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Divers aliments végétaux
mercredi 15 septembre 2010, par
L’épinard et autres Amaranthacées
L’épinard (Spinacia oleracea) est une Chénopodiacée, famille actuellement rangée dans les Amaranthacées.
Cette famille botanique est la source d’autres produits alimentaires comme la betterave, la bette (ou carde), la salicorme ou le quinoa :
- le quinoa a fait l’objet de peu d’observations :
- un enfant allergique à la farine de blé et présentant de nombreux test cutanés positifs pour les céréales ainsi que pour le quinoa
- un adulte pollinique avec anaphylaxie due au quinoa, chez qui il a été suspecté une réactivité pour la chénopodine (11S globuline)
- un enfant allergique à la farine de blé et présentant de nombreux test cutanés positifs pour les céréales ainsi que pour le quinoa
- dans la betterave une protéine Hev b 5-like a été repérée , mais une association latex-betterave n’est pas démontrée
- un cas d’allergie à la betterave chez un enfant de 10 ans polyopéré a été décrit , mais le test cutané était négatif pour le latex
- un cas aussi dans le Réseau d’Allergo-Vigilance avec la betterave rouge
- des tests cutanés positifs pour la betterave sont parfois rapportés chez des patients allergiques à l’épinard ou aux bettes , mais sans notion de sensibilisation au latex
- un cas d’allergie à la betterave chez un enfant de 10 ans polyopéré a été décrit
- les bettes ont fait l’objet de quelques observations d’allergie à l’ingestion ou à l’inhalation d’aérosols à l’épluchage ou à la cuisson . Ces réactions respiratoires ne s’accompagnaient pas d’allergie à l’ingestion des aliments cuits, d’une façon générale.
- un lien entre bettes et certains pollens est difficile à établir, les patients montrant une réactivité pour ces légumes étant parfois polliniques pour des Amaranthacées (chénopode, soude), parfois pour des pariétaires et/ou le platane (ce qui pourrait faire penser à des LTP) .
- un lien entre bettes et certains pollens est difficile à établir, les patients montrant une réactivité pour ces légumes étant parfois polliniques pour des Amaranthacées (chénopode, soude), parfois pour des pariétaires et/ou le platane (ce qui pourrait faire penser à des LTP)
L’épinard
Il a été décrit quelques cas d’allergie à l’épinard, y compris des asthmes professionnels . Mais les allergies alimentaires n’ont pas été contrôlées par TPO (ex. ).
Les pricks natifs sont sujets à caution car les épinards sont riches en histamine .
Les tests in vitro pour l’épinard sont à risque d’interférence par les IgE anti-CCD .
Une association avec le latex a été suggérée dans quelques cas, au moins en réactivité cutanée mais non prouvée par méthode d’inhibition.
L’épinard est peu souvent noté dans le syndrôme latex-aliments (1 cas/28 ). Hormis le cas d’un patient allemand et les cas de Le Sellin , une pollinose est rarement citée.
On a caractérisé 2 allergènes dans l’épinard : une profiline et une rubisCO.
La rubisCO est une enzyme retrouvée dans les feuilles des végétaux. Elle a longtemps été considérée comme l’exemple-même de protéine non allergisante . Pourtant elle avait été trouvée plus sensibilisante que l’arachide chez la souris . Et dernièrement la rubisCO a été montrée IgE-réactive dans le persil et la ciboulette .
Herrera a suggéré la présence d’un allergène homologue dans l’épinard (et la carde) et le champignon agaric. Des cyclophilines sont connues allergisantes dans des moisissures et un autre champignon (Psylocybe), et l’épinard contient aussi une cyclophiline.
Cependant les masses de ces cyclophilines (env 20 kDa) ne correspondent pas à celles trouvées en blot avec l’épinard (> 30 kDa).
Le manioc
La racine de manioc (Manihot esculenta) procure une source alimentaire importante dans les régions tropicales. C’est une Euphorbiacée.
Bien que peu riche en protéines , le manioc est parfois responsable de réactions allergiques alimentaires.
Elles restent exceptionnelles et ont été notées dans les pays où le manioc est de consommation courante (Brésil, Mozambique, Colombie) .
On ne connaît pas d’allergène particulier dans le manioc, mais un lien avec le latex d’hévéa (autre Euphorbiacée) est évoqué, notamment dans un cas avec réaction anaphylactique .
Une protéine homologue d’Hev b 5 (latex) a été identifiée dans le manioc mais son homologie avec Hev b 5 reste faible (42%) et, en blot, elle n’était pas reconnue par des patients positifs pour Hev b 5 .
