Evidence map›Paper›PMID 36812310›Full record

ArticleScience advances2023

Unmasking of the von Willebrand A-domain surface adhesin CglB at bacterial focal adhesions mediates myxobacterial gliding motility.

Salim T Islam, Nicolas Y Jolivet, Clémence Cuzin, Akeisha M Belgrave, Laetitia My, Betty Fleuchot, Laura M Faure, Utkarsha Mahanta, Ahmad A Kezzo, Fares Saïdi and 8 more

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
9.0field-weighted citation impact, top 1% of its field
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

18 citing papers in PubMed, 30 citations in OpenAlex.

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  16. Frontiers in microbiology · 2024
    Review
  17. Whole-Genome Sequence ofMicrobiology resource announcements · 2023
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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

18 authors at 6 institutions in 4 countries.

Salim T IslamInstitut National de la Recherche Scientifique (INRS), Centre Armand-Frappier Santé Biotechnologie, Université du Québec, Institut Pasteur International Network, Laval, QC H7V 1B7, Canada.ORCID 0000-0001-6853-8446
Nicolas Y JolivetInstitut National de la Recherche Scientifique (INRS), Centre Armand-Frappier Santé Biotechnologie, Université du Québec, Institut Pasteur International Network, Laval, QC H7V 1B7, Canada.ORCID 0000-0002-3734-9797
Clémence CuzinLaboratoire de Chimie Bactérienne, CNRS - Université Aix-Marseille UMR7283, Institut de Microbiologie de la Méditerranée, 13009 Marseille, France.ORCID 0000-0002-2972-8199
Akeisha M BelgraveIntegrated Sciences Program, Harrisburg University of Science and Technology, Harrisburg, PA 17101, USA.ORCID 0000-0002-4666-2734
Laetitia MyLaboratoire de Chimie Bactérienne, CNRS - Université Aix-Marseille UMR7283, Institut de Microbiologie de la Méditerranée, 13009 Marseille, France.ORCID 0000-0002-7876-1809
Betty FleuchotLaboratoire de Chimie Bactérienne, CNRS - Université Aix-Marseille UMR7283, Institut de Microbiologie de la Méditerranée, 13009 Marseille, France.
Laura M FaureLaboratoire de Chimie Bactérienne, CNRS - Université Aix-Marseille UMR7283, Institut de Microbiologie de la Méditerranée, 13009 Marseille, France.
Utkarsha MahantaInstitute of Bioinformatics and Applied Biotechnology, Electronic City, Bengaluru-560100, Karnataka, India.ORCID 0000-0002-7543-7931
Ahmad A KezzoInstitut National de la Recherche Scientifique (INRS), Centre Armand-Frappier Santé Biotechnologie, Université du Québec, Institut Pasteur International Network, Laval, QC H7V 1B7, Canada.ORCID 0000-0002-6502-2847
Fares SaïdiInstitut National de la Recherche Scientifique (INRS), Centre Armand-Frappier Santé Biotechnologie, Université du Québec, Institut Pasteur International Network, Laval, QC H7V 1B7, Canada.
Gaurav SharmaInstitute of Bioinformatics and Applied Biotechnology, Electronic City, Bengaluru-560100, Karnataka, India.ORCID 0000-0002-2861-7446
Jean-Bernard FicheCentre de Biochimie Structurale, CNRS UMR5048, INSERM U1054, 34090 Montpellier, France.ORCID 0000-0001-8658-1069
Benjamin P BrattonLewis-Sigler Institute for Integrative Genomics, Princeton University, Princeton, NJ 08540, USA.ORCID 0000-0003-1128-2560
Julien HerrouLaboratoire de Chimie Bactérienne, CNRS - Université Aix-Marseille UMR7283, Institut de Microbiologie de la Méditerranée, 13009 Marseille, France.
Marcelo NollmannCentre de Biochimie Structurale, CNRS UMR5048, INSERM U1054, 34090 Montpellier, France.
Joshua W ShaevitzLewis-Sigler Institute for Integrative Genomics, Princeton University, Princeton, NJ 08540, USA.
Eric DurandLaboratoire de Chimie Bactérienne, CNRS - Université Aix-Marseille UMR7283, Institut de Microbiologie de la Méditerranée, 13009 Marseille, France.
Tâm MignotLaboratoire de Chimie Bactérienne, CNRS - Université Aix-Marseille UMR7283, Institut de Microbiologie de la Méditerranée, 13009 Marseille, France.ORCID 0000-0003-4338-9063
Centre National de la Recherche Scientifique · FRInstitut National de la Recherche Scientifique · CAInstitute of Bioinformatics and Applied Biotechnology · INHarrisburg University of Science and Technology · USPrinceton University · USVanderbilt University · US

Funding

Spatial Patterning During DevelopmentP50GM071508 · NIGMS · PRINCETON UNIVERSITY · PI GAMMIE, ALISON E · 2004 to 2013
$30.6M
NIGMS NIH HHS P50 GM071508
6 · The paper itself

Abstract

The predatory deltaproteobacterium Myxococcus xanthus uses a helically-trafficked motor at bacterial focal-adhesion (bFA) sites to power gliding motility. Using total internal reflection fluorescence and force microscopies, we identify the von Willebrand A domain-containing outer-membrane (OM) lipoprotein CglB as an essential substratum-coupling adhesin of the gliding transducer (Glt) machinery at bFAs. Biochemical and genetic analyses reveal that CglB localizes to the cell surface independently of the Glt apparatus; once there, it is recruited by the OM module of the gliding machinery, a heteroligomeric complex containing the integral OM β barrels GltA, GltB, and GltH, as well as the OM protein GltC and OM lipoprotein GltK. This Glt OM platform mediates the cell-surface accessibility and retention of CglB by the Glt apparatus. Together, these data suggest that the gliding complex promotes regulated surface exposure of CglB at bFAs, thus explaining the manner by which contractile forces exerted by inner-membrane motors are transduced across the cell envelope to the substratum.

Indexed as

MyxococcalesAdhesins, BacterialBacterial AdhesionBacterial ProteinsFocal AdhesionsLipoproteinsAdhesins, BacterialBacterial ProteinsLipoproteins

Identifiers

PMID36812310
PMCPMC9946355
OpenAlexW4321481327

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.