphylaxis with elevated levels of plasma histamine as well as histological changes in both intestines and lungs. In the presence of anti-IL-4 antibodies, EC sensitization failed to provoke an IgE response, but still induced a Th2-predominant cellular immune response in lungs after oral challenge. CONCLUSION: We demonstrated for the first time that food allergy can be induced by allergen exposure through the skin. Our results identify a novel role of EC sensitization in the pathogenesis of food allergy.

↩

[71] - Barzaga PA, Teuber S, Petersen R. Detection of pine nut allergens by immunoblotting and immunoCAP. ACAAI Annual Meeting, San Antonio, 15-20 Nov. 2002, Poster n° P16

Little is known about pine nut allergens. The purpose of this study was to compare immunoblot detection of pine nut allergens to ImmunoCAP testing (Pharmacia Diagnostics) using sera from 12 patients with a very convincing history of pine nut allergy. All patient sera showed a positive IgE immunoblot to pine nut extract. One patient reported allergy only to pine nuts; the others reported primary allergy to another tree nut but had either systemic reactions or a less severe reaction upon accidental pine nut ingestion. Control sera were obtained from one patient with peanut allergy, one with Aspergillus allergy, and four with significant grass and tree pollen allergy, all of whom tolerated pine nuts. SDS-PAGE and IgE immunoblotting were performed using raw pine nut extract. Sera from grass-allergic patients showed IgE binding to multiple polypeptides above 21 kDa. Serum from the patient sensitive solely to pine nuts showed IgE binding to a polypeptide around 14 kDa in a non-reduced protein preparation and some binding to higher molecular weight proteins. The other patient sera showed binding to either a doublet around 17 kDa or to a lower molecular weight protein at about 10 kDa +/- multiple higher molecular weight polypeptides. Only serum from the patient solely allergic to pine nuts had a significantly positive ImmunoCAP value at 1.83 kU/l and two registered 0.35 kU/l and 0.44 kU/l with the remaining nine <0.35 kU/l. Interestingly, the 4 pollen-allergic control sera showed positive values of 0.50, 1.70, 1.23 and 2.07 kU/l. These findings demonstrate that IgE towards potentially relevant lower molecular weight allergens in pine nut may be poorly detected by ImmunoCAP testing in those patients whose primary allergy is to another tree nut. In addition, grass pollen allergic patients tolerant to pine nuts may have false positive pine nut ImmunoCAP testing. If more patients with anaphylaxis to other tree nuts demonstrate IgE to allergens from 7-10 kDa and 17 kDa, it could imply that either these patients could really tolerate pine nuts if challenged or there are issues of IgE avidity and homologous protein epitopes relevant to clinical cross-reactivity as yet unknown. These findings suggest that pine nut ImmunoCAP tests should be interpreted with caution and correlated with supporting clinical history.

↩

[72] - Añó MA, Maselli JP, Sanz ML, Fernández-Benítez M. Allergy to pine nut. Allergol Immunopathol (Madr) 2002;30:104-108

↩

[73] - Garcia-Menaya JM, Gonzalo-Garijo MA, Moneo I, Fernandez B, Garcia-Gonzalez F, Moreno F. A 17 kDa allergen detected in pine nuts. Allergy 2000;55:291-293

Few cases of allergy to pine nuts have been described. We report a case of anaphylactic reaction to pine nuts. The patient needed to be treated in the emergency room due to a systemic reaction immediately after eating pine nuts. METHODS: The patient was studied by prick tests and prick by prick tests. Specific IgE was measured by CAP and by SDS-PAGE/immunoblotting by a diffusion method. RESULTS: The patient showed positive prick by prick tests to pine nuts (12 mm of maximum wheal diameter). Specific IgE was positive (0.79 kU/l). The patient's serum recognized several proteins by immunoblot. However, a 17-kDa allergen band was detected with high intensity. This protein was found to be sensitive to reducing agents, losing its IgE-binding properties after reduction. CONCLUSIONS: The patient presented an IgE-mediated reaction and detected a 17-kDa protein from pine nuts not previously described.

↩

[74] - Miranda M, Bartolomé B, Malheiro D, Cadinha S, Ferraz Oliveira J, Castel-Branco M. Pine nut allergen pattern: monosensitized and polysensitized patients. EAACI 25th Congress, Vienna, 10-14 June, 2006, Poster n°571

Various reports have described pine nut allergens ranging from 68 kDa to 17 kDa. To compare pine nut IgE-binding pattern in two different sample conditions (reducing or non reducing) with serum from an atopic, asthmatic, mono-sensitized pine nut allergic 13-year-age girl (A) and a multisensitized 27-year-age man (B), we performed skin prick test (SPT) and skin prick-to-prick tests (SPTP), Pharmacia CapSystem® and EAST. Allergen molecular mass was studied by SDS-PAGE Immunoblotting following the Laemmli method, in two sample conditions: reducing or non reducing, in presence or absence of 2-mercaptoetanol, respectively. In patient A, SPT using raw pinenut yielded a significant reaction and similar tests to other raw nuts were negative. Specific IgE to Pinus strobus seed = 64 kU/l and to pine-tree (Pinus strobus) pollen < 0,35 KU/l. Serum specific IgE (EAST) to P. judaica pollen = 0,4 kU/L. In patient B, SPT revealed hypersensitivity to walnut, hazelnut, kiwi, peach and peanut. SPTP using raw pine-nut yielded a significant reaction. Serum specific IgE (Pharmacia CapSystem®) to Pinus strobus seed = 4.32 kU/l, peanut (f13) = 1.81 kU/l, (f17)= 2.16 kU/l, carrot (f31) = 1.08 kU/l, banana (f92) = 0.69 kU/l, peach (f95) = 2.33 kU/l, kiwi = 2.38 kU/l and (f256) = 1.59 kU/l. Serum specific specific IgE (EAST) to hazelnut = 5.1 kU/l, walnut = and pollen from Lolium perenne = 9 kU/l, P. judaica < 0.35 kU/l, Betula verrucosa = 0.9 kU/L, Artemisia vulgaris = 10.1 kU/l and Platanus acerifolia = 1.6 kU/l. SDS-PAGE Immunoblotting in non reducing conditions (without 2-mercaptoetanol) revealed a similar IgE-binding pattern with both sera: bands of c.a. 39 kDa, 28/25 kDa (probably double band) and 18/17 kDa (probably double band) were detected. However, in reducing conditions (presence of 2-mercaptoethanol), blot incubated with patient A serum showed three IgE-binding band of 58 kDa, 49 kDa and 32,5 kDa whereas a broad 13 kDa band was detected when patient B serum was used. CONCLUSION: We studied two cases of food hipersensitivity to pine nut, one of them monosensitized and the other multi sensitized. IgE-blot in non reducing conditions revealed the same IgE binding pattern with serum from both patients: bands of 39 kDa, 28/25 kDa and 18/17 kDa, whereas in reducing conditions different IgE binding band pattern was detected, bands of 58 kDa, 49 kDa and 32,5 kDa with serum from monosensitized patient and a 13 kDa band with multisensitized patient serum.

↩

[75] - Garcia-Menaya JM, Gonzalo-Garijo MA, Moneo I, Fernandez B, Garcia-Gonzalez F, Moreno F. A 17 kDa allergen detected in pine nuts. Allergy 2000;55:291-293

Few cases of allergy to pine nuts have been described. We report a case of anaphylactic reaction to pine nuts. The patient needed to be treated in the emergency room due to a systemic reaction immediately after eating pine nuts. METHODS: The patient was studied by prick tests and prick by prick tests. Specific IgE was measured by CAP and by SDS-PAGE/immunoblotting by a diffusion method. RESULTS: The patient showed positive prick by prick tests to pine nuts (12 mm of maximum wheal diameter). Specific IgE was positive (0.79 kU/l). The patient's serum recognized several proteins by immunoblot. However, a 17-kDa allergen band was detected with high intensity. This protein was found to be sensitive to reducing agents, losing its IgE-binding properties after reduction. CONCLUSIONS: The patient presented an IgE-mediated reaction and detected a 17-kDa protein from pine nuts not previously described.

