Soy allergy in perspective

Current Opinion in Allergy and Clinical Immunology

Volumn 8, Issue 3, 2008, Pages 270-275

  Ballmer Weber, Barbara K ^a,b   Vieths, Stefan ^a  

^a UNIVERSITY HOSPITAL ZURICH   (Switzerland)

^b PAUL EHRLICH INSTITUT   (Germany)

Author keywords

Birch pollen related food allergy; Genetically modified soy; Mungbean allergy; Soy allergy; Threshold doses

Indexed keywords

IMMUNOGLOBULIN E; ALLERGEN; BET V 1 ALLERGEN, BETULA VERRUCOSA; GLY M 4 ALLERGEN, GLYCINE MAX; GLY M I PROTEIN, GLYCINE MAX; PLANT ANTIGEN; VEGETABLE PROTEIN;

BIRCH; CROSS REACTION; DIAGNOSTIC TEST; FOOD ALLERGY; HUMAN; LEGUME; NONHUMAN; NUT ALLERGY; PATHOGENESIS; PEANUT; POLLEN ALLERGY; PRIORITY JOURNAL; REVIEW; SOYBEAN; DESENSITIZATION; IMMUNOLOGY; MOLECULAR MIMICRY; PATHOPHYSIOLOGY; STRUCTURAL HOMOLOGY;

ALLERGENS; ANTIGENS, PLANT; DESENSITIZATION, IMMUNOLOGIC; FOOD HYPERSENSITIVITY; HUMANS; MOLECULAR MIMICRY; PLANT PROTEINS; SOYBEANS; STRUCTURAL HOMOLOGY, PROTEIN;

EID: 49249093172     PISSN: 15284050     EISSN: 14736322     Source Type: Journal    
DOI: 10.1097/ACI.0b013e3282ffb157     Document Type: Review

References (42)

