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- W2014434049 abstract "A common epitope in Der_p_1 and Der_f_1, and a Der_p_1-specific epitope, both involved in IgE antibody binding, were identified by determining the X-ray crystal structures of each allergen in complex with a monoclonal antibody (mAb). The Der_p_1-specific mAb10B9 interferes with the binding of the cross-reactive mAb4C1 to Der_p_1, but not Der_f_1. The goal was to identify the amino acids that confer specificity for mAb10B9 by engineering a new mAb10B9 epitope on Der_f_1. Site-directed mutagenesis was performed in Der_f_1 based on the analysis of allergen-antibody crystal structures. Mutants were expressed in yeast Pichia pastoris, purified by affinity chromatography and analyzed by antibody binding assays. The expected overlap between epitopes for mAb4C1 and mAb10B9 was partial. Der_f_1 residues in equivalent positions to those in Der_p_1 recognized by mAb10B9, but not involved in 4C1mAb binding, were selected for mutagenesis. Four serines in Der_f_1 were sequentially mutated into the equivalent Der_p_1 residues (Ala, Gln, Asn). The mutation of at least two residues was sufficient for antibody binding by ELISA, indicating the creation of a new epitope. Dose-response curves displaced to the left and an increase in saturation levels of antibody binding as more substitutions were present in Der_f_1 indicated an increase in antibody affinity for the allergen. Specific residues for mAb10B9 binding were identified by creating a de novo epitope on Der_f_1. Structural studies of allergen epitopes combined with mutagenesis analysis provide detailed information to understand determinants of specificity and cross-reactivity, and are a proof-of-principle for analyzing allergen-IgE interactions." @default.
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- W2014434049 date "2013-02-01" @default.
- W2014434049 modified "2023-09-27" @default.
- W2014434049 title "De Novo Creation of an Antibody Binding Epitope On Group 1 Mite Allergens" @default.
- W2014434049 doi "https://doi.org/10.1016/j.jaci.2012.12.735" @default.
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