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  • Open Access

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

  • 1,
  • 1,
  • 1,
  • 2,
  • 2,
  • 3,
  • 1 and
  • 4
Clinical and Translational Allergy20111 (Suppl 1) :P6

https://doi.org/10.1186/2045-7022-1-S1-P6

  • Published:

Keywords

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

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.

Authors’ Affiliations

(1)
Universität Bayreuth, Biopolymere, Bayreuth, Germany
(2)
University Hospital, Dermatology, Zürich, Switzerland
(3)
Klinische Chemie und Laboratoriumsmedizin, Universitätsklinikum Regensburg, Regensburg, Germany
(4)
Paul-Ehrlich-Institut, Allergologie, Langen, Germany

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