Yman trouve 8 CAP manioc positifs parmi 30 sujets avec latex positif in vitro. De même pour le pollen de mercuriale (14 cas/30) ou de Poinsettia (19 cas/30). Mais Palosuo ne trouve pas de sujet positif pour le manioc parmi des patients positifs pour la mercuriale ou le ricin.
Un "syndrome euphorbiacées" est donc peu probable.
Plus intéressante est la parenté entre les cystéine protéases du latex et du manioc (90 % d’identité). Ces protéines n’ont pas été identifiées comme des allergènes jusqu’à présent mais pourraient être le rapport de l’association latex- manioc (cf Ficus et aliments).
Dans une autre observation le lien entre latex et manioc était évoqué, même si dans ce cas la réaction de la patiente était respiratoire (épluchage) .
L’allergie au manioc a été décrite avec un produit cru ou cuit. Le tapioca est tiré du manioc. Sa consommation est très limitée et cela pourrait expliquer l’absence apparente de cas d’allergie au manioc en Europe.
[1] - Moneret-Vautrin DA, Boulègue M, Leduc V, Morisset M, Denery-Papini S. Un cas exemplaire d'allergie à la farine de blé. Alim'Inter 2004;9:298-299 ↩
[2] - Astier C, Moneret-Vautrin DA, Puillandre E, Bihain BE. First case report of anaphylaxis to quinoa, a novel food in France. Allergy 2009;64:815-821 ↩
[3] - Fowler MR, Gartland J, Norton W, Slater A, Elliott MC, Scott NW. RS2: a sugar beet gene related to the latex allergen Hev b 5 family. J Exp Bot 2000;51:2125-2126
A novel gene (RS2) has been isolated from a Beta vulgaris (cv. Regina) cDNA library. The expression of this gene was enhanced in the mature storage organ as compared to leaf tissue. The protein encoded by this gene was found to be alanine- and glutamic acid-rich and it resembles members of the latex allergen Hev b 5 family.
↩[4] - Drouet M, Le Sellin J, Gay G, el Founini M, Sabbah A. Allergie aux chénopodiacées (betterave, épinard) associée à l'allergie au latex. Allerg Immunol (Paris) 1994;26:113-114 ↩
[5] - Herrera I, Moneo I, Caballero ML, de Paz S, Perez Pimiento A, Rebollo S. Food allergy to spinach and mushroom. Allergy 2002;57:261-262 ↩
[6] - de la Hoz B, Fernandez-Rivas M, Quirce S, Cuevas M, Fraj J, Davila I, et al. Swiss chard hypersensitivity: clinical and immunologic study. Ann Allergy 1991;67:487-492
Allergy to vegetables and fruits seems to be more prevalent in atopics, especially in birch pollen-sensitized individuals. We report a case of a grass pollen-sensitized woman, in whom the inhalation of vapor from boiling Swiss chard precipitated rhinoconjunctivitis and asthma. Type I hypersensitivity to Swiss chard was demonstrated by means of immediate skin test reactivity, specific IgE determination by RAST, basophil degranulation, histamine release test, and an immediate bronchial provocation test response to Swiss chard extract. The controls did not react to any of these tests. RAST inhibition assays suggest the presence of some cross-reactivity among Swiss chard and grass pollen antigens, as well as cross-reactivity between vegetables and weed pollens of the chenopod family.
↩[7] - Minciullo PL, Mistrello G, Patafi M, Zanoni D, Gangemi S. Cross-reactivity between Parietaria pollen and beet. Allergol Immunopathol (Madr) 2007;35:74-75
Allergy to beet is very rare. Until now, only a few reports about asthma induced by inhaling the vapor of cooked beet have been published. We describe two patients with allergic rhinitis and positive skin prick tests to Parietaria and beet only. To investigate possible cross-reactivity between Parietaria pollen and beet, we performed laboratory assays that showed beet-specific IgE in the sera of both patients and possible cross-reactivity between Parietaria and beet in one patient.
↩[8] - de la Hoz B, Fernandez-Rivas M, Quirce S, Cuevas M, Fraj J, Davila I, et al. Swiss chard hypersensitivity: clinical and immunologic study. Ann Allergy 1991;67:487-492
Allergy to vegetables and fruits seems to be more prevalent in atopics, especially in birch pollen-sensitized individuals. We report a case of a grass pollen-sensitized woman, in whom the inhalation of vapor from boiling Swiss chard precipitated rhinoconjunctivitis and asthma. Type I hypersensitivity to Swiss chard was demonstrated by means of immediate skin test reactivity, specific IgE determination by RAST, basophil degranulation, histamine release test, and an immediate bronchial provocation test response to Swiss chard extract. The controls did not react to any of these tests. RAST inhibition assays suggest the presence of some cross-reactivity among Swiss chard and grass pollen antigens, as well as cross-reactivity between vegetables and weed pollens of the chenopod family.
