Integrin-like tethering of motility complexes at bacterial focal adhesions

Islam, Salim Timo; Belgrave, Akeisha; Jolivet, Nicholas; My, Laetitia; Sharma, Gaurav; Singer, Mitchell; Shaevitz, Joshua et Mignot, Tâm . Integrin-like tethering of motility complexes at bacterial focal adhesions In: 4e Congrès de Bactériologie intégrative INRS-Institut Armand-Frappier, 28 mars 2019, Laval, Québec.

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Résumé

Directed surface motility of metazoan cells and protozoan parasites involves substratum engagement by surface-exposed integrin(-like) adhesins, directionally transported by molecular motors via coupling to the internal cytoskeleton. The predatory deltaproteobacterium Myxococcus xanthus uses a helicallytrafficked motor at bacterial focal adhesions to power gliding motility. However, the mechanisms of gliding machinery–substratum coupling and force mechanotransduction between inner-membrane motors and substratum are unknown. Herein, we use bead force spectroscopy and TIRF microscopy to characterize CglB as the essential substratum-coupling integrin αI-domain-like adhesin. Protease susceptibility reveals that CglB interacts with a globular-protein-accessorized β-barrel OM display platform, which regulates the cell-surface conformational state and accessibility of the adhesin. Surface retention of CglB is further regulated by a cell-surface metalloprotease, a phenomenon also modulated by the OM display platform. These data depict a complex mechanism for bacterial gliding adhesin secretion, cell-surface anchoring, and processing, with conserved themes between prokaryotic and eukaryotic cell motility.

Type de document:	Document issu d'une conférence ou d'un atelier
Mots-clés libres:	adhésions, biofilms
Centre:	Centre INRS-Institut Armand Frappier
Date de dépôt:	01 juill. 2024 14:15
Dernière modification:	01 juill. 2024 14:15
URI:	https://espace.inrs.ca/id/eprint/10327

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