Abstract
Background Birch pollen-allergic subjects often develop Bet v 1-specific IgE that cross-reacts with homologous food allergens. Bet v 1 and its homologs in pollen and food display exclusively conformational epitopes. We established a system to specifically analyze epitope cross-reactivity of Bet v 1-related allergens. The enzyme norcoclaurine synthase (NCS) from Thalictrum flavum is structurally homologous to Bet v 1 but does not bind IgE reacting with Bet v 1-like allergens. By substituting amino acids in a variant of NCS, the impact of individual residues of Bet v 1-like allergens in IgE binding can be studied.
Highlights
Birch pollen-allergic subjects often develop Bet v 1-specific IgE that cross-reacts with homologous food allergens
Sera of birch pollen allergic patients were analyzed for IgE binding to norcoclaurine synthase (NCS) variants and Bet v 1-like food allergens
CD spectra and 1H15N-HSQC NMR indicated Bet v 1-like structure of NCS variants. sIgE binding increased significantly with the number of amino acids substituted in NCS from ≤ 0.35 kUA/L in 94% (65/69) of sera to CAP values up to 17.4 kUA/L for NCSN57/I58E/D60N/V63P/D68K (NCS_5x) in 68% (47/69) of sera
Summary
Find the match! A tool for residue-specific analysis of epitopes in Bet v 1-like allergens. A tool for residue-specific analysis of epitopes in Bet v 1-like allergens. Dirk Schiller1*, Hanna Berkner, Maximilian Hartl, Christian Seutter von Loetzen, Michaela Gubesch, Felix Husslik, Daniela Weigand, Iris Lauer, Andreas Reuter, Jonas Lidholm, Barbara Ballmer-Weber, Stefan Vieths, Paul Rösch, Dirk Schiller. From 5th International Symposium on Molecular Allergology (ISMA 2013) Vienna, Austria. From 5th International Symposium on Molecular Allergology (ISMA 2013) Vienna, Austria. 6-7 December 2013
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