↩[9] - García González MC, de la Hoz Caballer B, Cerecedo I, Carnés J, Fernández-Caldas E. Collection and identification of aerosolised proteins during the boiling process of vegetables and legumes. EAACI 23th Congress, Amsterdam, 12-16 June, 2004, Poster n°964
Background: Although most food allergic reactions are caused by ingestion, IgE mediated respiratory reactions caused by the inhalation of vapours from boiling vegetables and legumes have been described. In these cases, IgE-mediated mechanisms have been suggested, but the responsible allergens have not been fully characterised. The aims of this study were to develop a method to collect allergens from vegetable vapours and to investigate if these proteins are capable of binding specific IgE.
Material and Methods: Three types of extracts (A, B and C) were prepared with potato, carrot, Swiss chard and green beans. Extracts A (raw), extracted in PBS 0.01 M (1:2 w/v); Extracts B (boiled), cooked in PBS 0.01 M (1:2 w/v) for 30 minutes; and Extract C (lyophilised vapours), collected during the boiling process. The vapours were passed through a refrigeration column and the drops collected and freeze-dried. Raw and boiled extracts were extracted for 4 hours, dialyzed against bidistilled water in a 3.5 kDa cut-off dialysis membrane, frozen and freeze-dried. Antigenic profile of the extracts was evaluated by SDS-PAGE and analysed by scanning densitometry.
Results: Several bands were visualised in the raw extracts in the molecular weight range of 9 to 90 KDa in the 4 analysed raw extracts. The protein profile of the boiled extracts showed low molecular weights bands, which could correspond to denatured proteins from the raw extracts. The total yield of vapour proteins obtained in each extract was 0,64% in potato, 0,48% in carrot, 0,4% in Swiss chard and 0,352% in green bean. Vapours extracts (Extracts C) showed several prominent bands; 1 band in potatoes (35 kDa), 2 bands in carrot vapours (60 and a 66 kDa), 2 bands in the Swiss chard vapours (62 and 71 kDa) and 1 band (38 kDa) in green bean vapours. Almost all these molecules had a corresponding band in their respective raw extracts. Faint IgE binding was observed to green bean vapours.
Conclusions: We have developed a reproducible method to collect vapours during the boiling process of foods. The results suggest that proteins are present in vapour drops aerosolised during the boiling process. More studies are necessary to elucidate if these proteins are capable of inducing respiratory symptoms and to what extent these proteins are denatured and capable of binding specific IgE.
↩[10] - Daroca P, Crespo JF, Reano M, James JM, Lopez-Rubio A, Rodriguez J. Asthma and rhinitis induced by exposure to raw green beans and chards. Ann Allergy Asthma Immunol 2000;85:215-218
Abstract BACKGROUND: Although the vast majority of IgE-mediated allergic reactions to foods occurs through ingestion, a few cases of unexpected allergic reactions to foods may occur through the exposure to airborne food allergen particles.
METHODS: Case reports. Skin prick tests and serum-specific IgE (CAP-FEIA) were used to identify specific IgE antibodies. Bronchial provocation tests were performed to determine the clinical relevance of inhaled exposure to raw and cooked green beans and raw chards. After demonstrating specific reactivity to them, SDS- PAGE and immunoblotting of raw and cooked green beans were carried out to identify relevant antigens.
RESULTS: Three women developed bronchial asthma and rhinitis after exposure to raw green beans, and one of them also when exposed to raw chards. All women tolerated ingestion of green beans. Patients reported multiple episodes while handling these vegetables for cooking activities. Allergy to green beans and chards was demonstrated by skin testing and serum-specific Ig E. Bronchial challenge test with these allergens showed positive responses to raw, but not cooked, green beans and chards. Oral food challenges with green beans (raw and cooked) and chards were negative in all patients. In order to further characterize the allergenic components of these extracts, SDS-PAGE and electroblotting studies were also performed. Immunoblots of raw and cooked green beans extract showed two IgE- binding bands with apparent molecular weights of 41.1 and 70.6 kD. Interestingly, a 47-kD IgE-binding protein was detected only in raw green bean extracts.
