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, Gaurav Sharma, Jean Bernard Fiche, Benjamin P. Bratton, Julien Herrou, Marcelo Nollmann, Joshua W. Shaevitz, Eric Durand, Tâm Mignot

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

The predatory deltaproteobacterium Myxococcus xanthus uses a helically-trafficked motor at bacterial focaladhesion (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.

Original languageEnglish (US)
JournalScience Advances
Volume9
Issue number8
DOIs
StatePublished - Feb 2023

All Science Journal Classification (ASJC) codes

  • General

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