Unmasking of the von Willebrand A-domain surface adhesin CglB at bacterial focal adhesions mediates myxobacterial gliding motility
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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.
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Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
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- Authors
- Islam, S. T., Jolivet, N. Y., Cuzin, C., Belgrave, A. M., My, L., Fleuchot, B., Faure, L. M., Mahanta, U., Kezzo, A. A., Saïdi, F., Sharma, G., Fiche, J.-B., Bratton, B. P., Herrou, J., Nollmann, M., Shaevitz, J. W., Durand, E., & Mignot, T.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Institut National de la Recherche Scientifique (CA)
- Harrisburg University of Science and Technology (US)
- Laboratoire de Chimie Bactérienne, CNRS - Université Aix-Marseille UMR7283, Institut de Microbiologie de la Méditerranée, 13009 Marseille, France.
- Institute of Bioinformatics and Applied Biotechnology (IN)
- Vanderbilt University (US)
- Centre de Biochimie Structurale, CNRS UMR5048, INSERM U1054, 34090 Montpellier, France.
- Princeton University (US)
- Corresponding author
- Islam, Salim T.
- Jolivet, Nicolas Y.
- Cuzin, Clémence
- Mignot, Tâm
- ORCID
- Venue
- Science Advances
- Published
- 2023-02-24
- Volume
- 9
- Issue
- 8
- Pages
- eabq0619-eabq0619
- ISSN
- 2375-2548 (ISSN-L)
- PMC
- PMC9946355
- OpenAlex
- W4321481327
- Cited by
- 38
- References
- 2
- Citations by year
- 2026: 3 · 2025: 7 · 2024: 17 · 2023: 5 · 2022: 3 · 2021: 3
- FWCI
- 5.31
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by-nc
- Locations
- Science Advances (publishedVersion, cc-by-nc)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Research Archive of Indian Institute of Technology Hyderabad (Indian Institute of Technology Hyderabad) (acceptedVersion)
- HAL (submittedVersion, cc-by-nc)
- EspaceINRS (National Institute for Scientific Research (Canada)) (submittedVersion)
- HAL (submittedVersion)
- Funders
- National Science Foundation (0844466, CAREER)
- Aix-Marseille Université
- Fondation ARC pour la Recherche sur le Cancer
- Centre National de la Recherche Scientifique
- National Institutes of Health (GM071508)
- Canadian Institutes of Health Research
- Natural Sciences and Engineering Research Council of Canada (06637, rgpin-2016-06637)
- National Institute of General Medical Sciences (P50GM071508)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Escherichia coli research studies
- Keywords
- Myxococcus xanthus, gliding motility, outer membrane lipoprotein, gltA, force transduction, surface adhesins
- MeSH terms
- Bacterial Adhesion, Bacterial Proteins, Lipoproteins, Myxococcales, Adhesins, Bacterial, Focal Adhesions
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