Soy: allergenic properties of proteins and IgE cross-reactions

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Abstract

Since the last century, European countries began to actively use soybean seeds as food additives or for food production with 100% milk and animal proteins replaced with soy.

In Russia, soy is a relatively new agricultural crop, which recently began to be used in food production. Meanwhile, some proteins of soybeans have pronounced allergenic properties. The World Health Organization classified eight soy proteins (Gly m 1–Gly m 8) as allergens capable of causing clinically significant immunoglobulin (Ig)E-mediated sensitization in patients with allergic diseases. Moreover, most of these allergens were included in the World Health Organization nomenclature over the past 15 years. Additionally, the presence of other soybean allergens that can bind to sIgE has scientific evidence. Moreover, some soy allergens have homology in amino acid sequence and three-dimensional similarity to proteins of other plants and animals. Therefore, questions of IgE-cross-reactivity are becoming relevant.

Thus, this review aimed to analyze and summarize scientific data on the chemical structure, properties, and allergenic activity of soy and soybean proteins (soybean seeds) and their cross-reactions with proteins of animal and plant origin.

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About the authors

Valentina B. Gervazieva

I. Mechnikov Research Institute of Vaccines and Sera

Email: vbger@mail.ru
ORCID iD: 0000-0001-5191-8709
SPIN-code: 9868-9164

MD, Dr. Sci. (Med.), Professor

Russian Federation, Moscow

Pavel V. Samoylikov

I. Mechnikov Research Institute of Vaccines and Sera

Author for correspondence.
Email: samoilikov@mail.ru
ORCID iD: 0000-0003-3580-3199
SPIN-code: 4294-2188
Scopus Author ID: 55931760300

MD, Cand. Sci. (Med.)

Russian Federation, Moscow

Evgeny M. Zaitsev

I. Mechnikov Research Institute of Vaccines and Sera

Email: pertussis@yandex.ru
ORCID iD: 0000-0002-4813-9074
SPIN-code: 5089-7661

MD, Dr. Sci. (Med.)

Russian Federation, Moscow

Anatoly S. Bykov

The First Sechenov Moscow State Medical University

Email: bykov_a_s@staff.sechenov.ru
ORCID iD: 0000-0002-8099-6201
SPIN-code: 3894-1190