↩

[76] - Barzaga PA, Teuber S, Petersen R. Detection of pine nut allergens by immunoblotting and immunoCAP. ACAAI Annual Meeting, San Antonio, 15-20 Nov. 2002, Poster n° P16

Little is known about pine nut allergens. The purpose of this study was to compare immunoblot detection of pine nut allergens to ImmunoCAP testing (Pharmacia Diagnostics) using sera from 12 patients with a very convincing history of pine nut allergy. All patient sera showed a positive IgE immunoblot to pine nut extract. One patient reported allergy only to pine nuts; the others reported primary allergy to another tree nut but had either systemic reactions or a less severe reaction upon accidental pine nut ingestion. Control sera were obtained from one patient with peanut allergy, one with Aspergillus allergy, and four with significant grass and tree pollen allergy, all of whom tolerated pine nuts. SDS-PAGE and IgE immunoblotting were performed using raw pine nut extract. Sera from grass-allergic patients showed IgE binding to multiple polypeptides above 21 kDa. Serum from the patient sensitive solely to pine nuts showed IgE binding to a polypeptide around 14 kDa in a non-reduced protein preparation and some binding to higher molecular weight proteins. The other patient sera showed binding to either a doublet around 17 kDa or to a lower molecular weight protein at about 10 kDa +/- multiple higher molecular weight polypeptides. Only serum from the patient solely allergic to pine nuts had a significantly positive ImmunoCAP value at 1.83 kU/l and two registered 0.35 kU/l and 0.44 kU/l with the remaining nine <0.35 kU/l. Interestingly, the 4 pollen-allergic control sera showed positive values of 0.50, 1.70, 1.23 and 2.07 kU/l. These findings demonstrate that IgE towards potentially relevant lower molecular weight allergens in pine nut may be poorly detected by ImmunoCAP testing in those patients whose primary allergy is to another tree nut. In addition, grass pollen allergic patients tolerant to pine nuts may have false positive pine nut ImmunoCAP testing. If more patients with anaphylaxis to other tree nuts demonstrate IgE to allergens from 7-10 kDa and 17 kDa, it could imply that either these patients could really tolerate pine nuts if challenged or there are issues of IgE avidity and homologous protein epitopes relevant to clinical cross-reactivity as yet unknown. These findings suggest that pine nut ImmunoCAP tests should be interpreted with caution and correlated with supporting clinical history.

↩

[77] - Ibañez MD, Lombardero M, Martinez san Ireneo M, Muñoz MC. Anaphylaxis induced by pine nuts in two young girls. Pediatr Allergy Immunol 2003;14:317-319

BACKGROUND: The aetiology of food allergy remains unclear. Although failure to develop or breakdown in oral tolerance has been proposed, the existence of physiologic sensitization routes other than the gastrointestinal tract cannot be excluded. OBJECTIVE: The purpose of this study is to clarify whether or not exposure to allergen through the skin can promote food allergy. METHODS: BALB/c mice were shaved on the back, and a patch impregnated with 100 micro g of ovalbumin (OVA) was applied to the dorsal skin for a 1-week period and then removed. After three courses of sensitization, OVA-specific antibodies in sera were measured, and then mice were orally challenged with 50 mg of OVA. Anaphylactic symptoms, plasma histamine levels, and histology of intestines and lungs after oral challenge were examined. RESULTS: Epicutaneous (EC) sensitization of mice to OVA induced a high level of OVA-specific IgE. Subsequent oral challenge with OVA resulted in symptoms of systemic anaphylaxis with elevated levels of plasma histamine as well as histological changes in both intestines and lungs. In the presence of anti-IL-4 antibodies, EC sensitization failed to provoke an IgE response, but still induced a Th2-predominant cellular immune response in lungs after oral challenge. CONCLUSION: We demonstrated for the first time that food allergy can be induced by allergen exposure through the skin. Our results identify a novel role of EC sensitization in the pathogenesis of food allergy.

↩

[78] - Miranda M, Bartolomé B, Malheiro D, Cadinha S, Ferraz Oliveira J, Castel-Branco M. Pine nut allergen pattern: monosensitized and polysensitized patients. EAACI 25th Congress, Vienna, 10-14 June, 2006, Poster n°571

Various reports have described pine nut allergens ranging from 68 kDa to 17 kDa. To compare pine nut IgE-binding pattern in two different sample conditions (reducing or non reducing) with serum from an atopic, asthmatic, mono-sensitized pine nut allergic 13-year-age girl (A) and a multisensitized 27-year-age man (B), we performed skin prick test (SPT) and skin prick-to-prick tests (SPTP), Pharmacia CapSystem® and EAST. Allergen molecular mass was studied by SDS-PAGE Immunoblotting following the Laemmli method, in two sample conditions: reducing or non reducing, in presence or absence of 2-mercaptoetanol, respectively. In patient A, SPT using raw pinenut yielded a significant reaction and similar tests to other raw nuts were negative. Specific IgE to Pinus strobus seed = 64 kU/l and to pine-tree (Pinus strobus) pollen < 0,35 KU/l. Serum specific IgE (EAST) to P. judaica pollen = 0,4 kU/L. In patient B, SPT revealed hypersensitivity to walnut, hazelnut, kiwi, peach and peanut. SPTP using raw pine-nut yielded a significant reaction. Serum specific IgE (Pharmacia CapSystem®) to Pinus strobus seed = 4.32 kU/l, peanut (f13) = 1.81 kU/l, (f17)= 2.16 kU/l, carrot (f31) = 1.08 kU/l, banana (f92) = 0.69 kU/l, peach (f95) = 2.33 kU/l, kiwi = 2.38 kU/l and (f256) = 1.59 kU/l. Serum specific specific IgE (EAST) to hazelnut = 5.1 kU/l, walnut = and pollen from Lolium perenne = 9 kU/l, P. judaica < 0.35 kU/l, Betula verrucosa = 0.9 kU/L, Artemisia vulgaris = 10.1 kU/l and Platanus acerifolia = 1.6 kU/l. SDS-PAGE Immunoblotting in non reducing conditions (without 2-mercaptoetanol) revealed a similar IgE-binding pattern with both sera: bands of c.a. 39 kDa, 28/25 kDa (probably double band) and 18/17 kDa (probably double band) were detected. However, in reducing conditions (presence of 2-mercaptoethanol), blot incubated with patient A serum showed three IgE-binding band of 58 kDa, 49 kDa and 32,5 kDa whereas a broad 13 kDa band was detected when patient B serum was used. CONCLUSION: We studied two cases of food hipersensitivity to pine nut, one of them monosensitized and the other multi sensitized. IgE-blot in non reducing conditions revealed the same IgE binding pattern with serum from both patients: bands of 39 kDa, 28/25 kDa and 18/17 kDa, whereas in reducing conditions different IgE binding band pattern was detected, bands of 58 kDa, 49 kDa and 32,5 kDa with serum from monosensitized patient and a 13 kDa band with multisensitized patient serum.

