nGly m 5, Soy

Further reading

Common Background: Soybean f14

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Code: f431
Latin name: Glycine max
Source material: nGly m 5 is purified from a soy extract
Common names: Vicilin, alpha Subunit of beta-Conglycinin

Allergen components

  • rGly m 4
  • nGly m 5
  • nGly m 6

Biological function

A vicilin-like protein.

Mw: 40-70 kDa

Other allergens isolated

Soya protein consists of 136 phytochemicals and at least 21 allergenic proteins that have been identified. , Seed proteins in Soybean comprise 2 major fractions that account for 70% to 80% of total protein composition: 11S and 7S globulins.

The following allergens have been characterised:

  • Gly m 1, a 7-8 kDa protein, also known as HPS or Soybean hydrophobic protein. ,
  • Gly m 2, an 8 kDa protein.7,
  • Gly m 3, a 12-15 kDa protein, a profilin.4
  • Gly m 4, a Bet v 1 homologue.7,
  • Gly m 5, a vicilin-like protein, also known as vicilin or alpha subunit of beta-conglycinin.1, 2, 7
  • Gly m 6, an 11S globulin (legumin-like protein), also known as legumin, and G1 subunit of glycinin, G2 subunit of glycinin, G3 subunit of glycinin, G4 subunit of glycinin, G5 subunit of glycinin.1, 7,
  • Gly m 2S albumin.
  • Gly m 39kD.9
  • Gly m Bd28K.
  • Gly m Bd30K, a 30-34 kDa protein, a thiol protease of the papain family, also known as P34.
  • Gly m Lectin.
  • Gly m Bd 60K.
  • Gly m Oleosin.
  • Gly m Trypsin Inhibitor.
  • Gly m IFR, an isoflavone reductase.

Allergen Description

Gly m 5 is a vicilin-like protein, also known as vicilin or alpha Subunit of beta-Conglycinin. Unlike with Gly m 1 and Gly m 2, major allergens to which subjects are exposed through inhalation of Soybean dust, the exposure route to the Gly m 5 allergen is Soybean ingestion.7

Vicilins are seed-storage globulins that are the major components of plant seeds, and constitute important protein sources for the human diet. Also known as 7/8S globulins, these proteins are quantitatively important seed-storage proteins, which often exist as large trimeric oligomers (of about 150 to 190 kDa) in the seed protein bodies, with individual subunits usually 40 to 70 kDa in size.

Vicilin proteins are also known by other names: conarachin of Peanut (Ara h 1), phaseolin of common bean, beta-conglycinin of Soybean, and canavalin of jack bean.20 However, not all vicilins are allergenic.

Sensitisation to the Soybean storage proteins Gly m 5 or Gly m 6 has been shown to be associated with severe reactions to Soybean. Therefore Gly m 5 and Gly m 6 could be considered diagnostic markers for identifying Soy-allergic subjects who are at high risk for severe clinical symptoms.1 However, in Birch tree-prevalent areas, primary sensitisation to Bet v 1 with potential clinical cross-reactivity to Soybean Gly m 4 may be frequent, especially in soy products with a low level of processing; this factor needs to be taken into account when assessing the risk for severe Soybean-related allergic reactions, as Gly m 4 is able to cause severe allergic reactions to Soy in subjects with Birch pollen allergy.1, 5, 10

The potential benefit of evaluating Gly m 5 or Gly m 6 was demonstrated in a clinical study of 25 European adults and 5 children with confirmed Soybean allergy, where no correlation could be demonstrated between the dose of Soybean and the severity of symptoms, nor between the pattern of IgE reactivity (which was highly individual) and the severity of symptoms. However, of the group, 7 (23%) had severe Soy-related allergic reactions, and of these, 6 who experienced anaphylaxis either by history or during Soybean challenge were sensitized to Gly m 5 or Gly m 6.1 The study also reported that the major Soybean storage proteins are putative major soybean allergens in children: in the 5 children with Soy allergy, a high frequency (>50%) of IgE-binding to Gly m 6 and (especially) to Gly m 5 was found.