MD, Dr. Sci. (Med.), Professor

Russian Federation, Moscow

References

  1. Jędrusek-Golińska A, Zielińska-Dawidziak M, Zielińska P, et al. Analysis of risk and consumers’ awareness regarding the gluten content in meat products on the example of frankfurter type sausages. Quality Assurance Safety Crops Foods. 2019;11(6):529–537. doi: 10.3920/QAS2018.1401
  2. Kleine-Tebbe J, Beyer K, Ebisawa M. EAACI molecular allergology user’s guide. Pediatr Allergy Immunol. 2016;27(Suppl 23):225–234. doi: 10.1111/pai.12563
  3. Radlović N, Leković Z, Radlović V, et al. Food allergy in children. Srp Arh Celok Lek. 2016;144(1-2):99–103. doi: 10.2298/sarh1602099r
  4. Wang HY, Li Y, Li JJ, et al. Serological investigation of IgG and IgE antibodies against food antigens in patients with inflammatory bowel disease. World J Clin Cases. 2019;7(16):2189–2203. doi: 10.12998/wjcc.v7.i16.2189
  5. Ramadan S, Marsh J, El-Sherbeny GA, et al. Purification of soybean cupins and comparison of IgE binding with peanut allergens in a population of allergic subjects. Food Chem Toxicol. 2021;147:111866. doi: 10.1016/j.fct.2020.111866
  6. Sampson HA, Mendelson L, Rosen JP. Fatal and near-fatal anaphylactic reactions to food in children and adolescents. N Engl J Med. 1992;327(6):380–384. doi: 10.1056/NEJM199208063270603
  7. Hao GD, Zheng YW, Wang ZX, et al. High correlation of specific IgE sensitization between birch pollen, soy and apple allergens indicates pollen-food allergy syndrome among birch pollen allergic patients in northern China. J Zhejiang Univ Sci B. 2016;17(5):399–404. doi: 10.1631/jzus.B1500279
  8. Radauer C, Nandy A, Ferreira F, et al. Update of the WHO/IUIS Allergen Nomenclature Database based on analysis of allergen sequences. Allergy. 2014;69(4):413–419. doi: 10.1111/all.12348
  9. Gonzalez R, Varela J, Carreira J, Polo F. Primary structure of the major inhalant allergen from soybean hulls, Gly m 1: soybean hydrophobic protein and soybean hull allergy. Lancet. 1995;346:48–49.
  10. Rodrigo MJ, Morell F, Helm RM, et al. Identification and partial characterization of the soybean-dust allergens involved in the Barcelona asthma epidemic. J Allergy Clin Immunol. 1990;85(4): 778–784. doi: 10.1016/0091-6749(90)90198-d
  11. Codina R, Lockey RF, Fernández CE, Rama R. Identification of the soybean hull allergens responsible for the Barcelona asthma outbreaks. Int Arch Allergy Immunol. 1999;119(1):69–71. doi: 10.1159/000024178
  12. Codina RM, Calderón E, Lockey RF, et al. Specific immunoglobulins to soybean hull allergens in soybean asthma. Chest. 1997;111(1): 75–80. doi: 10.1378/chest.111.1.75
  13. Rihs HP, Chen Z, Ruëff F, et al. IgE binding of the recombinant allergen soybean profiling (rGly m 3) is mediated by conformational epitopes. J Allergy Clin Immunol. 1999;104(6):1293–1301. doi: 10.1016/s0091-6749(99)70027-8
  14. 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(5):797–804. doi: 10.1067/mai.2002.128946
  15. Dunwell JM. Cupins: a new superfamily of functionally diverse proteins that include germins and plant storage proteins. Biotechnology Gen Engineering Rev. 1998;15(1):1–32. doi: 10.1080/02648725.1998.10647950
  16. Holzhauser T, Wackermann O, Ballmer-Weber BK, et al. Soybean (Glycine max) allergy in Europe: Gly m 5 (b-conglycinin) and Gly m 6 (glycinin) are potential diagnostic markers for severe allergic reactions to soy. J Allergy Clin Immunol. 2009;123(2):452–458. doi: 10.1016/j.jaci.2008.09.034
  17. Ito K, Sjölander S, Sato S, et al. IgE to Gly m 5 and Gly m 6 is associated with severe allergic reactions to soybean in Japanese children. J Allergy Clin Immunol. 2011;128(3):673–675. doi: 10.1016/j.jaci.2011.04.025
  18. Riascos JJ, Weissinger SM, Weissinger AK, et al. The seed biotinylated protein of soybean (Glycine max): a boiling-resistant new allergen (Gly m 7) with the capacity to induce IgE-Mediated Allergic Responses. J Agric Food Chem. 2016;64(19):3890–3900. doi: 10.1021/acs.jafc.5b05873
  19. Ebisawa M, Brostedt P, Sjölander S, et al. Gly m 2S albumin is a major allergen with a high diagnostic value in soybean-allergic children. J Allergy Clin Immunol. 2013;132(4):976–978. doi: 10.1016/j.jaci.2011.04.025
  20. Yumioka-Ito H, Misaki R, Yokoro M, et al. Cloning of a cDNA Encoding the Gly m Bd 28K Precursor and Its Vacuole Transport in Tobacco BY2 Suspension-Cultured Cells. J Nutr Sci Vitaminol. 2014;60(2):129–139. doi: 10.3177/jnsv.60.129
  21. Ogawa T, Bando N, Tsuji H, et al. Investigation of the IgE-binding proteins in soybeans by immunoblotting with the sera of the soybean-sensitive patients with atopic dermatitis. J Nutr Sci Vitaminol. 1991;37(6):555–565. doi: 10.3177/jnsv.37.555
  22. Xiang P, Baird LM, Jung R, et al. P39, a novel soybean protein allergen, belongs to a plant-specific protein family and is present in protein storage vacuoles. J Agric Food Chem. 2008;56(6):2266–2272. doi: 10.1021/jf073292x
  23. Gu X, Beardslee T, Zeece M, et al. Identification of IgE-binding proteins in soy lecithin. Int Arch Allergy Immunol. 2001;126(3): 218–225. doi: 10.1159/000049517
