Structural dynamics of RbmA governs plasticity of <i>Vibrio cholerae</i> biofilms.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 28762945.
- Also identified by DOI 10.7554/eLife.26163 and PMC identifier 5605196.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
Biofilm formation is critical for the infection cycle of <i>Vibrio cholerae. Vibrio</i> exopolysaccharides (VPS) and the matrix proteins RbmA, Bap1 and RbmC are required for the development of biofilm architecture. We demonstrate that RbmA binds VPS directly and uses a binary structural switch within its first fibronectin type III (FnIII-1) domain to control RbmA structural dynamics and the formation of VPS-dependent higher-order structures. The structural switch in FnIII-1 regulates interactions in trans with the FnIII-2 domain, leading to open (monomeric) or closed (dimeric) interfaces. The ability of RbmA to switch between open and closed states is important for <i>V. cholerae</i> biofilm formation, as RbmA variants with switches that are locked in either of the two states lead to biofilms with altered architecture and structural integrity.
Medical subject headings
- Bacterial Proteins
- Biofilms
- Vibrio cholerae