Find the match! A tool for residue-specific analysis of epitopes in Bet v 1-like allergens
نویسندگان
چکیده
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.
منابع مشابه
Generation of a protein scaffold for the analysis of functional immunoglobulin epitopes of Bet v 1-like allergens
Background Millions of patients with allergy to tree pollen are sensitized to the major allergen of birch (Betula verrucosa) pollen, Bet v 1. Bet v 1-specific IgE cross-reacts with Bet v 1-homologous proteins from plant foods. Only little information on functional IgE epitopes of Bet v 1 and Bet v 1-like allergens in foods is available. We sought to generate a synthetic protein tool to identify...
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A novel approach to reduce the anaphylactic activity of allergens is suggested. The strategy makes use of the presence of conformational immunoglobulin E (IgE) epitopes on one of the most common allergens. The three dimensional structure of the major birch pollen allergen, Bet v 1, was disrupted by expressing two parts of the Bet v 1 cDNA representing amino acids 1-74 and 75-160 in Escherichia ...
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