↩

[79] - Garcia-Menaya JM, Gonzalo-Garijo MA, Moneo I, Fernandez B, Garcia-Gonzalez F, Moreno F. A 17 kDa allergen detected in pine nuts. Allergy 2000;55:291-293

Few cases of allergy to pine nuts have been described. We report a case of anaphylactic reaction to pine nuts. The patient needed to be treated in the emergency room due to a systemic reaction immediately after eating pine nuts. METHODS: The patient was studied by prick tests and prick by prick tests. Specific IgE was measured by CAP and by SDS-PAGE/immunoblotting by a diffusion method. RESULTS: The patient showed positive prick by prick tests to pine nuts (12 mm of maximum wheal diameter). Specific IgE was positive (0.79 kU/l). The patient's serum recognized several proteins by immunoblot. However, a 17-kDa allergen band was detected with high intensity. This protein was found to be sensitive to reducing agents, losing its IgE-binding properties after reduction. CONCLUSIONS: The patient presented an IgE-mediated reaction and detected a 17-kDa protein from pine nuts not previously described.

↩

[80] - Barzaga PA, Teuber S, Petersen R. Detection of pine nut allergens by immunoblotting and immunoCAP. ACAAI Annual Meeting, San Antonio, 15-20 Nov. 2002, Poster n° P16

Little is known about pine nut allergens. The purpose of this study was to compare immunoblot detection of pine nut allergens to ImmunoCAP testing (Pharmacia Diagnostics) using sera from 12 patients with a very convincing history of pine nut allergy. All patient sera showed a positive IgE immunoblot to pine nut extract. One patient reported allergy only to pine nuts; the others reported primary allergy to another tree nut but had either systemic reactions or a less severe reaction upon accidental pine nut ingestion. Control sera were obtained from one patient with peanut allergy, one with Aspergillus allergy, and four with significant grass and tree pollen allergy, all of whom tolerated pine nuts. SDS-PAGE and IgE immunoblotting were performed using raw pine nut extract. Sera from grass-allergic patients showed IgE binding to multiple polypeptides above 21 kDa. Serum from the patient sensitive solely to pine nuts showed IgE binding to a polypeptide around 14 kDa in a non-reduced protein preparation and some binding to higher molecular weight proteins. The other patient sera showed binding to either a doublet around 17 kDa or to a lower molecular weight protein at about 10 kDa +/- multiple higher molecular weight polypeptides. Only serum from the patient solely allergic to pine nuts had a significantly positive ImmunoCAP value at 1.83 kU/l and two registered 0.35 kU/l and 0.44 kU/l with the remaining nine <0.35 kU/l. Interestingly, the 4 pollen-allergic control sera showed positive values of 0.50, 1.70, 1.23 and 2.07 kU/l. These findings demonstrate that IgE towards potentially relevant lower molecular weight allergens in pine nut may be poorly detected by ImmunoCAP testing in those patients whose primary allergy is to another tree nut. In addition, grass pollen allergic patients tolerant to pine nuts may have false positive pine nut ImmunoCAP testing. If more patients with anaphylaxis to other tree nuts demonstrate IgE to allergens from 7-10 kDa and 17 kDa, it could imply that either these patients could really tolerate pine nuts if challenged or there are issues of IgE avidity and homologous protein epitopes relevant to clinical cross-reactivity as yet unknown. These findings suggest that pine nut ImmunoCAP tests should be interpreted with caution and correlated with supporting clinical history.

↩

[81] - Añó MA, Maselli JP, Sanz ML, Fernández-Benítez M. Allergy to pine nut. Allergol Immunopathol (Madr) 2002;30:104-108

↩

[82] - Senna G, Roncarolo D, Dama A, Mistrello G. Anaphylaxis to pine nuts and immunological cross-reactivity with pine pollen proteins. J Investig Allergol Clin Immunol 2000;10:44-46

Despite the wide use of pine nuts, the fruit of Pinus pinea, only a few reports of allergic reactions to them have been published. We present herein a case of food allergy to pine nuts in a patient who showed no clinical symptoms to pine pollen despite the presence in her serum of specific IgE antibodies. In order to verify whether the reaction against pine nuts was IgE mediated, specific IgE against pine nuts and pollen were evaluated by skin-prick test, prick by prick and RAST. Immunoblotting and immunoblotting-inhibition were used to evaluate the allergenic components of both extracts and their cross-reactivity. Prick by prick with fresh pine nuts and RAST with pine nut and pine pollen extracts showed that the patient had high levels of specific IgE against both extracts. Immunoblotting experiments showed the presence in serum of IgE antibodies against several components in pine nuts and pollen. Immunoblotting-inhibition experiments demonstrated the presence of some cross-reacting components. These data confirm the existence of food allergy induced by pine nuts. This sensitization to pine nuts developed with no symptoms of pine pollinosis. Development of pollinosis may require a longer time of exposure to allergens. Based on the cross-reactivity between pine nut and pine pollen extracts, cosensitization to these two allergens could be possible.

↩

[83] - Roux N, Hogendijk S, Hauser C. Severe anaphylaxis to pine nuts. Allergy 1998;53:213-214

↩

[84] - Micheau P, Juchet A, Rancé F, Brémont F, Dutau G. Allergie au pignon de pin. Rev Fr Allergol Immunol Clin 2001;41:348

↩

[85] - de las Marinas D, Vila L, Sanz ML. Allergy to pine nuts. Allergy 1998;53:220-222

↩

[86] - Miranda M, Bartolomé B, Malheiro D, Cadinha S, Ferraz Oliveira J, Castel-Branco M. Pine nut allergen pattern: monosensitized and polysensitized patients. EAACI 25th Congress, Vienna, 10-14 June, 2006, Poster n°571

Various reports have described pine nut allergens ranging from 68 kDa to 17 kDa. To compare pine nut IgE-binding pattern in two different sample conditions (reducing or non reducing) with serum from an atopic, asthmatic, mono-sensitized pine nut allergic 13-year-age girl (A) and a multisensitized 27-year-age man (B), we performed skin prick test (SPT) and skin prick-to-prick tests (SPTP), Pharmacia CapSystem® and EAST. Allergen molecular mass was studied by SDS-PAGE Immunoblotting following the Laemmli method, in two sample conditions: reducing or non reducing, in presence or absence of 2-mercaptoetanol, respectively. In patient A, SPT using raw pinenut yielded a significant reaction and similar tests to other raw nuts were negative. Specific IgE to Pinus strobus seed = 64 kU/l and to pine-tree (Pinus strobus) pollen < 0,35 KU/l. Serum specific IgE (EAST) to P. judaica pollen = 0,4 kU/L. In patient B, SPT revealed hypersensitivity to walnut, hazelnut, kiwi, peach and peanut. SPTP using raw pine-nut yielded a significant reaction. Serum specific IgE (Pharmacia CapSystem®) to Pinus strobus seed = 4.32 kU/l, peanut (f13) = 1.81 kU/l, (f17)= 2.16 kU/l, carrot (f31) = 1.08 kU/l, banana (f92) = 0.69 kU/l, peach (f95) = 2.33 kU/l, kiwi = 2.38 kU/l and (f256) = 1.59 kU/l. Serum specific specific IgE (EAST) to hazelnut = 5.1 kU/l, walnut = and pollen from Lolium perenne = 9 kU/l, P. judaica < 0.35 kU/l, Betula verrucosa = 0.9 kU/L, Artemisia vulgaris = 10.1 kU/l and Platanus acerifolia = 1.6 kU/l. SDS-PAGE Immunoblotting in non reducing conditions (without 2-mercaptoetanol) revealed a similar IgE-binding pattern with both sera: bands of c.a. 39 kDa, 28/25 kDa (probably double band) and 18/17 kDa (probably double band) were detected. However, in reducing conditions (presence of 2-mercaptoethanol), blot incubated with patient A serum showed three IgE-binding band of 58 kDa, 49 kDa and 32,5 kDa whereas a broad 13 kDa band was detected when patient B serum was used. CONCLUSION: We studied two cases of food hipersensitivity to pine nut, one of them monosensitized and the other multi sensitized. IgE-blot in non reducing conditions revealed the same IgE binding pattern with serum from both patients: bands of 39 kDa, 28/25 kDa and 18/17 kDa, whereas in reducing conditions different IgE binding band pattern was detected, bands of 58 kDa, 49 kDa and 32,5 kDa with serum from monosensitized patient and a 13 kDa band with multisensitized patient serum.

