ArticleThe Journal of allergy and clinical immunology2024
Structural analysis of human IgE monoclonal antibody epitopes on dust mite allergen Der p 2.
Article in The Journal of allergy and clinical immunology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Characterization of a major house dust mite allergen Der p 22 among Malaysian adult population.The World Allergy Organization journal · 2025Article
- Human IgE monoclonal antibodies define two unusual epitopes trapping dog allergen Can f 1 in different conformations.Protein science : a publication of the Protein Society · 2025Article
- Epitope-Specific Antibodies in Allergic Disease and Clinical Tolerance.Immunological reviews · 2025Review
- Editorial: Allergen-specific antibodies: from basic science to clinical application.Frontiers in allergy · 2025Article
- Pre-clinical allergenicity assessment of IgE epitope-targeted Der p 2 mutants demonstrate potential as hypoallergenic AIT candidates.Frontiers in immunology · 2025Article
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Authors and funding
13 authors.
Funding
Abstract
backgroundHuman 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.
objectiveWe 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.
methodsX-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.
resultsThe structure of recombinant Der p 2 with hIgE mAb 4C8 Fab was determined at 3.05 Å. The newly identified epitope region does not overlap with the hIgE mAb 2F10 epitope or the region recognized by 3 overlapping hIgE mAbs (1B8, 5D10, and 2G1). Compared with wild-type Der p 2, single or double 4C8 and 2F10 epitope mutants bound less IgE antibodies from allergic patients by as much as 93%. Human FcεRIα-transgenic mice sensitized by hIgE mAbs, which were susceptible to anaphylaxis when challenged with wild-type Der p 2, could no longer cross-link FcεRI to induce anaphylaxis when challenged with the epitope mutants.
conclusionsThese data establish the structural basis of allergenicity of 2 hIgE mAb nonoverlapping epitopes on Der p 2, which appear to make important contributions to the hIgE repertoire against Der p 2 and provide molecular targets for future design of allergy therapeutics.
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