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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

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In many cases, patients allergic to birch pollen also show allergic reactions after ingestion of plant-derived food. This observation is explained on 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 present 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 differ in detail. The Gly m 4 local structures that display those differences are also found in proteins from yellow lupine. The three-dimensional structure of Gly m 4 in combination with immunological data allows us to propose surface patches that might represent cross-reactive epitopes.

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Correspondence to Paul Rösch.

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This article is published under license to BioMed Central Ltd. This is an open access article distributed under the terms of the Creative Commons Attribution License (, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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  • Food Allergen
  • Surface Patch
  • Pollen Allergen
  • Birch Pollen
  • Conformational Epitope