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

Abstract : 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.
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Petya Violinova Krasteva, Joaquin Bernal-Bayard, Laetitia Travier, Fernando Ariel Martin, Pierre-Alexandre Kaminski, et al.. Insights into the structure and assembly of a bacterial cellulose secretion system. Nature Communications, Nature Publishing Group, 2017, 8 (1), pp.2065. ⟨10.1038/s41467-017-01523-2⟩. ⟨pasteur-01688314⟩

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