{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Alptekin B"],"funding":["Valent Biosciences"],"pagination":["2328-2341"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12329162"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["247(5)"],"pubmed_abstract":["Glomalin, a substance produced by arbuscular mycorrhizal (AM) fungi, has well-documented benefits for plant and soil health, including water retention and soil aggregation. Glomalin quantification has been performed by enzyme-linked immunosorbent assay (ELISA) using a monoclonal antibody, MAb32B11, that has been described as targeting a heat shock protein 60 (RiHSP60). In this study, we re-examined the molecular nature of the antigen recognized by MAb32B11. MAb32B11 did not cross-react with the RiHSP60 polypeptide. Glomalin extracts of Rhizophagus irregularis showed strong and dose-dependent cross-reactivity with MAb32B11 even when protein levels were undetectable, raising doubts about the proteinaceous nature of the antigen. Protease treatments of glomalin extracts did not affect the ELIS"],"journal":["The New phytologist"],"pubmed_title":["From glomalin to glomalose: unraveling the molecular identity of the MAb32B11 antigen."],"pmcid":["PMC12329162"],"funding_grant_id":["MSN279975"],"pubmed_authors":["Hirsch H","Daniels D","Alptekin B","King L","Irving T","Floss D","Ane JM","Kleven B","McLimans C"],"additional_accession":[]},"is_claimable":false,"name":"From glomalin to glomalose: unraveling the molecular identity of the MAb32B11 antigen.","description":"Glomalin, a substance produced by arbuscular mycorrhizal (AM) fungi, has well-documented benefits for plant and soil health, including water retention and soil aggregation. Glomalin quantification has been performed by enzyme-linked immunosorbent assay (ELISA) using a monoclonal antibody, MAb32B11, that has been described as targeting a heat shock protein 60 (RiHSP60). In this study, we re-examined the molecular nature of the antigen recognized by MAb32B11. MAb32B11 did not cross-react with the RiHSP60 polypeptide. Glomalin extracts of Rhizophagus irregularis showed strong and dose-dependent cross-reactivity with MAb32B11 even when protein levels were undetectable, raising doubts about the proteinaceous nature of the antigen. Protease treatments of glomalin extracts did not affect the ELIS","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Sep","modification":"2026-04-12T19:25:00.841Z","creation":"2026-04-07T13:17:34.813Z"},"accession":"S-EPMC12329162","cross_references":{"pubmed":["40474598"],"doi":["10.1111/nph.70253"]}}