Evidence map›Paper›PMID 40474598›Full record

ArticleThe New phytologist2025

From glomalin to glomalose: unraveling the molecular identity of the MAb32B11 antigen.

Burcu Alptekin, Hayley Hirsch, Bailey Kleven, Lauren King, Caitlin McLimans, Dierdra Daniels, Thomas Irving, Daniela Floss, Jean-Michel Ané

Abstract read
In one paragraph

Article in The New phytologist, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Burcu Alptekin *Department of Bacteriology, University of Wisconsin - Madison, Madison, WI, 53706, USA.ORCID https://orcid.org/0000-0002-0041-0240
Hayley Hirsch *Department of Bacteriology, University of Wisconsin - Madison, Madison, WI, 53706, USA.ORCID https://orcid.org/0009-0003-0783-5828
Bailey KlevenDepartment of Bacteriology, University of Wisconsin - Madison, Madison, WI, 53706, USA.ORCID https://orcid.org/0000-0001-8889-9310
Lauren KingDepartment of Bacteriology, University of Wisconsin - Madison, Madison, WI, 53706, USA.ORCID https://orcid.org/0009-0000-6020-6287
Caitlin McLimansDepartment of Bacteriology, University of Wisconsin - Madison, Madison, WI, 53706, USA.ORCID https://orcid.org/0009-0003-9707-2595
Dierdra DanielsValent BioSciences, Libertyville, IL, 60048, USA.ORCID https://orcid.org/0000-0001-8015-7005
Thomas IrvingDepartment of Bacteriology, University of Wisconsin - Madison, Madison, WI, 53706, USA.ORCID https://orcid.org/0000-0003-3040-4543
Daniela FlossValent BioSciences, Libertyville, IL, 60048, USA.ORCID https://orcid.org/0009-0009-0639-5713
Jean-Michel AnéDepartment of Bacteriology, University of Wisconsin - Madison, Madison, WI, 53706, USA.ORCID https://orcid.org/0000-0002-3128-9439

Funding

Valent Biosciences MSN279975
6 · The paper itself

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 ELISA signal. However, treatment with periodate, which degrades polysaccharides, significantly reduced the signal. A strong correlation between carbohydrate content and the ELISA signal was observed in glomalin extracts. These findings indicate that MAb32B11 recognizes a carbohydrate, likely originating from cell walls of AM fungi. Further analysis of glomalin extracts using size exclusion chromatography suggests that the epitope of MAb32B11 is a complex carbohydrate in the size range of 511-600 kDa. Understanding the true nature of glomalin will enhance our ability to quantify it accurately and leverage its agricultural benefits.

Indexed as

Antibodies, MonoclonalAntigens, FungalFungal ProteinsCross ReactionsEnzyme-Linked Immunosorbent AssayGlycoproteinsMycorrhizaeAntibodies, MonoclonalAntigens, FungalFungal ProteinsglomalinGlycoproteinsarbuscular mycorrhizal fungicarbon sinkglomalinHSP60soil health

Identifiers

PMID40474598
PMCPMC12329162

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.