ArticleThe Journal of biological chemistry2020
Hydrogen/deuterium exchange memory NMR reveals structural epitopes involved in IgE cross-reactivity of allergenic lipid transfer proteins.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- Food-Pollen Cross-Reactivity and its Molecular Diagnosis in China.Current allergy and asthma reports · 2024Review
- Epitope binning for multiple antibodies simultaneously using mammalian cell display and DNA sequencing.Communications biology · 2024Article
- Structural Characterization of Monoclonal Antibodies and Epitope Mapping by FFAP Footprinting.Analytical chemistry · 2024Article
- A systematic review of allergen cross-reactivity: Translating basic concepts into clinical relevance.The journal of allergy and clinical immunology. Global · 2024Review
- Human Monoclonal IgE Antibodies-a Major Milestone in Allergy.Current allergy and asthma reports · 2023Review
- Hydrogen Deuterium Exchange and other Mass Spectrometry-based Approaches for Epitope Mapping.Frontiers in analytical science · 2023Article
- Critical structural elements for the antigenicity of wheat allergen LTP1 (Tri a 14) revealed by site-directed mutagenesis.Scientific reports · 2022Article
- Lipid Ligands and Allergenic LTPs: Redefining the Paradigm of the Protein-Centered Vision in Allergy.Frontiers in allergy · 2022Review
- Mapping invisible epitopes by NMR spectroscopy.The Journal of biological chemistry · 2020Article
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Authors and funding
17 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Identification of antibody-binding epitopes is crucial to understand immunological mechanisms. It is of particular interest for allergenic proteins with high cross-reactivity as observed in the lipid transfer protein (LTP) syndrome, which is characterized by severe allergic reactions. Art v 3, a pollen LTP from mugwort, is frequently involved in this cross-reactivity, but no antibody-binding epitopes have been determined so far. To reveal human IgE-binding regions of Art v 3, we produced three murine high-affinity mAbs, which showed 70-90% coverage of the allergenic epitopes from mugwort pollen-allergic patients. As reliable methods to determine structural epitopes with tightly interacting intact antibodies under native conditions are lacking, we developed a straightforward NMR approach termed hydrogen/deuterium exchange memory (HDXMEM). It relies on the slow exchange between the invisible antigen-mAb complex and the free
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