Generation of a protein scaffold for the analysis of functional immunoglobulin epitopes of Bet v 1-like allergens
نویسندگان
چکیده
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 and analyze functional immunoglobulin binding sites on Bet v 1 and Bet v 1-like allergens.
منابع مشابه
Find the match! A tool for residue-specific analysis of epitopes in Bet v 1-like allergens
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...
متن کاملA novel approach to specific allergy treatment: the recombinant fusion protein of a bacterial cell surface (S-layer) protein and the major birch pollen allergen Bet v 1 (rSbsC-Bet v 1) combines reduced allergenicity with immunomodulating capacity.
Counterregulating the disease-eliciting Th2-like immune response of allergen-specific Th lymphocytes by fostering an allergen-specific Th1-like response is a promising concept for future immunotherapy of type I allergy. The use of recombinant allergens combined with more functional adjuvants has been proposed. In this respect, we present a novel approach. The gene sequence encoding the major bi...
متن کاملImmunoglobulin E and G4 epitopes of the major allergen of birch pollen Bet v 1 share residues critical for antibody binding
Background Millions of patients with allergy to birch pollen develop clinically cross-reactive IgE against Bet v 1-like proteins in plant foods. Specific immunotherapy (SIT) with birch pollen extracts induces the biosynthesis of Bet v 1-specific immunoglobulin (Ig)G4. IgG4 is believed to act as a blocking antibody preventing IgE binding to Bet v 1, thus alleviating allergic symptoms. Only littl...
متن کاملHomoplasmic Stability and Cytoplasmic Inheritence of DARPin G3 Scaffold Protein in Generative and Vegetative Propagation of Transplastoic Tobacco Plants
Plastid engineering gives numerous benefits for the next generation of transgenic technology, consisting of the convenient use of transgene stacking and the production of high expression levels of recombinant proteins. Designed ankyrin repeat proteins (DARPin) are relatively small non-immunoglobulin scaffold proteins that bind to their specific target with high affinity. The G3 is a type of DAR...
متن کاملConversion of the major birch pollen allergen, Bet v 1, into two nonanaphylactic T cell epitope-containing fragments: candidates for a novel form of specific immunotherapy.
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 ...
متن کامل