↩

[87] - Subba Rao PV, Rajagopal D, Ganesh KA. B- and T-cell epitopes of tropomyosin, the major shrimp allergen. Allergy 1998;53(suppl. 46):44-47

The major crustacean allergen characterized from different species of shrimp is the muscle protein tropomyosin. Two shared epitopes corresponding to 47-63 and 150-158 of the deduced amino-acid sequence of the brown shrimp, M. ensis, were identified as IgE-binding B-cell epitopes. A 21-mer peptide spanning the amino-acid residues 261-281 was identified as a putative T-cell epitope capable of reducing ongoing tropomyosin-specific IgG and IgE responses in a mouse model. These observations suggest that peptide immunotherapy may also be effective in the treatment of food hypersensitivity.

↩

[88] - Ibañez MD, Lombardero M, Martinez san Ireneo M, Muñoz MC. Anaphylaxis induced by pine nuts in two young girls. Pediatr Allergy Immunol 2003;14:317-319

BACKGROUND: The aetiology of food allergy remains unclear. Although failure to develop or breakdown in oral tolerance has been proposed, the existence of physiologic sensitization routes other than the gastrointestinal tract cannot be excluded. OBJECTIVE: The purpose of this study is to clarify whether or not exposure to allergen through the skin can promote food allergy. METHODS: BALB/c mice were shaved on the back, and a patch impregnated with 100 micro g of ovalbumin (OVA) was applied to the dorsal skin for a 1-week period and then removed. After three courses of sensitization, OVA-specific antibodies in sera were measured, and then mice were orally challenged with 50 mg of OVA. Anaphylactic symptoms, plasma histamine levels, and histology of intestines and lungs after oral challenge were examined. RESULTS: Epicutaneous (EC) sensitization of mice to OVA induced a high level of OVA-specific IgE. Subsequent oral challenge with OVA resulted in symptoms of systemic anaphylaxis with elevated levels of plasma histamine as well as histological changes in both intestines and lungs. In the presence of anti-IL-4 antibodies, EC sensitization failed to provoke an IgE response, but still induced a Th2-predominant cellular immune response in lungs after oral challenge. CONCLUSION: We demonstrated for the first time that food allergy can be induced by allergen exposure through the skin. Our results identify a novel role of EC sensitization in the pathogenesis of food allergy.

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[89] - Robotham JM, Wang F, Seamon V, Teuber SS, Sathe SK, Sampson HA, et al. Ana o 3, an important cashew nut (Anacardium occidentale L.) allergen of the 2S albumin family. J Allergy Clin Immunol 2005;115:1284-1290

BACKGROUND: Cashew nut allergy is the second most commonly reported tree nut allergy in the United States. We have previously cloned and characterized major cashew allergens belonging to the vicilin and legumin families of seed storage proteins . OBJECTIVE: Here we set out to describe a third major cashew allergen, a 2S albumin . METHODS: The recombinant cashew 2S albumin was amplified from a cDNA library by means of PCR, sequenced, and expressed in Escherichia coli. Immunoblotting was used to screen for reactivity with patients' sera, and inhibition immunoblotting was used to identify the corresponding native cashew nut proteins. The mass of affinity-purified native allergen was determined by means of matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectroscopy. Patients' sera were used to probe solid-phase 2S albumin peptides to identify linear epitopes . RESULTS: The cloned allergen, designated Ana o 3, was identified as 2S albumin. MALDI-TOF mass spectroscopy of native Ana o 3 yielded a molecular mass of 12,598 d. Immunoblot analysis showed 21 (81%) of 26 sera from patients with cashew allergy were reactive. Three native Ana o 3 large-subunit isoforms with molecular weights ranging from approximately 6 to 10 kd were identified. Probing of overlapping synthetic Ana o 3 peptides with patients' sera identified 16 reactive peptides, 4 of which gave strong signals and one of which positionally overlaps linear epitopes in mustard and walnut allergenic 2S albumins. The overlapping cashew and walnut epitopes also share considerable homology . CONCLUSIONS: We conclude that this 2S albumin protein is a major allergen in cashew nut and demonstrates a possible basis for cross-reactivity with walnut 2S albumin.

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[90] - Bublin M, Mari A, Ebner C, Knulst A, Scheiner O, Hoffmann-Sommergruber K, et al. IgE sensitization profiles toward green and gold kiwifruits differ among patients allergic to kiwifruit from 3 European countries. J Allergy Clin Immunol 2004;114:1169-1175

Background Kiwifruits have become a major elicitor of plant food allergy. Until recently, the only species of kiwifruit grown commercially was the common green-fleshed Actinidia deliciosa cv Hayward. In 1999, the yellow-fleshed cultivar Actinidia chinensis cv Hort16A was introduced into the international market. Objective : We compared the allergen compositions of green and gold kiwifruits and assessed the sensitization patterns of patients with kiwifruit allergy toward both varieties. Method s : Sera from 90 patients with kiwifruit allergy from Austria, central Italy, and the Netherlands were tested for IgE binding to green and gold kiwifruit protein extracts and to purified actinidin, the major kiwifruit allergen, by ELISA. In addition, ELISA inhibitions and immunoblots were performed with selected sera. Relevant allergens were identified by N-terminal sequencing and immunoblotting with allergen-specific antibodies. Result s : IgE immunoblotting showed marked differences in the allergen compositions of green and gold kiwifruit extracts. Phytocystatin, a novel plant food allergen, and a thaumatin-like protein were identified as allergens common for both cultivars. Two allergens with homologies to chitinases were found in gold kiwifruits, whereas actinidin was detected exclusively in green kiwifruits. Patients from Central Europe and central Italy showed distinct sensitization profiles toward green and gold kiwifruit extracts as well as actinidin. Whereas sera from Austrian and Dutch patients mainly recognized green kiwifruit extract and actinidin, almost all Italian sera showed IgE binding to both kiwifruit species, but only half of them contained actinidin-specific IgE. Green and gold kiwifruit extracts were shown to be highly cross-reactive as determined by IgE ELISA inhibition. Conclusion : The presence of common allergens and the IgE cross-reactivity to green kiwifruit qualifies gold kiwifruit as a potential new allergen source for patients allergic to green kiwifruits.

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[91] - Dalal I, Binson I, Levine A, Somekh E, Ballin A, Reifen R. The pattern of sesame sensitivity among infants and children. Pediatr Allergy Immunol 2003;14:312-316

Recently, we found sesame to be a major cause of severe IgE-mediated food allergic reactions among infants and young children in Israel. The purpose of this study was to describe the different patterns of sesame sensitivity. We have identified three subgroups among our patients (n = 32). Group I (n = 23, M/F; 14/9) consisted of cases with IgE-mediated sesame allergy. The mean age of the first allergic reaction was 11.7 months. Although the main clinical manifestation was urticaria/angiedema (n = 14, 60%), anaphylaxis was the presenting symptom in seven (30%) patients; all of them were younger than 1 year. Sixteen (70%) were found to be allergic to other foods, and other atopic diseases were identified in 18 (78%) patients. Three patients 'outgrew' their allergy within 1-2 years. Group II (n = 2) included cases in whom sesame allergy was ruled out based on a negative skin prick test (SPT) together with a negative open oral challenge. Group III (n = 7) consisted of patients that were found to be SPT positive for sesame as part of a screening for other food allergies. Although sesame products have become fashionable in westernized countries, early exposure may cause sesame to share eventually the same 'noteriety and fate' as peanut - a major cause of severe food allergic reactions.

