<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Alptekin B</submitter><funding>Valent Biosciences</funding><pagination>2328-2341</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12329162</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>247(5)</volume><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</pubmed_abstract><journal>The New phytologist</journal><pubmed_title>From glomalin to glomalose: unraveling the molecular identity of the MAb32B11 antigen.</pubmed_title><pmcid>PMC12329162</pmcid><funding_grant_id>MSN279975</funding_grant_id><pubmed_authors>Hirsch H</pubmed_authors><pubmed_authors>Daniels D</pubmed_authors><pubmed_authors>Alptekin B</pubmed_authors><pubmed_authors>King L</pubmed_authors><pubmed_authors>Irving T</pubmed_authors><pubmed_authors>Floss D</pubmed_authors><pubmed_authors>Ane JM</pubmed_authors><pubmed_authors>Kleven B</pubmed_authors><pubmed_authors>McLimans C</pubmed_authors></additional><is_claimable>false</is_claimable><name>From glomalin to glomalose: unraveling the molecular identity of the MAb32B11 antigen.</name><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</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 Sep</publication><modification>2026-04-12T19:25:00.841Z</modification><creation>2026-04-07T13:17:34.813Z</creation></dates><accession>S-EPMC12329162</accession><cross_references><pubmed>40474598</pubmed><doi>10.1111/nph.70253</doi></cross_references></HashMap>