Unmasking of the von Willebrand A-domain surface adhesin CglB at bacterial focal adhesions mediates myxobacterial gliding motility. Author Salim Islam, Nicolas Jolivet, Clémence Cuzin, Akeisha Belgrave, Laetitia My, Betty Fleuchot, Laura Faure, Utkarsha Mahanta, Ahmad Kezzo, Fares Saïdi, Gaurav Sharma, Jean-Bernard Fiche, Benjamin Bratton, Julien Herrou, Marcelo Nollmann, Joshua Shaevitz, Eric Durand, Tâm Mignot Publication Year 2023 Type Journal Article 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. Keywords Bacterial Adhesion, Bacterial Proteins, Adhesins, Bacterial, Focal Adhesions, Lipoproteins, Myxococcales Journal Sci Adv Volume 9 Issue 8 Pages eabq0619 Date Published 2023/02/22 ISSN Number 2375-2548 DOI 10.1126/sciadv.abq0619 Alternate Journal Sci Adv PMCID PMC9946355 PMID 36812310 PubMedPubMed CentralGoogle ScholarBibTeXEndNote X3 XML