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[92] - Wallowitz M, Peterson WR, Uratsu S, Comstock SS, Dandekar AM, Teuber SS. Jug r 4, a Legumin Group Food Allergen from Walnut (Juglans regia Cv. Chandler). J Agric Food Chem 2006;54:8369-8375

Allergy to walnut is the most frequently reported tree nut allergy in the United States. Walnut 2S albumin, a vicilin-like protein, and a lipid transfer protein allergen have previously been described. Our objective was to clone and express a cDNA encoding a legumin group protein, assess IgE-binding with sera from walnut allergic patients, and investigate cross-reactivity with selected nuts. Primers were used to obtain the cDNA by 5' and 3' rapid amplification of cDNA ends from walnut mRNA. The cDNA was subcloned into the pMAL-c2X vector and the recombinant fusion protein, named rJug r 4, was expressed in Escherichia coli. The obtained cDNA encoded a precursor protein with a predicted molecular weight of 58.1 kD, which showed significant sequence homology to hazelnut and cashew legumin allergens. Serum IgE from 21 of 37 (57%) patients bound the rJug r 4 fusion protein. In vitro cross-reactivity was demonstrated with hazelnut, cashew, and peanut protein extracts.

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[93] - Subba Rao PV, Rajagopal D, Ganesh KA. B- and T-cell epitopes of tropomyosin, the major shrimp allergen. Allergy 1998;53(suppl. 46):44-47

The major crustacean allergen characterized from different species of shrimp is the muscle protein tropomyosin. Two shared epitopes corresponding to 47-63 and 150-158 of the deduced amino-acid sequence of the brown shrimp, M. ensis, were identified as IgE-binding B-cell epitopes. A 21-mer peptide spanning the amino-acid residues 261-281 was identified as a putative T-cell epitope capable of reducing ongoing tropomyosin-specific IgG and IgE responses in a mouse model. These observations suggest that peptide immunotherapy may also be effective in the treatment of food hypersensitivity.

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[94] - de las Marinas D, Vila L, Sanz ML. Allergy to pine nuts. Allergy 1998;53:220-222

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[95] - Jansen A, Vermeulen A, Dieges PH, Van Toorenenbergen AW. Allergy to pine nuts in a bird fancier. Allergy 1996;51:741-744

A patient is described with the bird-egg syndrome who experienced an anaphylactic reaction after eating some of her parrot's food (pine nuts: Pinus pinea). Specific IgE against this nut and another pine nut (P. cembra) was demonstrated by RAST. Cross-reactivity between these botanically related seeds was shown by RAST inhibition. Besides avian antigens, bird food antigens should be taken into consideration when symptoms of allergy occur on exposure to birds.

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[96] - Añó MA, Maselli JP, Sanz ML, Fernández-Benítez M. Allergy to pine nut. Allergol Immunopathol (Madr) 2002;30:104-108

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[97] - Ibañez MD, Lombardero M, Martinez san Ireneo M, Muñoz MC. Anaphylaxis induced by pine nuts in two young girls. Pediatr Allergy Immunol 2003;14:317-319

BACKGROUND: The aetiology of food allergy remains unclear. Although failure to develop or breakdown in oral tolerance has been proposed, the existence of physiologic sensitization routes other than the gastrointestinal tract cannot be excluded. OBJECTIVE: The purpose of this study is to clarify whether or not exposure to allergen through the skin can promote food allergy. METHODS: BALB/c mice were shaved on the back, and a patch impregnated with 100 micro g of ovalbumin (OVA) was applied to the dorsal skin for a 1-week period and then removed. After three courses of sensitization, OVA-specific antibodies in sera were measured, and then mice were orally challenged with 50 mg of OVA. Anaphylactic symptoms, plasma histamine levels, and histology of intestines and lungs after oral challenge were examined. RESULTS: Epicutaneous (EC) sensitization of mice to OVA induced a high level of OVA-specific IgE. Subsequent oral challenge with OVA resulted in symptoms of systemic anaphylaxis with elevated levels of plasma histamine as well as histological changes in both intestines and lungs. In the presence of anti-IL-4 antibodies, EC sensitization failed to provoke an IgE response, but still induced a Th2-predominant cellular immune response in lungs after oral challenge. CONCLUSION: We demonstrated for the first time that food allergy can be induced by allergen exposure through the skin. Our results identify a novel role of EC sensitization in the pathogenesis of food allergy.

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[98] - Oppel T, Thomas P, Wollenberg A. Cross-Sensitization between Poppy Seed and Buckwheat in a Food-Allergic Patient with Poppy Seed Anaphylaxis. Int Arch Allergy Immunol 2006;140:170-173

The opium poppy, Papaver somniferum L., is the source of both poppy seeds and opium. The commercially available seeds are widely used as ingredients for various kinds of food. IgE-mediated sensitization to poppy seeds is rare, but, if present, clinical symptoms are usually severe. Cross-sensitizations between poppy seeds and other food allergens have been described with sesame, hazelnut, rye grain and kiwi fruit. We report the case of a 17-year-old female with an apparently food-allergic reaction after ingestion of a poppy seed cake. Allergological workup revealed a poppy seed anaphylaxis and led to the identification of a novel cross-sensitization with buckwheat.

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[99] - Keskin O, Sekerel BE. Poppy seed allergy: a case report and review of the literature. Allergy Asthma Proc 2006;27:396-398

Seeds of the poppy plant are traditionally used in bakeries, e.g., for garnishing bread or making cakes. Reports of allergic type I sensitivity to poppy seed are rare. According to the literature, severe reactions may occur, affecting mainly patients with allergy to pollens or nuts. We report on a 16-year-old boy who has developed erythema and angioedema, conjunctivitis, and dyspnea due to inhalation of poppy seed. Skin-prick tests were positive for poppy seed, hazelnut, and chickpea. The concentration of specific IgE for poppy seed, hazelnut, and peanut were 3.36 kU/L (class 2), 1.5 kU/L (class 2), and 6.17 kU/L (class 3), respectively. Allergic reactions associated with inhalation of food allergens have been reported for some foods but not for poppy seed. This is the first report on inhalative allergy to the poppy seed. Although poppy seeds are not commonly used, we underline the possible importance of such rare and often hidden sources of allergens, especially in patients with nut allergy.

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[100] - Besler M, Hefle SL, Jensen-Jarolim E. Allergen Data Collection: poppy Seed (Papaver somniferum). Internet Symp Food Allergens 2001;3(2):87-92

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[101] - Wüthrich B. Epidemiologie der Allergien in der Schweiz. Ther Umsch 2001;58:253-258

