Structural analysis of human IgE monoclonal antibody epitopes on dust mite allergen Der p 2.

ABSTRACT:

Background

Human IgE (hIgE) mAbs against major mite allergen Der p 2 developed using human hybridoma technology were used for IgE epitope mapping and analysis of epitopes associated with the hIgE repertoire.

Objective

We sought to elucidate the new hIgE mAb 4C8 epitope on Der p 2 and compare it to the hIgE mAb 2F10 epitope in the context of the allergenic structure of Der p 2.

Methods

X-ray crystallography was used to determine the epitope of anti-Der p 2 hIgE mAb 4C8. Epitope mutants created by targeted mutagenesis were analyzed by immunoassays and in vivo using a human high-affinity IgE receptor (FcεRIα)-transgenic mouse model of passive systemic anaphylaxis.

Results

The structure of recombinant Der p 2 with hIgE mAb 4C8 Fab was determined at 3.05 Å. The newl

SUBMITTER: Ball A 

PROVIDER: S-EPMC11409219 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature