Abstract
Methods bGST was expressed in Escherichia coli, purified and characterized by mass spectrometry. BALB/c mice were immunized with bGST or Bet v 1. Antibody and T cell responses were assessed. 217 sera from birch pollen-allergic patients were tested for IgE-reactivity to bGST by ELISA. The allergenicity of bGST was evaluated with IgE-loaded rat basophil leukaemia cells (RBL) expressing the a-chain of the human receptor FceRI. Cross-reactivity of IgE between bGST and GST from house dust mite, Der p 8, was assessed with murine and human sera in ELISA. The release kinetics of bGST and Bet v 1 from birch pollen upon hydration were studied by immunoblotting.
Highlights
Proteomic profiling of birch pollen detected a protein homologous to glutathione-S-transferases (GST) in prominent amounts
Glutathione-s-transferase is a minor allergen in birch pollen because of restricted release from hydrated pollen grains
The minor allergenicity of bGST may be explained by a limited exposure of patients to this protein
Summary
Proteomic profiling of birch pollen detected a protein homologous to glutathione-S-transferases (GST) in prominent amounts. Glutathione-s-transferase is a minor allergen in birch pollen because of restricted release from hydrated pollen grains Stephan Deifl1*, Christian Zwicker1, Eva Vejvar2, Claudia Kitzmüller1, Gabriele Gadermaier2, Birgit Nagl1, Susanne Vrtala1, Gerhard Zlabinger3, Peter Briza2, Fatima Ferreira2, Barbara Bohle1 From 5th International Symposium on Molecular Allergology (ISMA 2013) Vienna, Austria. Background Recently, proteomic profiling of birch pollen detected a protein homologous to glutathione-S-transferases (GST) in prominent amounts.
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