The Swiss Study on Air Pollution and Lung Diseases in Adults (SAPALDIA) was carried out during 1991-1993 in eight Swiss areas with different environmental characteristics. The cross-sectional examination included 9651 adults, aged 18-60 years, who all participated in a detailed interview. In 8357 subjects complete allergy skin and in-vitro tests were available in addition. The prevalence of atopic sensitization (positive skin prick test to any of the tested inhalant allergens and/or a positive Phadiatop as an in-vitro screening test for atopy) was 32.3%, with a higher prevalence in males (35.7%) than in females (28.8%). Skin sensitization was predominantly caused by grass pollen (12.7%), followed by house dust mite (8.9%), silver birch pollen (7.9%) and cat epithelia (3.8%). 11.1% suffered from current hay fever, 6.8% from asthma, 4.5% from atopic asthma. Smokers had statistically significant (p < 0.001) higher mean serum IgE concentrations (geometric mean 39.7 kU/l) than nonsmokers (27.2 kU/l), In Phadiatop positive subjects, the IgE levels were highest, with a mean of 104.3 kU/l (99.0-109.8). The SCARPOL Study (Swiss Study on Childhood Allergy and Respiratory Symptoms with respect to Air Pollution and Climate) ist based on a sample of 4470 children from 10 different areas who completed parenteral questionnaire. 35.7% of the 2879 children who underwent skin prick testing were sensitized to at least one tested aeroallergen, 22.5% to gras pollen, 12.4% to house dust mites, 11.4% to birch pollen and 6.4% to cat epithelia. 17% of the 13- to 15-year-old (8th grade) suffered from hayfever. The prevalence of asthma (ever) for the whole sample was 9%, without differences between the age groups. The lifetime prevalence of atopic dermatitis was 13% and the current prevalence 8%. The risk of eczema was higher in Swiss children than in children of immigrants, in infants with a birthweight below 2500 g, in children with a positive family history of atopic dermatitis, and in children from higher socioeconomic classes. Farm children (n = 133) living in a rural area suffer less frequently from pollinosis (2.4%) and bronchial asthma (1.6%) than children (n = 966) with no direct contact to agriculture, but living in the same area (prevalence of hayfever 18.3%, of asthma 9.1%). This figures are similar to results from former East and Western Germany and from the former USSR and Baltic areas. These large Swiss epidemiologic studies confirmed both, the high prevalence of atopy and atopic diseases, and the health impact of moderate air pollution levels and of factors associated with the 'western lifestyle'.

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[102] - Osterballe M, Hansen TK, Mortz CG, Bindslev-Jensen C. The clinical relevance of sensitization to pollen-related fruits and vegetables in unselected pollen-sensitized adults. Allergy 2005;60:218-225

BACKGROUND: Previous studies have described cross-reactivity between fresh fruits, vegetables and pollen. However, no data demonstrates the clinical relevance of sensitization to pollen-related fruits and vegetables in unselected pollen-sensitized adults with and without symptoms in the pollen season . OBJECTIVE: The aim of this study was to estimate the clinical relevance of sensitization to pollen-related fruits and vegetables in unselected pollen-sensitized adults and to examine the diagnostic value of skin-prick test (SPT), histamine release and specific IgE compared with the outcome of oral challenge . METHODS: In total, 936 unselected adults (female : male 479 : 457, median age 33.7 years) were examined for pollen sensitization and clinical cross-reactivity with pollen-related fruits and vegetables by questionnaire, SPT, histamine release, specific IgE and oral challenge . RESULTS: The prevalence of pollen sensitization was 23.8% (n = 223). The probability of a clinical reaction to pollen-related foods in the respective pollen-sensitized groups was: 24% (birch), 4% (grass), 10% (mugwort), 35% (birch + grass), 8% (grass + mugwort) and 52% (birch + grass + mugwort). The odds ratio of a clinical reaction to pollen-related fruits and vegetables in symptomatic pollen-sensitized adults was as high as four times (birch + grass) the odds ratio of a clinical reaction in asymptomatic pollen-sensitized adults . CONCLUSION: This study not only demonstrates a high prevalence of clinical reactions to fruits and vegetables in pollen-sensitized adults, but also a discrepancy between the prevalence of sensitization to fruits and vegetables and the clinical relevance in different pollen-sensitized groups with symptoms in the pollen season as a significant factor.

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[103] - Jensen-Jarolim E, Gerstmayer G, Kraft D, Scheiner O, Ebner H, Ebner C. Serological characterization of allergens in poppy seeds. Clin Exp Allergy 1999;29:1075-1079

BACKGROUND AND OBJECTIVE: Poppy seeds in food can induce immediate-type allergic reactions ranging from mild local symptoms to severe anaphylactic reactions. Previous publications showed that poppy seeds cross-react with other plant-derived allergens. The IgE-binding components have not been defined so far. METHODS: We analysed sera from 11 patients with adverse reactions after ingestion of poppy seed-containing food by IgE-immunoblotting. Nine of 11 patients showed concomitant IgE binding to allergens of birch, mugwort or grass pollen in RAST-CAP, and suffered from characteristic seasonal symptoms. RESULTS: Ten of 11 patients showed IgE binding to a 45-kDa protein, 4/11 to a 34-kDa, 5/11 to a 17-kDa, 5/11 to a 14-kDa, and 3/11 to a 5-kDa component. Furthermore, individual IgE binding to proteins of 20, 25, 30 and 40 kDa proteins could be observed. Periodate treatment of blots markedly reduced the IgE binding capacity of the 40- and 45-kDa compounds, indicating the existence of IgE epitopes of the carbohydrate type. Inhibition studies indicated the presence of homologues of pollen allergens in extracts from poppy seeds, i.e. Bet v 1 and Bet v 2. CONCLUSION: The serological analysis showed IgE binding to protein and sugar components of poppy seeds. The 40- and 45-kDa allergens are glycoproteins and contain IgE binding carbohydrate moieties. Moreover, cross-reacting homologues of pollen allergens including Bet v 1 and profilin were detected in poppy seed extract.

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[104] - Frantzen B, Bröcker EB, Trautmann A. Immediate-type allergy caused by poppy seed. Allergy 2000;55:97-98

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[105] - Oppel T, Thomas P, Wollenberg A. Cross-Sensitization between Poppy Seed and Buckwheat in a Food-Allergic Patient with Poppy Seed Anaphylaxis. Int Arch Allergy Immunol 2006;140:170-173

The opium poppy, Papaver somniferum L., is the source of both poppy seeds and opium. The commercially available seeds are widely used as ingredients for various kinds of food. IgE-mediated sensitization to poppy seeds is rare, but, if present, clinical symptoms are usually severe. Cross-sensitizations between poppy seeds and other food allergens have been described with sesame, hazelnut, rye grain and kiwi fruit. We report the case of a 17-year-old female with an apparently food-allergic reaction after ingestion of a poppy seed cake. Allergological workup revealed a poppy seed anaphylaxis and led to the identification of a novel cross-sensitization with buckwheat.

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[106] - Keskin O, Sekerel BE. Poppy seed allergy: a case report and review of the literature. Allergy Asthma Proc 2006;27:396-398

Seeds of the poppy plant are traditionally used in bakeries, e.g., for garnishing bread or making cakes. Reports of allergic type I sensitivity to poppy seed are rare. According to the literature, severe reactions may occur, affecting mainly patients with allergy to pollens or nuts. We report on a 16-year-old boy who has developed erythema and angioedema, conjunctivitis, and dyspnea due to inhalation of poppy seed. Skin-prick tests were positive for poppy seed, hazelnut, and chickpea. The concentration of specific IgE for poppy seed, hazelnut, and peanut were 3.36 kU/L (class 2), 1.5 kU/L (class 2), and 6.17 kU/L (class 3), respectively. Allergic reactions associated with inhalation of food allergens have been reported for some foods but not for poppy seed. This is the first report on inhalative allergy to the poppy seed. Although poppy seeds are not commonly used, we underline the possible importance of such rare and often hidden sources of allergens, especially in patients with nut allergy.