  24. Codina R, Ardusso L, Lockey RF, et al. Identification of the soybean hull allergens involved in sensitization to soybean dust in a rural population from Argentina and N-terminal sequence of a major 50 KD allergen. Clin Exp Allergy. 2002;32(7):1059–1063. doi: 10.1046/j.1365-2222.2002.01411.x
  25. Baur X, Pau M, Czuppon A, Fruhmann G. Characterization of soybean allergens causing sensitization of occupationally exposed bakers. Allergy. 1996;51(5):326–330. doi: 10.1111/j.1398-9995.1996.tb04617.x
  26. Batista R, Martins I, Jeno P, et al. A proteomic study to identify soya allergens ― the human response to transgenic versus non-transgenic soya samples. Int Arch Allergy Immunol. 2007;144(1): 29–38. doi: 10.1159/000102611
  27. Kleine-Tebbe J, Beyer K, Ebisawa M. Soy allergy. In: EAACI Molecular Allergologyuser’s Guide. European Academy of Allergy and Clinical Immunology; 2016. Р. 225–234.
  28. Radauer C, Bublin M, Wagner S, et al. Allergens are distributed into few protein families and possess a restricted number of biochemical functions. J Allergy Clin Immunol. 2008;121(4):847–852. doi: 10.1016/j.jaci.2008.01.025
  29. Valenta R, Duchene M, Ebner C, et al. Profilins constitute a novel family of functional plant pan-allergens. J Exp Med. 1992;175(2): 377–385. doi: 10.1084/jem.175.2.377
  30. Tatham AS, Shewry PR. Allergens to wheat and related cereals. Clin Exp Allergy. 2008;38(11):1712–1726. doi: 10.1111/j.1365-2222.2008.03101.x
  31. Alvarado MI, Jimeno L, De La Torre, et al. Profilin as a severe food allergen in allergic patients overexposed to grass pollen. Allergy. 2014;69(12):1610–1616. doi: 10.1111/all.12509
  32. Mari A. Multiple pollen sensitization: a molecular approach to the diagnosis. Int Arch Allergy Immunol. 2001;125(1):57–65. doi: 10.1159/000053797
  33. Pablos I, Wildner S, Asam C, et al. Pollen allergens for molecular diagnosis. Curr Allergy Asthma Rep. 2016;16(4):31. doi: 10.1007/s11882-016-0603-z
  34. Barre A, Sordet C, Culerrier R, et al. Vicilin allergens of peanut and tree nuts (walnut, hazelnut and cashew nut) share structurally related IgE-binding epitopes. Mol Immunol. 2008;45(5):1231–1240. doi: 10.1016/j.molimm.2007.09.014
  35. Kroghsbo S, Bogh KL, Rigby NM, et al. Sensitization with 7S globulins from peanut, hazelnut, soy or pea induces IgE with different biological activities which are modified by soy tolerance. Int Arch Allergy Immunol. 2011;155(3):212–224. doi: 10.1159/000321200
  36. López-Torrejón G, Salcedo G, Martín-Esteban M, et al. Len c 1, a major allergen and vicilin from lentil seeds: protein isolation and cDNA cloning. J Allergy Clin Immunol. 2003;112(6):1208–1215. doi: 10.1016/j.jaci.2003.08.035
  37. Beyer K, Bardina L, Grishina G, Sampson HA. Identification of sesame seed allergens by 2-dimensional proteomics and Edman sequencing: seed storage proteins as common food allergens. J Allergy Clin Immunol. 2002;110(1):154–159. doi: 10.1067/mai.2002.125487
  38. Candreva AM, Ferrer-Navarro M, Quiroga A, et al. Identification of cross-reactive B-cell epitopes between Bos d 9.0101 (Bos Taurus) and Gly m 5.0101 (Glycine max) by epitope mapping MALDI-TOF MS. Proteomics. 2017;17(15-16). doi: 10.1002/pmic.201700069
  39. Beardslee 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(4):299–307. doi: 10.1159/000053642
  40. Wang F, Robotham JM, Teuber SS, et al. Ana o 2, a major cashew (Anacardium occidentale L.) nut allergen of the legumin family. Int Arch Allergy Immunol. 2003;132(1):27–39. doi: 10.1159/000073262
  41. Wallowitz M, Peterson WR, Uratsu S, et al. Jug r 4, a legumin group food allergen from walnut (Juglans regia Cv. Chandler). J Agric Food Chem. 2006;54(21):8369–8375. doi: 10.1021/jf061329s
  42. Beyer K, Grishina G, Bardina L, Sampson HA. Identification of 2 new sesame seed allergens: Ses i 6 and Ses i 7. J Allergy Clin Immunol. 2007;119(6):1554–1556. doi: 10.1016/j.jaci.2007.03.041
  43. Beyer K, Grishina G, Bardina L, et al. Identification of an 11S globulin as a major hazelnut food allergen in hazelnut-induced systemic reactions. J Allergy Clin Immunol. 2002;110(3):517–523. doi: 10.1067/mai.2002.127434
  44. Barre A, Jacquet G, Sordet C, et al. Homology modelling and conformational analysis of IgE-binding epitopes of Ara h 3 and other legumin allergens with a cupin fold from tree nuts. Mol Immunol. 2007;44(12):3243–3255. doi: 10.1016/j.molimm.2007.01.023
  45. Gervaziyeva VB, Sveranovskaya VV. Alimentary allergy and hypersensivity to soya bean protein. Med Immunol. 2005;7(1):15–20. (In Russ). doi: 10.15789/1563-0625-2005-1-15-20
  46. Skypala IJ. Food-Induced anaphylaxis: role of hidden allergens and cofactors. Front Immunol. 2019;10:673. doi: 10.3389/fimmu.2019.00673
  47. Rahaman T, Vasiljevic T, Ramchandran L. Effect of processing on conformational changes of food proteins related to allergenicity. Trends Food Sci. Technol. 2016;49:24–34. doi: 10.1016/j.tifs.2016.01.001

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