CONCLUSIONS: We report three patients who developed asthma and rhinitis caused by exposure to raw, but not to cooked, green beans and chards in a non-occupational environment. Only minor differences of IgE reactivity between nitrocellulose-blotted raw and boiled green bean extract were found
↩[11] - González-Mancebo E, Alfaya T, Pulido Z, León F, Cuevas M, de la Hoz B. Swiss chard-induced asthma. Allergy 2000;55:511-512 ↩
[12] - Minciullo PL, Patafi M, Marotta G, Tigano V, Barresi L, Ferlazzo B, et al. Platanus acerifolia co-sensitivity in patients with parietaria judaica allergy and oral allergic syndrome. Allergy Clin Immunol Int 2005;17(Suppl. 1):250
Plane tree pollen allergy is a clinical disorder affecting particularly populations of the United States and Western Europe, but little is known about its relevant allergens. Pla a 1 and Pla a 2 are known as major allergens of Platanus acerifolia. Recently, a new allergen, called Pla a 3 has been characterized as major allergen in plane pollen allergic patients with concomitant allergy to vegetables and/or fruits in the Mediterranean area. It is a lipid transfer protein (LTP) that cross-reacts with food LTPs, in particular with lettuce, cherry and hazelnut LTP. Other previous studies described an association between the pollen of the Platanus tree and hazelnut, peach, apple, banana, peanut, celery, maize and chickpea. This association could be explained by the in vitro IgE crossreactivity detected. No data are present about a possible cross-reactivity between plane tree pollen and other plant or thee pollens. During the period between January 2004 and November 2004, 14 patients, referred to our Operative Unit for seasonal rhinitis and/or asthma symptoms, showed positivity to skin prick test to plane tree. All patients showed co-sensitivity to other pollens and in particular 13 out of 14 patients presented skin positivity to Parietaria judaica, the most important pollen in our area. Other important co-sensitivities were with Olea europea (10 patients) and grass pollen (7 patients). No monosensitivity to platanus was found. Therefore, platanus sensitivity in our area seems no to be so important and might be related to parietaria pollen.
Moreover, 5 out of 14 patients with platanus sensitivity, referred an oral allergic syndrome (OAS) and showed skin positivity for vegetables and/or fruits. All of 5 patients were sensitive to peach, 4 to apple, 4 to hazelnut, 4 to almond, 4 to beet, 3 to peanut and 3 to walnut. Since in the Mediterranean area OAS occurs independently of an associated birch pollinosis and since platanus pollinosis in our area seems no to play an important role, it may be hypothesised that the skin positivity to platanus is related to fruit LTP in patients with OAS. The role of parietaria allergens in cross-reactivity with platanus and fruit LTP should be investigate.
↩[13] - Schuller A, Morisset M, Maadi F, Kolopp Sarda MN, Fremont S, Parisot L, et al. Occupational asthma due to allergy to spinach powder in a pasta factory. Allergy 2005;60:408-409 ↩
[14] - Sanchez I, Rodriguez F, Garcia-Abujeta JL, Fernandez L, Quiñones D, Martin-Gil D. Oral allergy syndrome induced by spinach. Allergy 1997;53:1245-1246 ↩
[15] - Sanchez I, Rodriguez F, Garcia-Abujeta JL, Fernandez L, Quiñones D, Martin-Gil D. Oral allergy syndrome induced by spinach. Allergy 1997;53:1245-1246 ↩
[16] - Aalberse RC, Koshte V, Clemens JG. Immunoglobulin E antibodies that crossreact with vegetable foods, pollen, and Hymenoptera venom. J Allergy Clin Immunol 1981;68:356-364
IgE in some human sera reacted with an antigen present in a large number of unrelated foods: potato, spinach, wheat, buckwheat, peanut, honey and others. The antigen, which was periodate-sensitive and heat-stable, was also found in pollen. Even more surprisingly, these antibodies often reacted in vitro with bee and vespid venom and were sometimes apparently induced by Hymenoptera stings
↩[18] - Gaspar A, Braga C, Murta R, Morais-Almeida M, Rosado-Pinto J. Anaphylactic Reaction to Manioc: Cross-reactivity with Latex ? AAAAI 59th Annual Meeting, Denver, 7-12 March, 2003, Poster n°115
Manioc (Manihot esculenta) is a highly important food in South America and Africa. The authors present a case of a 51-year-old woman, born in Mozambique, with personal history of bronchial asthma and multiple pelvic-abdominal surgeries (last one performed 9 years ago), who, since the last two years, experienced several episodes of anaphylactic reactions immediately after eating foods cross-reacting with latex (chestnut, mango, peach, kiwi, passion fruit, papaya, fig, melon, tomato and spinach), as well as after eating raw and cooked manioc. Previously, she ate the referred foods, namely manioc, with no adverse reaction, and denied clinical symptoms upon latex exposure. The patient was referred to our Immunoallergy Department. Skin prick tests to common aeroallergens were negative. Prick tests with five commercial latex extracts were strongly positive. Prick tests with commercial food extracts were positive to chestnut, mango and potato. Prick tests with fresh foods were positive to peach, kiwi, passion fruit, papaya, fig, melon, tomato, spinach and manioc. The challenge test with latex glove was strongly positive (anaphylactic reaction). A SDS-PAGE was performed with an extract of manioc. The immunoblotting strips demonstrated the existence of tree bands of around 35, 42 and 50 kDa to manioc extract. The recognition of these bands was totally inhibited by latex extract (AlaBLOT® inhibition, DPC-Los Angeles). In conclusion, this case report represents the first description of an allergic reaction to manioc. Cross-reactivity between manioc and latex was proved by inhibition analysis, and manioc should be added to the list of foods cross-reacting with latex.
