KRASTEVA, Petya Violinova; BERNAL-BAYARD, Joaquin; TRAVIER, Laetitia; MARTIN, Fernando Ariel; KAMINSKI, Pierre-Alexandre; KARIMOVA, Gouzel; FRONZES, Rémi; GHIGO, Jean-Marc

doi:10.1038/s41467-017-01523-2

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Article de revue

Ce document a été publié dans

Nature Communications. 2017-12-12, vol. 8, n° 1, p. 2065

Résumé en anglais

Secreted exopolysaccharides present important determinants for bacterial biofilm formation, survival, and virulence. Cellulose secretion typically requires the concerted action of a c-di-GMP-responsive inner membrane synthase (BcsA), an accessory membrane-anchored protein (BcsB), and several additional Bcs components. Although the BcsAB catalytic duo has been studied in great detail, its interplay with co-expressed subunits remains enigmatic. Here we show that E. coli Bcs proteins partake in a complex protein interaction network. Electron microscopy reveals a stable, megadalton-sized macromolecular assembly, which encompasses most of the inner membrane and cytosolic Bcs components and features a previously unobserved asymmetric architecture. Heterologous reconstitution and mutational analyses point toward a structure-function model, where accessory proteins regulate secretion by affecting both the assembly and stability of the system. Altogether, these results lay the foundation for more comprehensive models of synthase-dependent exopolysaccharide secretion in biofilms and add a sophisticated secretory nanomachine to the diverse bacterial arsenal for virulence and adaptation.< Réduire

Mots clés en anglais

Bacterial secretion

Bacterial structural biology

Biofilms

Electron microscopy

URI

https://oskar-bordeaux.fr/handle/20.500.12278/183213

DOI

http://dx.doi.org/10.1038/s41467-017-01523-2

Projet Européen

Molecular and Structural Biology of Bacterial Transformation

Project ANR

Integrative Biology of Emerging Infectious Diseases - ANR-10-LABX-0062

Unités de recherche

MFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234

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Insights into the structure and assembly of a bacterial cellulose secretion system