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

Petya Violinova Krasteva (), Joaquin Bernal-Bayard, Laetitia Travier, Fernando Ariel Martin, Pierre-Alexandre Kaminski, Gouzel Karimova, Rémi Fronzes and Jean-Marc Ghigo ()
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Petya Violinova Krasteva: Institut Pasteur, 25–28 rue du Docteur Roux
Joaquin Bernal-Bayard: Institut Pasteur
Laetitia Travier: Institut Pasteur
Fernando Ariel Martin: Institut Pasteur
Pierre-Alexandre Kaminski: Institut Pasteur, 25–28 rue du Docteur Roux
Gouzel Karimova: Institut Pasteur, 25–28 rue du Docteur Roux
Rémi Fronzes: Institut Pasteur, 25–28 rue du Docteur Roux
Jean-Marc Ghigo: Institut Pasteur

Nature Communications, 2017, vol. 8, issue 1, 1-10

Abstract: 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.

Date: 2017
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-01523-2

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DOI: 10.1038/s41467-017-01523-2

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