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[107] - Jensen-Jarolim E, Gerstmayer G, Kraft D, Scheiner O, Ebner H, Ebner C. Serological characterization of allergens in poppy seeds. Clin Exp Allergy 1999;29:1075-1079

BACKGROUND AND OBJECTIVE: Poppy seeds in food can induce immediate-type allergic reactions ranging from mild local symptoms to severe anaphylactic reactions. Previous publications showed that poppy seeds cross-react with other plant-derived allergens. The IgE-binding components have not been defined so far. METHODS: We analysed sera from 11 patients with adverse reactions after ingestion of poppy seed-containing food by IgE-immunoblotting. Nine of 11 patients showed concomitant IgE binding to allergens of birch, mugwort or grass pollen in RAST-CAP, and suffered from characteristic seasonal symptoms. RESULTS: Ten of 11 patients showed IgE binding to a 45-kDa protein, 4/11 to a 34-kDa, 5/11 to a 17-kDa, 5/11 to a 14-kDa, and 3/11 to a 5-kDa component. Furthermore, individual IgE binding to proteins of 20, 25, 30 and 40 kDa proteins could be observed. Periodate treatment of blots markedly reduced the IgE binding capacity of the 40- and 45-kDa compounds, indicating the existence of IgE epitopes of the carbohydrate type. Inhibition studies indicated the presence of homologues of pollen allergens in extracts from poppy seeds, i.e. Bet v 1 and Bet v 2. CONCLUSION: The serological analysis showed IgE binding to protein and sugar components of poppy seeds. The 40- and 45-kDa allergens are glycoproteins and contain IgE binding carbohydrate moieties. Moreover, cross-reacting homologues of pollen allergens including Bet v 1 and profilin were detected in poppy seed extract.

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[108] - Frantzen B, Bröcker EB, Trautmann A. Immediate-type allergy caused by poppy seed. Allergy 2000;55:97-98

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[109] - Fontaine JF, Lavaud F, Deslée G, Sabouraud D, Lebargy F. Allergie alimentaire à la graine de lin: à propos d'un cas. Rev Fr Allergol Immunol Clin 2006;46:375

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[110] - León F, Rodríguez M, Cuevas M. The major allergen of linseed. Allergy 2002;57:968

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[111] - Gall H. Food-dependent exercise-induced anaphylaxis to flaxseed. Allergol Int 2000;49:219-221

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[112] - Tubella LM, Marco FM, Lopez T, Sempere JM, Pruñonosa J. Bronchospasm induced by linseed. EAACI 22th Congress, Paris, 7-11 June, 2003, Poster n°1248

Flax (Linum usitatissimum) is a plant belonging to the Linaceae family widely used in the textile industry. The seeds from flax are a source of vegetable oil with industrial and medicinal uses. In addition whole seeds are used as a laxative. There are few reports on allergic reactions to flaxseed, mainly anaphylaxis following intake of oil, seed grains or bread, not associated to other food allergies. We describe a case of flaxseed allergy in an atopic patient sensitized to cereal flours. Case Report: A 33 year-old male developed dyspnea and wheezing some minutes after taking for the first time a spoonful of flax seeds prescribed as a laxative. The patient was followed at our clinic because occupational asthma and rhinitis. Seven years before, when working as a baker, he developed asthma and rhinitis and was diagnosed of occupational asthma by sensitization to multiple flours. The patient moved to a different job with a marked improvement of his clinical condition. Methods: Skin prick tests (SPT) were performed with a battery of commercial inhalant allergens and flours (IPI, SA, Madrid, Spain). We prepared a saline extract from linseed at 20% (w/v) in PBS. This extract was used for SPT and specific IgE determinations (ELISA on CNBr activated cellulose discs). Allergens were analyzed by 15% SDS-PAGE and western blot on nitrocellulose membranes. Results: SPTs were positive to house dust mites, cat, dog, grass and weeds pollens (Artemisia and Chenopodium). SPT was also positive to flours from wheat, oat, barley, rye, maize and rice. Linseed extract (2.5 mg/ml) induced a positive reaction (9 mm wheal) and was negative in a group of 6 atopic patients. IgE was positive to linseed (2.4 kU/l). SDS-PAGE revealed an heterogeneous pattern of multiple protein bands. In contrast immunoblotting showed IgE binding to a single low molecular weight band at about 12 kd. Conclusions: We describe a patient with bronchospasm induced by oral intake of flax seeds, whose sensitization may be related to previous sensitization to cereal flours. Other groups have found linseed allergens ranging from 20 to about 175 kd. In a single case report of anaphylaxis after ingestion of flax seeds an allergen of about 56 kd was found. Our finding of a low molecular weight allergen (12 kd) could represent a differential feature of this case, attributable to a different origin of sensitization.

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[113] - Gall H. Food-dependent exercise-induced anaphylaxis to flaxseed. Allergol Int 2000;49:219-221

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[114] - Kanny G. Le ricin et ses dérivés, un allergène ubiquitaire …. Alim'Inter 2002;7:65-66

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[115] - Besançon S, Kanny G. Ricin. Alim'Inter 2002;7:81-84

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[116] - Navarro-Rouimi R, Charpin D. Anaphylactic reaction to castor bean seeds. Allergy 1999;54:1117

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[117] - Singh A, Panzani RC, Singh AB. Specific IgE to castor bean (Ricinus communis) pollen in the sera of clinically sensitive patients to seeds. J Investig Allergol Clin Immunol 1997;7:169-174

Human sensitization to castor bean seeds in occupational workers and people living close to oil processing factories has been acknowledged for a long time. In view of the crossreactivity among different plant parts of the same species, we studied crossreactivity between seeds of castor bean and its pollen at the molecular level. Sera from 26 seed-positive atopics, when analyzed for ELISA aganist seed and pollen extracts of castor bean, showed binding with both seed and pollen extracts, but binding was stronger with seed extracts as compared to pollen. ELISA inhibition revealed partial similarity as pollen extract could not achieve 90% inhibition even at 100 ug/ml, and remained the same alter protein concentrations of 40 ug/ml. Antigenic extracts of seeds and pollen separated into 12 and 20 fractions on SDS-PAGE, respectively. The 26 sera studied for specific IgE binding to different fractions of seed and pollen extracts showed IgE binding in 17 and 16 cases respectively, but with weak binding to pollen fractions. The crossreactivity was confirmed with pooled sera by blot inhibition. Seed antigen completely inhibited the sera for specific IgE at 10 mg/ml protein while pollen antigen showed only partial inhibition. Crossreactivity and presence of common epitopes between seed and pollen extracts are confirmed

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[118] - Palosuo T, Panzani R, Singh AB, Alenius H, Turjanmaa K. Allergen cross-reactivity between proteins of the latex from Hevea brasiliensis, seeds and pollen of Ricinus communis, and pollen of Mercurialis annua, members of the Euphorbiaceae family. Allergy Asthma Proc 2002;23:141-147

Allergen cross-reactions among three strongly sensitizing Euphorbiaceae species, i.e., the rubber tree (Hevea brasiliensis), castor bean (Ricinus communis), and the Mediterranean weed Mercurialis annua were studied in Finnish patients (n = 25) allergic to natural rubber latex (NRL), but with no known exposure to castor bean or M. annua, and French patients allergic to castor bean (n = 26) or to M. annua (n = 9), but not to NRL. In immunoglobulin E (IgE)-immunoblotting, 28% of NRL-allergic patient sera recognized castor bean seed and 48% reacted to castor bean pollen proteins. Likewise, 35% of the NRL-allergic patient sera bound to M. annua pollen allergens. Nineteen percent of castor bean-allergic patients showed IgE to NRL and 8% to M. annua proteins. Sera from patients allergic to M. annua reacted in 44% to NRL, in 56% to castor bean seed, and in 78% to castor bean pollen proteins. In immunoblotting, castor bean seed extract inhibited the binding of NRL-reactive IgE to 20 kDa, 30 kDa of NRL, and 55 kDa of proteins; NRL extract, in turn, inhibited the binding of castor bean- reactive IgE to 14, 21-22, 29, and 32-34 kDa of castor bean proteins. In ELISA inhibition, NRL extract inhibited 33% of the binding of M. annua--reactive IgE of pooled sera to M. annua pollen. In conclusion, allergen cross-reactivity in vitro was observed among three botanically related Euphorbiaceae members, H. brasiliensis, R. communis, and M. annua, but the molecular specificity of the observed cross-reactions as well as their clinical significance remains to be elucidated. Allergen cross-reactivity should be taken into account in diagnostic work.