↩[19] - Kaatz M, Hipler CH, Bauer HI, Wigger-Alberti W, Elsner P. A case of cross allergy between latex and spinach. 8th International Symposium on Problems of Food Allergy, Venice 2001, March 11-13
Allergies to latex proteins are very frequently observed in health workers. Their prevalence is estimated to be 10% of personnel in operating theatres and intensive care units. Cross allergy between avocado, banana and kiwi on the one hand with latex protein on the other is well established. However cross allergy between spinach and latex has been described only twice up to date. The following case report describes a 61 year old patient, who developed severe pruritus associated with agitation/restlessness/anxiety after ingestion of spinach. After treatment with intravenous Dimetidine and Prednisolone symptoms were rapidly resolved. Specific symptoms in relation to latex were not described. Allergy testing was performed to identify the suspected allergens. Prick tests were performed using histamine as control positive results were obtained with latex, spinach, peach, apricot, birch, hazel, alder and grass pollen. Banana had negative test results. Specific IgE was 3.32 kU/l for SX 1 (CAP class 2), the test result for latex (k82) was CAP class 3, for r Bet v (t215) CAP class 2. Cellular antigen stimulation test (CAST) performed with extracts of latex and spinach revealed positive test results for both: with latex 370 pg/mL sLT and with spinach 2602 pg /mL sLT. Western blot testing of latex, kiwi, banana, spinach and mango could also reveal bands specific for latex (14, 19, 23, 27, 44, 67 kD). The above laboratory investigations were able to confirm the clinical reaction to spinach in our patient, we were also able to confirm allergy to spinach by allergy testing (prick test). At the same time we diagnose latex allergy in our patient (prick test, specific IgE, CAST, Western blot). In addition to the two cases mentioned in medical literature we present a third case of cross allergy between latex protein and spinach. We were however unable to identify the allergen responsible in case of spinach. It has been speculated that latex and spinach own corresponding epitopes leading to cross allergy.
↩[20] - Maillard H, Lemerle E, Garot D, Leclech C, Machet L. [Crossed spinach-latex allergy revealed by exercise-induced anaphylaxis]. Allerg Immunol (Paris) 1999;31:156-157
Diagnosis of exercise-induced anaphylaxis is based on conjunction between a specific factor: a specific or nonspecific food allergy and exercise. The authors report observation of a patient who presented with exercise-induced anaphylaxis associated with food allergy to spinach, but also with a cross reaction with latex
↩[21] - Branco Ferreira M, Pedro E, Meneses Santos J, Pereira dos Santos MC, Palma Carlos ML, Bartolome B, et al. Latex and chickpea (Cicer arietinum) allergy: first description of a new association. Eur Ann Allergy Clin Immunol 2004;36:366-371
In this paper we describe the existence of cross-reactivity between allergens from latex and chickpea, a food from the Leguminosae family, which is common in the Mediterranean diet. We present the case report of a spina bifida boy with a clinical relevant food allergy to chickpea (oral syndrome + dysphonia), developing after the appearance of latex allergy symptoms (lip angioedema + intraoperative anaphylaxis). Specific IgE to latex and chickpea was demonstrated by skin prick tests, measurement of patient's serum specific IgE and IgE-immunoblotting. Cross-reactivity was studied by means of EAST-inhibition and western blotting-inhibition. A strong inhibition was observed in several IgE-binding bands when latex extract was used in solid phase and patient serum was preincubated with chickpea extract (chickpea extract as inhibitor phase). As far as we know, this is the first report of cross-reactivity between latex and chickpea, a food which should therefore be added to the extensive list of latex cross-reactive foods.
↩[22] - Gaspar A, Raulf-Heimsoth M, Pires G, Rihs HP, Yeang HY, Matos V, et al. Latex allergen sensitization patterns in different risk groups and latex-fruit syndrome patients from Portugal. EAACI 23th Congress, Amsterdam, 12-16 June, 2004, Poster n°1188
Background: Latex allergy has been recognized as a clinically important health problem, mainly in some risk groups: spina bifida (SB), other congenital malformations submitted to multiple surgeries (MS) and health care workers (HCW).
