ArticleInflammation research : official journal of the European Histamine Research Society ... [et al.]2017
Mapping of the binding sites of human histamine N-methyltransferase (HNMT) monoclonal antibodies.
Article in Inflammation research : official journal of the European Histamine Research Society ... [et al.], 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 11 citations in OpenAlex.
- Sea Cucumber Polysaccharides Promote Gut-Liver Axis Health by Modulating Microbiota, Metabolism, and Gene Expression in Mice.Foods (Basel, Switzerland) · 2025Article
- HNMT Upregulation Induces Cancer Stem Cell Formation and Confers Protection against Oxidative Stress through Interaction with HER2 in Non-Small-Cell Lung Cancer.International journal of molecular sciences · 2022Article
- Histamine Intolerance: The Current State of the Art.Biomolecules · 2020Review
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Authors and funding
3 authors at 2 institutions in 2 countries.
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Abstract
objectiveRecently, we characterized mouse monoclonal antibodies that allow the specific and sensitive detection of human histamine N-methyltransferase (HNMT). To understand differences in binding characteristics and recognition of enzyme variants we mapped the antibody binding sites.
methodsFragments of human HNMT were expressed as glutathione S-transferase fusion proteins that were used for testing antibody binding on immunoblots. Combined information from species cross-reactivity, sequence comparison, protein structure, and binding site prediction software were used to localize the epitope recognized by each antibody.
resultsAll eight monoclonal HNMT antibodies bound to linear epitopes in the C-terminal domain of the 292 amino acid protein. Of the five antibodies cross-reacting with HNMT from other species, one bound region L
conclusionsOur HNMT monoclonal antibodies bind in three different regions of the protein and those binding the same putative epitope exhibit similar binding characteristics and species cross-reactivity. Antibodies binding non-overlapping epitopes will facilitate analyses of all clinically relevant variants described for HNMT.
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