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[119] - Bashir ME, Hubatsch I, Leinenbach HP, Zeppezauer M, Panzani RC, Hussein IH. Ric c 1 and Ric c 3, the allergenic 2S albumin storage proteins of Ricinus communis: complete primary structures and phylogenetic relationships. Int Arch Allergy Immunol 1998;115:73-82

The 2S albumin storage protein of Ricinus communis consists of the two heterodimeric proteins Ric c 1 and Ric c 3 each of which is composed of a small and a large subunit linked together by disulphide bridges. The complete primary structures of both heterodimeric proteins were determined by enzymatic degradation and automated Edman degradation. The sequences of all four chains correspond to the known cDNA sequence of the gene of a presumed precursor molecule and to the previously determined partial sequences for Ric c 1 and Ric c 3. In addition, few differences in amino acid positions were found which seem to be related to different varieties of R. communis. Sequence comparisons with 2S albumin from other plant genera revealed high degrees of homology and support the view of a common genetic origin of this protein family. Ric c 1 and Ric c 3 which have 11,212 and 12,032 daltons, respectively, share a similar molecular size, biological function and allergenicity with the 2S albumins from Brassica juncea (Braj 1E) and Sinapis alba L (Sin a 1). Ric c 1 and Ric c 3 may be classified as isoallergens if, additionally, the high degree of similarity in the position of polar residues is taken into account.

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[120] - Thorpe SC, Kemeny DM, Panzani RC, McGurl B, Lord M. Allergy to castor bean. II. Identification of the major allergens in castor bean seeds. J Allergy Clin Immunol 1988;82:67-72

Castor bean proteins were separated and identified by isoelectric focusing and sodium dodecyl sulfate-polyacrylamide gel electrophoresis and blotted onto nitrocellulose paper. The capacity of the castor bean proteins to bind human IgE was probed with sera from castor bean-sensitive patients and radiolabeled anti-IgE. It proved difficult to identify allergens with isoelectric focusing. However, three allergens were identified when proteins were first separated on sodium dodecyl sulfate-polyacrylamide gel electrophoresis: the 2S storage albumin, the 11S crystalloid proteins, and a third protein doublet with molecular weights of 47 and 51 kd. Specific IgE antibody to the 2S storage albumin, measured by RAST, was detected in most (96%) castor bean-sensitive patients, confirming it as the major allergen. We would like to suggest that the 2S albumin be named Ric c I, that the crystalloid proteins be named Ric c II, and that the 47/51 kd doublet be named allergen 3.

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[121] - Thorpe SC, Kemeny DM, Panzani RC, McGurl B, Lord M. Allergy to castor bean. II. Identification of the major allergens in castor bean seeds. J Allergy Clin Immunol 1988;82:67-72

Castor bean proteins were separated and identified by isoelectric focusing and sodium dodecyl sulfate-polyacrylamide gel electrophoresis and blotted onto nitrocellulose paper. The capacity of the castor bean proteins to bind human IgE was probed with sera from castor bean-sensitive patients and radiolabeled anti-IgE. It proved difficult to identify allergens with isoelectric focusing. However, three allergens were identified when proteins were first separated on sodium dodecyl sulfate-polyacrylamide gel electrophoresis: the 2S storage albumin, the 11S crystalloid proteins, and a third protein doublet with molecular weights of 47 and 51 kd. Specific IgE antibody to the 2S storage albumin, measured by RAST, was detected in most (96%) castor bean-sensitive patients, confirming it as the major allergen. We would like to suggest that the 2S albumin be named Ric c I, that the crystalloid proteins be named Ric c II, and that the 47/51 kd doublet be named allergen 3.

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[122] - Palosuo T, Panzani R, Singh AB, Alenius H, Turjanmaa K. Allergen cross-reactivity between proteins of the latex from Hevea brasiliensis, seeds and pollen of Ricinus communis, and pollen of Mercurialis annua, members of the Euphorbiaceae family. Allergy Asthma Proc 2002;23:141-147

Allergen cross-reactions among three strongly sensitizing Euphorbiaceae species, i.e., the rubber tree (Hevea brasiliensis), castor bean (Ricinus communis), and the Mediterranean weed Mercurialis annua were studied in Finnish patients (n = 25) allergic to natural rubber latex (NRL), but with no known exposure to castor bean or M. annua, and French patients allergic to castor bean (n = 26) or to M. annua (n = 9), but not to NRL. In immunoglobulin E (IgE)-immunoblotting, 28% of NRL-allergic patient sera recognized castor bean seed and 48% reacted to castor bean pollen proteins. Likewise, 35% of the NRL-allergic patient sera bound to M. annua pollen allergens. Nineteen percent of castor bean-allergic patients showed IgE to NRL and 8% to M. annua proteins. Sera from patients allergic to M. annua reacted in 44% to NRL, in 56% to castor bean seed, and in 78% to castor bean pollen proteins. In immunoblotting, castor bean seed extract inhibited the binding of NRL-reactive IgE to 20 kDa, 30 kDa of NRL, and 55 kDa of proteins; NRL extract, in turn, inhibited the binding of castor bean- reactive IgE to 14, 21-22, 29, and 32-34 kDa of castor bean proteins. In ELISA inhibition, NRL extract inhibited 33% of the binding of M. annua--reactive IgE of pooled sera to M. annua pollen. In conclusion, allergen cross-reactivity in vitro was observed among three botanically related Euphorbiaceae members, H. brasiliensis, R. communis, and M. annua, but the molecular specificity of the observed cross-reactions as well as their clinical significance remains to be elucidated. Allergen cross-reactivity should be taken into account in diagnostic work.

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[123] - Palosuo T, Panzani R, Singh AB, Alenius H, Turjanmaa K. Allergen cross-reactivity between proteins of the latex from Hevea brasiliensis, seeds and pollen of Ricinus communis, and pollen of Mercurialis annua, members of the Euphorbiaceae family. Allergy Asthma Proc 2002;23:141-147

Allergen cross-reactions among three strongly sensitizing Euphorbiaceae species, i.e., the rubber tree (Hevea brasiliensis), castor bean (Ricinus communis), and the Mediterranean weed Mercurialis annua were studied in Finnish patients (n = 25) allergic to natural rubber latex (NRL), but with no known exposure to castor bean or M. annua, and French patients allergic to castor bean (n = 26) or to M. annua (n = 9), but not to NRL. In immunoglobulin E (IgE)-immunoblotting, 28% of NRL-allergic patient sera recognized castor bean seed and 48% reacted to castor bean pollen proteins. Likewise, 35% of the NRL-allergic patient sera bound to M. annua pollen allergens. Nineteen percent of castor bean-allergic patients showed IgE to NRL and 8% to M. annua proteins. Sera from patients allergic to M. annua reacted in 44% to NRL, in 56% to castor bean seed, and in 78% to castor bean pollen proteins. In immunoblotting, castor bean seed extract inhibited the binding of NRL-reactive IgE to 20 kDa, 30 kDa of NRL, and 55 kDa of proteins; NRL extract, in turn, inhibited the binding of castor bean- reactive IgE to 14, 21-22, 29, and 32-34 kDa of castor bean proteins. In ELISA inhibition, NRL extract inhibited 33% of the binding of M. annua--reactive IgE of pooled sera to M. annua pollen. In conclusion, allergen cross-reactivity in vitro was observed among three botanically related Euphorbiaceae members, H. brasiliensis, R. communis, and M. annua, but the molecular specificity of the observed cross-reactions as well as their clinical significance remains to be elucidated. Allergen cross-reactivity should be taken into account in diagnostic work.

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Graines de tournesol

Pignons de pin

Graines de pavot

Graines de lin

Graines de ricin

Rubriques