Purpose: To study IgE-binding reactivity to latex allergens, by using recombinant and natural allergens, in latex-allergic patients from different risk groups including patients with latex-fruit syndrome (LFS).
Material and Methods: We selected sera of 51 latex-allergic patients within different risk groups: 20 with SB, 10 MS and 21 HCW; all these patients had positive skin prick tests with commercial latex extract (ALK-Abelló) and serum latex-specific IgE determined by UniCAP®(Pharmacia Diagnostics). Sixteen out of the 51 patients had LFS. A panel of single recombinant latex allergens was coupled to ImmunoCAPs (CAP system®) and the isolated natural allergen nHev b 2 was coupled on paper disks (EAST testing). This panel comprised rHev b 1, nHev b 2, rHev b 3, rHev b 5, rHev b 6.01, rHev b 7, rHev b 8, rHev b 9, rHev b 10 and rHev b 11. The recombinant allergens were produced as fusion protein with maltose-binding protein (MBP) in E. coli. MBP coupled on ImmunoCAPs served as control. Specific IgE values of >0.35kU/l were considered positive. Major allergen is defined if produces a positive IgE response in more than 50% of the tested group.
Results: Recombinant Hev b 1 specific IgE antibodies were detected in 70% sera from SB, 30% from MS, 5% from HCW, and in 13% sera from LFS patients. For nHev b 2: SB-69%, MS-71%, HCW-71% and LFS-75%. For rHev b 3: SB-50%, MS-20%, HCW-10% and LFS-13%. For rHev b 5: SB-55%, MS-40%, HCW-62% and LFS-75%. For rHev b 6.01: SB-45%, MS-30%, HCW-76% and LFS-81%. For rHev b 7: SB-33%, MS-0%, HCW-16% and LFS-27%. For rHev b 8: SB-10%, MS-0%, HCW-5% and LFS-6%. For rHev b 9 and rHev b 10: SB-0%, MS-0%, HCW-5% and LFS-7%. For rHev b 11: SB-7%, MS-0%, HCW-5% and LFS-7%.
Conclusions: The different routes of exposure influence the IgE antibody pattern. The major latex allergens identified in SB were Hev b 1, Hev b 2, Hev b 3 and Hev b 5, being Hev b 1 the most important one. The major allergen identified in MS was Hev b 2. For occupational exposure route, the major latex allergens identified in HCW were Hev b 2, Hev b 5 and Hev b 6.01, being prohevein the most important one. Regarding cross-reactivity with foods, the major allergens identified in LFS were Hev b 2, Hev b 5 and Hev b 6.01.
↩[23] - Kaatz M, Hipler CH, Bauer HI, Wigger-Alberti W, Elsner P. A case of cross allergy between latex and spinach. 8th International Symposium on Problems of Food Allergy, Venice 2001, March 11-13
Allergies to latex proteins are very frequently observed in health workers. Their prevalence is estimated to be 10% of personnel in operating theatres and intensive care units. Cross allergy between avocado, banana and kiwi on the one hand with latex protein on the other is well established. However cross allergy between spinach and latex has been described only twice up to date. The following case report describes a 61 year old patient, who developed severe pruritus associated with agitation/restlessness/anxiety after ingestion of spinach. After treatment with intravenous Dimetidine and Prednisolone symptoms were rapidly resolved. Specific symptoms in relation to latex were not described. Allergy testing was performed to identify the suspected allergens. Prick tests were performed using histamine as control positive results were obtained with latex, spinach, peach, apricot, birch, hazel, alder and grass pollen. Banana had negative test results. Specific IgE was 3.32 kU/l for SX 1 (CAP class 2), the test result for latex (k82) was CAP class 3, for r Bet v (t215) CAP class 2. Cellular antigen stimulation test (CAST) performed with extracts of latex and spinach revealed positive test results for both: with latex 370 pg/mL sLT and with spinach 2602 pg /mL sLT. Western blot testing of latex, kiwi, banana, spinach and mango could also reveal bands specific for latex (14, 19, 23, 27, 44, 67 kD). The above laboratory investigations were able to confirm the clinical reaction to spinach in our patient, we were also able to confirm allergy to spinach by allergy testing (prick test). At the same time we diagnose latex allergy in our patient (prick test, specific IgE, CAST, Western blot). In addition to the two cases mentioned in medical literature we present a third case of cross allergy between latex protein and spinach. We were however unable to identify the allergen responsible in case of spinach. It has been speculated that latex and spinach own corresponding epitopes leading to cross allergy.
