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

Islam, Salim Timo ORCID: https://orcid.org/0000-0001-6853-8446; Jolivet, Nicolas Y; Cuzin, Clémence; Belgrave, Akeisha M; My, Laetitia; Fleuchot, Betty; Faure, Laura M; Mahanta, Utkarsha; Kezzo, Ahmad A; Saïdi, Fares; Sharma, Gaurav; Fiche, Jean-Bernard; Bratton, Benjamin P; Herrou, Julien; Nollmann, Marcelo; Shaevitz, Joshua W; Durand, Eric et Mignot, Tâm (2023). Unmasking of the von Willebrand A-domain surface adhesin CglB at bacterial focal adhesions mediates myxobacterial gliding motility Science Advances , vol. 9 , nº 8:eabq06. pp. 1-20. DOI: 10.1126/sciadv.abq0619.

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Résumé

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.

Type de document:	Article
Mots-clés libres:	Adhesins; Bacterial; Bacterial Adhesion; Bacterial Proteins; Focal Adhesions; Lipoproteins; Myxococcales
Centre:	Centre INRS-Institut Armand Frappier
Date de dépôt:	09 déc. 2023 18:49
Dernière modification:	09 déc. 2023 18:49
URI:	https://espace.inrs.ca/id/eprint/13401

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