@article{4673,
  keywords = {Bacterial Adhesion, Bacterial Proteins, Adhesins, Bacterial, Focal Adhesions, Lipoproteins, Myxococcales},
  author = {Salim Islam and Nicolas Jolivet and Cl{\'e}mence Cuzin and Akeisha Belgrave and Laetitia My and Betty Fleuchot and Laura Faure and Utkarsha Mahanta and Ahmad Kezzo and Fares Sa{\"\i}di and Gaurav Sharma and Jean-Bernard Fiche and Benjamin Bratton and Julien Herrou and Marcelo Nollmann and Joshua Shaevitz and Eric Durand and T{\^a}m Mignot},
  title = {Unmasking of the von Willebrand A-domain surface adhesin CglB at bacterial focal adhesions mediates myxobacterial gliding motility.},
  abstract = { <p>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.</p> },
  year = {2023},
  journal = {Sci Adv},
  volume = {9},
  pages = {eabq0619},
  month = {2023/02/22},
  issn = {2375-2548},
  doi = {10.1126/sciadv.abq0619},
  language = {eng},
}