Compiled by Dr Harris Steinman, developer of Allergy Advisor,


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  2. Krishnan HB, Kim WS, Jang S, Kerley MS. All three subunits of soybean beta-conglycinin are potential food allergens. J Agric Food Chem 2009;57(3):938-43.
  3. Fang N, Yu S, Badger TM. Comprehensive phytochemical profile of soy protein isolate. J Agric Food Chem 2004;52(12):4012-20.
  4. Wilson S, Blaschek K, de Mejia E. Allergenic proteins in soybean: processing and reduction of P34 allergenicity. Nutr Rev 2005;63(2):47-58.
  5. Mittag D, Vieths S, Vogel L, Becker WM, Rihs HP, Helbling A, Wuthrich B, Ballmer-Weber BK. Soybean allergy in patients allergic to birch pollen: clinical investigation and molecular characterization of allergens. J Allergy Clin Immunol 2004;113(1):148-54.
  6. Helm R, Cockrell G, Herman E, Burks A, Sampson H, Bannon G. Cellular and molecular characterization of a major soybean allergen. Int Arch Allergy Immunol 1998;117(1):29-37.
  7. International Union of Immunological Societies Allergen Nomenclature: IUIS official list 2010
  8. Codina R, Oehling AG Jr, Lockey RF. Neoallergens in heated soybean hull. Int Arch Allergy Immunol 1998;117(2):120-5.
  9. Codina R, Lockey RF, Fernandez-Caldas E, Rama R. Purification and characterization of a soybean hull allergen responsible for the Barcelona asthma outbreaks. II. Purification and sequencing of the Gly m 2 allergen. Clin Exp Allergy 1997;27(4):424-30.
  10. Kleine-Tebbe J, Vogel L, Crowell DN, Haustein UF, Vieths S. 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.
  11. Guo P, Piao X, Cao Y, Ou D, Li D. Recombinant Soybean Protein beta-Conglycinin alpha'-Subunit Expression and Induced Hypersensitivity Reaction in Rats. Int Arch Allergy Immunol 2007;145(2):102-110.
  12. Gu X, Beardslee T, Zeece M, Sarath G, Markwell J. Identification of IgE-binding proteins in soy lecithin. Int Arch Allergy Immunol 2001;126(3):218-25.
  13. Tsuji H, Bando N, Hiemori M, Yamanishi R, Kimoto M, Nishikawa K, Ogawa T. Purification of characterization of soybean allergen Gly m Bd 28K. Biosci Biotechnol Biochem 1997;61(6):942-7.
  14. Ogawa T, Tsuji H, Bando N, Kitamura K, Zhu YL, Hirano H, Nishikawa K. Identification of the soybean allergenic protein, Gly m Bd 30K, with the soybean seed 34-kDa oil-body-associated protein. Biosci Biotechnol Biochem 1993;57(6):1030-3.
  15. Fu TJ, Abbott UR, Hatzos C. Digestibility of food allergens and nonallergenic proteins in simulated gastric fluid and simulated intestinal fluid-a comparative study. J Agric Food Chem 2002;50(24):7154-60.
  16. Ogawa A, Samoto M, Takahashi K. Soybean allergens and hypoallergenic soybean products. J Nutr Sci Vitaminol (Tokyo) 2000;46(6):271-9.
  17. Pons L, Chery C, Romano A, Namour F, Artesani MC, Gueant JL. The 18 kDa peanut oleosin is a candidate allergen for IgE-mediated reactions to peanuts. Allergy 2002;57 Suppl 72:88-93.
  18. Baur X, Pau M, et al. Characterization of soybean allergens causing sensitization of occupationally exposed bakers. Allergy 1996;51(5):326-30.
  19. Karamloo F, Wangorsch A, Kasahara H, Davin LB, Haustein D, Lewis NG, Vieths S. Phenylcoumaran benzylic ether and isoflavonoid reductases are a new class of cross-reactive allergens in birch pollen, fruits and vegetables. Eur J Biochem 2001;268(20):5310-20.
  20. Teuber SS, Jarvis KC, Dandekar AM, Peterson WR, Ansari AA. Identification and cloning of a complementary DNA encoding a vicilin-like proprotein, jug r 2, from English walnut kernel (Juglans regia), a major food allergen. J Allergy Clin Immunol 1999;104(6):1311-20.


As in all diagnostic testing, the diagnosis is made by the physican based on both test results and the patient history.