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© J.M. Ghigo (Institut Pasteur) and Brigite Arbeille (LBC-ME. Faculté de Médecine de Tours)
Colorized scanning electron microscopy of an E. coli biofilm developing on a glass surface
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Nature Communications - 25 Sep 2017

Krasteva, P.V.*#, J. Bernal*, L. Travier, F.A. Martin, P.A. Kaminski, G. Karimova, R. Fronzes, and J.-M. Ghigo*#. (*equal contribution; # co-corresponding authors)

Link to Pubmed [PMID] – 29234007

Nat Commun. 2017 Dec 12;8(1):2065. doi: 10.1038/s41467-017-01523-2.

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. Whereas 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. Together, 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.

https://www.ncbi.nlm.nih.gov/pubmed/29234007