↩[25] - Astwood JD, Leach JN, Fuchs RL. Stability of food allergens to digestion in vitro. Nat Biotechnol 1996;14:1269-1273
One of the concerns regarding the development of genetically modified foods is the introduction of allergenic molecules, predominantly proteins. Prospective testing for allergenic proteins from sources with no prior history of causing allergy is hampered by the absence of suitable techniques and models. Stability to digestion was tested as a candidate physicochemical property for use in distinguishing allergenic proteins from non-allergenic proteins. A simple model of gastric digestion was tested using some major food allergens (peanut Ara h2 and lectin, soybean [beta]-conglycinin subunits, SKTI and Gly m BD 30K, mustard Bra J IE, milk casein and [beta]-lactoglobulin, bovine serum albumin, and several egg proteins). Soybean [beta]-conglycinin was stable for 60 min; in comparison, a non-allergenic protein (spinach RUBISCO) was digested within 15 s. Data support the hypothesis that food allergens must be sufficiently stable to reach the intestinal mucosa where absorption and sensitization can occur. It is concluded that stability to digestion is an important parameter which distinguishes food allergens from non-allergens
↩[26] - Birmingham N, Thanesvorakul S, Gangur V. Relative immunogenicity of commonly allergenic foods versus rarely allergenic and nonallergenic foods in mice. J Food Prot 2002;65:1988-1991
Food allergies affect 6 to 8% of children and 2% of adults in the United States. For reasons that are not clear, eight types of food account for a vast majority (approximately 90%) of food-induced hypersensitivity reactions. In this study, C57Bl/6 mice were used to test the hypothesis that commonly allergenic foods are intrinsically more immunogenic than rarely allergenic or nonallergenic foods in allergy-susceptible hosts. Groups of mice (n = 4 to 5) were injected intraperitoneally with the protein extracts (plus alum as an adjuvant) from chicken eggs, peanuts, almonds, filberts-hazelnuts, walnuts, soybeans, and wheat (commonly allergenic foods) and coffee, sweet potatoes, carrots, white potatoes, cherries, lettuce, and spinach (rarely allergenic and nonallergenic foods). Primary and secondary immune responses (as measured by specific IgG1 antibody serum levels) were measured by an enzyme-linked immunosorbent assay. Proteins from peanuts, almonds, filberts, sweet potatoes, cherries, and spinach elicited robust primary and/or secondary immune responses. Proteins from eggs, walnuts, and lettuce elicited poor primary responses but significant secondary responses. In contrast, wheat, soybeans, coffee, carrots, and white potatoes elicited barely detectable to poor primary and secondary immune responses. The order of the immunogenicity levels of these foods in mice is as follows: almonds = filberts > spinach (Rubisco) > peanuts > or = sweet potatoes > cherries > lettuce > walnuts > chicken eggs > carrots > or = white potatoes > wheat = coffee = soybeans. In summary, these data demonstrate for the first time that: (i) foods vary widely with regard to their relative immunogenicity in allergy-susceptible hosts and (ii) intrinsic immunogenicity in mice does not distinguish commonly allergenic foods from rarely allergenic or nonallergenic foods.
↩[27] - de Lacoste-Delaval A, Guérin L, Leduc V. Allergie alimentaire à la salade. Rev Fr Allergol Immunol Clin 2006;46:374 ↩
[28] - Herrera I, Moneo I, Caballero ML, de Paz S, Perez Pimiento A, Rebollo S. Food allergy to spinach and mushroom. Allergy 2002;57:261-262 ↩
[29] - Herrera I, Ferrer B, Rodriguez-Sanchez JL, Juarez C. Crossreactivity between allergens: new data. 16th European Congress of Immunology, Paris, September 6-9, 2006, poster n° 1602
In previous studies we demonstrated the existence of IgE antibodies with crossreactivity between sources without taxonomical relationship, fungi imperfecti moulds and two frequently consumed foods, mushroom and spinach. To study the allergens responsible for this crossreactivity, spinach and mushroom extracts were analysed by immunoblott assays with sera from patients sensitized to Alternaria alternata and Cladosporium herbarum moulds. Inhibition assays were performed to study the existence of a relationship between proteins present in the two different extracts.
Results obtained showed that moulds allergic patients had a strong recognition of a 30 kD protein present in both extracts, spinach and mushroom. Inhibition assays confirmed a relationship between these food proteins and Cladosporium herbarum.