1. Sampson HA, Ho DG. Relationship between food-specific IgE concentrations and the risk of positive food challenges in children and adolescents. J Allergy Clin Immunol 1997; 100:444-451.
2. Niggemann B, Sielaff B, Beyer K, et al. Outcome of double-blind, placebocontrolled food challenge tests in 107 children with atopic dermatitis. Clin Exp Allergy 1999; 29:91-96.
3. Sicherer SH, Morrow EH, Sampson HA. Dose-response in double-blind, placebo-controlled oral food challenges in children with atopic dermatitis. J Allergy Clin Immunol 2000; 105:582-586.
4. Besler M, Helm R, Ogawa T. Allergen data collection-update: soybean. ISFA 2000; 2 (Suppl 3):1-35.
5. Sicherer SH, Sampson HA, Burks AW. Peanut and soy allergy: a clinical and therapeutic dilemma. Allergy 2000; 55:515-521.
6. Moroz LA, Yang WH. Kunitz soybean trypsin inhibitor: a specific allergen in food anaphylaxis. N Engl J Med 1980; 302:1126-1128.
7. Burks AW, Cockrell G, Connaughton C, et al. Identification of peanut agglutinin and soybean trypsin inhibitor as minor legume allergens. Int Arch Allergy Immunol 1994; 105:143-149.
8. Gu X, Beardslee T, Zeece M, et al. Identification of IgE-binding proteins in soy lecithin. Int Arch Allergy Immunol 2001; 126:218-225.
9. Helm RM, Cockrell G, Herman E, et al. Cellular and molecular characterization of a major soybean allergen. Int Arch Allergy Immunol 1998; 117:29-37.
10. Helm RM, Cockrell G, Connaughton C, et al. Mutational analysis of the IgEbinding epitopes of P34/GlymBd 30k. J Allergy Clin Immunol 2000; 105:378- 384.
11. Ogawa T, Bando N, Tsuji H, et al. Investigation of the IgE-binding proteins in soybean by immunoblotting with the sera of the soybean-sensitive patients with atopic dermatitis. J Nutr Sci Vitaminol 1991; 37:555-565.
12. Ogawa T, Bando N, Tsuji H, et al. a-Subunit of b-conglycinin, an allergenic protein recognized by IgE antibodies of soybean sensitive patients with atopic dermatitis. Biosci Biotech Biochem 1995; 59:831-833.
13. Bearslee TA, Zeece MG, Sarath G, Markwell JP. Soybean glycinin G1 acidic chain shares IgE epitopes with peanut allergen Ara h 3. Int Arch Allergy Immunol 2000; 123:299-307.
14. Barnett D, Howden ME. Lectins and the radioallergosorbent test. J Allergy Clin Immunol 1987; 80:558-561.
15. Helm RM, Cockrell G, Connaughton C, et al. A soybean G2 glycinin allergen. Int Arch Allergy Immunol 2000; 123:205-212.
16. Batista R,Martins I, Nee' P, et al. A proteomic study to identify soya allergens - the human response to transgenic versus nontransgenic soya samples. Int Arch Allergy Immunol 2007; 144:29-38. This study was aimed at addressing changes of endogenous allergen expressions in soybean after genetic modification. Western blots of single samples from GMO and nonGMO soybeans did not show differences in IgE binding pattern. Furthermore, the authors identified by proteomic approach two new potential soy allergens: a maturation associated protein and a cysteine proteinase inhibitor.
17. Rozenfeld P, Docena GH, Anon MC, Fossati CA. Detection and identification of a soy protein component that cross-reacts with caseins from cow's milk. Clin Exp Immunol 2002; 130:49-58.
18. Lin J, Shewry PR, Archer DB, et al. The potential allergenicity of two 2S albumins from soybean (Glycine max L.): a protein microarray approach. Int Arch Allergy Immunol 2006; 141:91-102.
19. Mittag D, Vieths S, Vogel L, et al. Birch pollen-related allergy to soybean: clinical investigation and molecular characterization of allergens. J Allergy Clin Immunol 2004; 113:148-154.
20. Gonzalez R, Polo F, Zapatero L, et al. Purification and characterization of major inhalant allergens from soybean hulls.Clin Exp Allergy 1992; 22:748- 755.
21. Rihs H-P, Chen Z, Rueff F, et al. IgE binding of the recombinant allergen soybean profilin (rGly m 3) is mediated by conformational epitopes. J Allergy Clin Immunol 1999; 104:1293-1301.
22. Kleine-Tebbe J, Vogel L, Crowell DN, et al. Severe oral allergy syndrome and anaphylactic reactions caused by a Bet v 1- related PR-10 protein in soybean, SAM22. J Allergy Clin Immunol 2002; 110:797-804.
23. Anto JM, Sunyer J, Rodriguez-Roisin R, et al. Toxicoepidemiological Committee. Community outbreaks of asthma associated with inhalation of soybean dust. N Engl Med 1989; 320:1097-1102.
24. Gomez-Olles S, CruzMJ, Bodanovic J, et al. Assessment of soy aeroallergen levels in different work environments. Clin Exp Allergy 2007; 37:1863- 1872. Asthma epidemics have been induced by soy bean hull proteins, whereas soy flour dust proteins might elicit occupational allergy in food and feed industry. This study assessed soy hull and soy flour aeroallergen exposure in various work environments. The levels of low molecular weight in soy hull proteins were highest at sites of soybean unloading or precessing, whereas soy flour levels were particular high in the animal feed industry.
25. Ballmer-Weber BK, Holzhauser T, Scibilia J, et al. Clinical characteristics of soybean allergy in Europe: a double-blind, placebo-controlled food challenge study. J Allergy Clin Immunol 2007; 119:1489-1496. Thirty patients with a history of soy allergy were included and 23 patients underwent a titrated double-blind placebo-controlled food challenge. Cumulative threshold doses for allergic reactions ranged from 10 mg to 50 g for subjective symptoms and from 454mg to 50 g for objective symptoms. Threshold doses appeared thus to be more than one order of magnitude higher than in peanut allergy. When data were fitted by a normal distribution statistical model, it predicted that 1% of soy allergic patients would react subjectively and objectively with 0.21 and 37.2mg soy protein, respectively.
