2K7H

NMR solution structure of soybean allergen Gly m 4

Summary for 2K7H

• Entry DOI: 10.2210/pdb2k7h/pdb
• Descriptor: Stress-induced protein SAM22 (1 entity in total)
• Functional Keywords: allergens, soybean, protein, allergen, pathogenesis-related protein, plant defense
• Biological source: Glycine max (Soybean)
• Total number of polymer chains: 1
• Total formula weight: 16658.55

Authors

Berkner, H.,Neudecker, P.,Mittag, D.,Ballmer-Weber, B.K.,Schweimer, K.,Vieths, S.,Roesch, P. (deposition date: 2008-08-11, release date: 2009-05-05, Last modification date: 2024-05-29)

Primary citation

Berkner, H.,Neudecker, P.,Mittag, D.,Ballmer-Weber, B.K.,Schweimer, K.,Vieths, S.
Cross-reactivity of pollen and food allergens: soybean Gly m 4 is a member of the Bet v 1 superfamily and closely resembles yellow lupine proteins
Biosci.Rep., 29:183-192, 2009

PubMed Abstract: In many cases, patients allergic to birch pollen also show allergic reactions after ingestion of certain fruits or vegetables. This observation is explained at the molecular level by cross-reactivity of IgE antibodies induced by sensitization to the major birch pollen allergen Bet v 1 with homologous food allergens. As IgE antibodies recognize conformational epitopes, a precise structural characterization of the allergens involved is necessary to understand cross-reactivity and thus to develop new methods of allergen-specific immunotherapy for allergic patients. Here, we report the three-dimensional solution structure of the soybean allergen Gly m 4, a member of the superfamily of Bet v 1 homologous proteins and a cross-reactant with IgE antibodies originally raised against Bet v 1 as shown by immunoblot inhibition and histamine release assays. Although the overall fold of Gly m 4 is very similar to that of Bet v 1, the three-dimensional structures of these proteins differ in detail. The Gly m 4 local structures that display those differences are also found in proteins from yellow lupine with known physiological function. The three-dimensional structure of Gly m 4 may thus shed some light on the physiological function of this subgroup of PR10 proteins (class 10 of pathogenesis-related proteins) and, in combination with immunological data, allow us to propose surface patches that might represent cross-reactive epitopes.

PubMed: 18834331
DOI: 10.1042/BSR20080117

Experimental method

SOLUTION NMR