↩[30] - Shewry PR. Tuber storage proteins. Ann Bot (Lond) 2003;91:755-769
A wide range of plants are grown for their edible tubers, but five species together account for almost 90 % of the total world production. These are potato (Solanum tuberosum), cassava (Manihot esculenta), sweet potato (Ipomoea batatus), yams (Dioscorea spp.) and taro (Colocasia, Cyrtosperma and Xanthosoma spp.). All of these, except cassava, contain groups of storage proteins, but these differ in the biological properties and evolutionary relationships. Thus, patatin from potato exhibits activity as an acylhydrolase and esterase, sporamin from sweet potato is an inhibitor of trypsin, and dioscorin from yam is a carbonic anhydrase. Both sporamin and dioscorin also exhibit antioxidant and radical scavenging activity. Taro differs from the other three crops in that it contains two major types of storage protein: a trypsin inhibitor related to sporamin and a mannose-binding lectin. These characteristics indicate that tuber storage proteins have evolved independently in different species, which contrasts with the highly conserved families of storage proteins present in seeds. Furthermore, all exhibit biological activities which could contribute to resistance to pests, pathogens or abiotic stresses, indicating that they may have dual roles in the tubers.
↩[31] - Gaspar A, Neto-Braga C, Pires G, Murta R, Morais-Almeida M, Rosado-Pinto J. Anaphylactic reaction to manioc: cross-reactivity to latex. Allergy 2003;58:683-684 ↩
[32] - Galvao CES, Iwai LK, Andrade MEB, Kalil J, Morato Castro FF. Latex allergy and cross-reactivity to manioc: Report of 2 cases. AAAAI 60th Annual Meeting, San Francisco, 19-23 March 2004, Poster n°144
Rationale Allergy to natural latex is frequently associated with hypersensitivity to fruits and recently, a case of cross-reactivity to manioc was reported.
Objective : The authors present the cases of two female patients sensitized to latex who have developed anaphylactic reaction with urticaria and bronchospasm immediately after eating boiled manioc.
Method : Skin prick test to common aeroallergens, latex, manioc and other foods were performed. Serum latex specific IgE levels were measured with CAP-RAST method and RAST inhibition tests were carried out with manioc and latex.
Result s : Skin prick tests to common aeroallergens were negative. Skin prick tests to commercial latex extract were positive in both patients as well as prick tests with raw and boiled manioc. They both had positive skin tests to fresh papaya and one of them to pineapple. Tests were negative to banana, kiwi and chestnut. They both presented elevated serum latex specific IgE. RAST inhibition assays revealed cross-reactivity between latex and manioc.
Conclusion : These two cases support the previously reported cross-reactivity between latex and manioc, definitely adding it to the list of foods cross-reacting with latex.
↩[33] - Caraballo L, Mercado D, Pantoja A, Mercado J. The allergenic properties of cassava (Manihot esculenta): a case of cassava allergy. AAAAI 57th Annual Meeting, New Orleans, 16-21 March, 2001, Poster n°606 ↩
[34] - Gaspar A, Neto-Braga C, Pires G, Murta R, Morais-Almeida M, Rosado-Pinto J. Anaphylactic reaction to manioc: cross-reactivity to latex. Allergy 2003;58:683-684 ↩
[35] - de Souza CR, Beezhold D, Carvalho LJ. Pt2L4 Protein, a Homologue to Hev b 5 from Rubber Tree, May Not Be Responsible for the Cross-Reactions to Cassava Show by People Allergic to Latex. Protein Pept Lett 2008;15:900-902
Pt2L4 is a protein from cassava homologue to Hevb5, a principal allergen from latex. Here we aimed to elucidate immunological relationships between these proteins. Our results revealed that epitopes found in Hev b 5 are not entirely conserved in Pt2L4 which is not recognized by IgE from patients allergic to Hev b 5.
↩[36] - Yman L, Lundberg M. Latex-related allergens of the plant family Euphorbiaceae. ICACI 2000, 15-20 Oct. 2000, Sydney, Australia, Abstract P-676 ↩
[37] - 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.
↩[38] - Ibero M, Castillo MJ, Pineda F. Allergy to Cassava: A New Allergenic Food With Cross-Reactivity to Latex. J Investig Allergol Clin Immunol 2007;17:409-412
Imprimer la bibliographiePatients who are allergic to latex (Hevea brasiliensis) may exhibit cross-hypersensitivity with foods. We present a case of anaphylaxis due to cassava in a patient suffering from pollinosis, latex allergy, and latex-fruit syndrome. We performed sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and immunoblotting with cassava, avocado, chestnut, banana, kiwi, and latex extracts in order to analyze the protein bands and their molecular weights, and identify immunoglobulin (Ig) E-binding bands. Immunoblot inhibition and enzyme-linked immunosorbent assay (ELISA) inhibition were performed with latex in order to assess cross-reactivity. Cassava exhibited numerous protein bands, 5 of which were IgE-binding (89.75, 46.28, 26.68, 21.38, and 19.49 kd). These cassava IgE-binding bands were 100% inhibited by preincubation of the patient's serum with latex extract. The ELISA inhibition between latex and cassava was 23%. Our results confirm cassava as another food with clinical cross-reactivity in patients suffering from latex allergy.
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