26. Vieths S, Scheurer S, Ballmer-Weber B. Current understanding of crossreactivity of food allergens and pollen. Ann N Y Acad Sci 2002; 964:47-68.
27. Crowell DN, John ME, Russell D, Amasino RM. Characterization of a stressinduced, developmentally regulated gene family from soybean. Plant Mol Biol 1992; 18:459-466.
28. Lidholm J, Ballmer-Weber BK, Mari A, Vieths S. Component-resolved diagnostics in food allergy. Curr Opin Allergy Clin Immunol 2006; 6:234-240.
29. Gubesch M, Theler B, Dutta M, et al. Allergenic potential of novel food: clinical and molecular investigation of exotic vegtables (water spinach, hyacinth bean and Ethiopian eggplant). Allergy 2007; 62:1243-1250. Foods not commonly consumed in the European Union must be proven safe before brought to market, including an assessment of allergenicity. This paper presents a strategy for allergenicity assessment of natural novel foods using three novel vegetables as example, that is, water spinach, hyacinth bean and Ethiopian eggplant. These natural novel vegetables contain proteins homologous to known allergens in endemic vegetable foods, i.e. Bet v 1 homologous proteins, profilins and lipid transfer proteins. Most of the included soy allergic patients were sensitized to the investigated vegetables, to which they never have been exposed before and in particular to hyacinth beans. Most of the included patients were birch pollen allergic and were sensitized to Gly m 4 making crossreaction between Bet v 1 homologous in legumes to be the most likely pathway to initiate crossreaction in that group of soybean allergic patients.
30. Friedman M, Brandon DL. Nutritional and health benefits of soy proteins. J Agric Food Chem 2001; 49:1069-1086.
31. Mittag D, Vieths S, Vogel L, et al. Birch pollen-related food allergy to legumes: identification and characterization of the Bet v 1 homologue in mungbean (Vigna radiata), Vig r 1. Clin Exp Allergy 2005; 35:1049-1055.
32. Mittag D, Akkerdaas J, Ballmer-Weber BK, et al. Ara h 8, a Bet v 1-homologous allergen from peanut, is a major allergen in patients with combined birch pollen and peanut allergy. J Allergy Clin Immunol 2004; 114:1410- 1417.
33. Taylor SL, Hefle SL, Bindslev-Jensen C, et al. Factors affecting the determination of threshold doses for allergenic foods: how much is too much? J Allergy Clin Immunol 2002; 109:24-30.
34. Anibarro B, Seoane FJ, Mugica MV. Involvement of hidden allergens in food allergic reactions. J Investig Allergol Clin Immunol 2007; 17:168-172. This retrospective study in a Spanish adult population reported that 22.4% of allergic reactions occurred by ingestion of the so-called hidden allergens. The most frequent hidden allergen in the investigated population was Anisakis simplex followed by legumes. All but one of the latter reactions occurred in soy allergic patients. Sources of hidden allergens were identified in boiled ham, sausages, cheese puffs, precooked dishes, desserts and gravy.
35. Magnolfi CF, Zani G, Lacave L, et al. Soy allergy in atopic children. Ann Allergy Asthma Immunol 1996; 77:197-201.
36. Zeiger RS, Sampson HA, Bock SA, et al. Soy allergy in infants and children with IgE-associated cow's milk allergy. J Pediatr 1999; 134: 614-622.
37. Wensing M, Penninks AH, Hefle SL, et al. The distribution of individual threshold doses eliciting allergic reactions in a population with peanut allergy. J Allergy Clin Immunol 2002; 110:915-920.
38. Hourihane JO'B, Kilburn SA, Nordlee JA, et al. An evaluation of the sensitivity of subjects with peanut allergy to very low doses of peanut protein: a randomized, double-blind, placebo-controlled food challenge study. J Allergy Clin Immunol 1997; 100:596-600.
39. James C. Executive summary of global status of commercialized Biotech/GM Crops: 2005. Ithaca, NY, USA: International Service for the Acquisition of Agri-biotech Applications; 2005. Briefs No. 34.
40. Harrison LA, Bailey MR, Naylor MW, et al. The expressed protein in glyphosate- tolerant soybean, 5-enolpyruvylshikimate-3-phosphate synthase from Agrobacterium sp. strain CP 4, is rapidly digested in vitro and is not toxic to acutely gavaged mice. J Nutr 1996; 126:728-740.
41. Hoff M, Dae-Yeul S, Gubesch M, et al. Serum testing of genetically modified soybeans with special emphasis on potential allergenicity of the heterologous protein CP4 EPSPS. Mol Nutr Food Res 2007; 51:946-955. The genetically modified soy roundup ready soy contains the biotech protein CP4 EPSPS. In that study different patient populations, that is, soy allergic adult subjects and children with atopic dermatitis and sensitization to soy but also different control groups were included. No increased allergenicity of CP4 EPSPS could be detected. IgE Western blot patterns of single samples from GMO and nonGMO soybeans were identical.
42. Batista R, Nunes B, CarmoM, et al. Lack of detactable allergenicity of transgenic maize and soya samples. J Allergy Clin Immunol 2005; 116:403-410.