ArticleProceedings of the National Academy of Sciences of the United States of America2015
In situ proteolysis of the Vibrio cholerae matrix protein RbmA promotes biofilm recruitment.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Bacterial zinc metalloproteases as facilitators of pathogenic success: a review.Archives of microbiology · 2026Review
- Article
- Surface remodeling and inversion of cell-matrix interactions underlie community recognition and dispersal in Vibrio cholerae biofilms.Nature communications · 2025Article
- A large-scale type I CBASS antiphage screen identifies the phage prohead protease as a key determinant of immune activation and evasion.Cell host & microbe · 2024Article
- Vibrio cholerae biofilms use modular adhesins with glycan-targeting and nonspecific surface binding domains for colonization.Nature communications · 2023Article
- Cell specialization in cyanobacterial biofilm development revealed by expression of a cell-surface and extracellular matrix protein.NPJ biofilms and microbiomes · 2023Article
- Matrix is everywhere: extracellular DNA is a link between biofilm and mineralization in Bacillus cereus planktonic lifestyle.NPJ biofilms and microbiomes · 2023Article
- New Insights into Vibrio cholerae Biofilms from Molecular Biophysics to Microbial Ecology.Advances in experimental medicine and biology · 2023Article
- Secreted Proteases Control the Timing of Aggregative Community Formation in Vibrio cholerae.mBio · 2021Article
- Massive Integration of Planktonic Cells within a Developing Biofilm.Microorganisms · 2021Article
- Vibrio cholerae biofilm scaffolding protein RbmA shows an intrinsic, phosphate-dependent autoproteolysis activity.IUBMB life · 2021Article
- Searching for the Secret of Stickiness: How Biofilms Adhere to Surfaces.Frontiers in microbiology · 2021Review
- Cell position fates and collective fountain flow in bacterial biofilms revealed by light-sheet microscopy.Science (New York, N.Y.) · 2020Article
- Reciprocal c-di-GMP signaling: Incomplete flagellum biogenesis triggers c-di-GMP signaling pathways that promote biofilm formation.PLoS genetics · 2020Article
- Potential of NFrontiers in microbiology · 2020Review
- Breakdown of Vibrio cholerae biofilm architecture induced by antibiotics disrupts community barrier function.Nature microbiology · 2019Article
- Biofilms: The Microbial "Protective Clothing" in Extreme Environments.International journal of molecular sciences · 2019Review
- Functional characterization of a subtilisin-like serine protease fromThe Journal of biological chemistry · 2019Article
- Article
- A Self-Assembling Whole-Cell Vaccine Antigen Presentation Platform.Journal of bacteriology · 2018Article
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Authors and funding
6 authors.
Funding
Abstract
The estuarine gram-negative rod and human diarrheal pathogen Vibrio cholerae synthesizes a VPS exopolysaccharide-dependent biofilm matrix that allows it to form a 3D structure on surfaces. Proteins associated with the matrix include, RbmA, RbmC, and Bap1. RbmA, a protein whose crystallographic structure suggests two binding surfaces, associates with cells by means of a VPS-dependent mechanism and promotes biofilm cohesiveness and recruitment of cells to the biofilm. Here, we show that RbmA undergoes limited proteolysis within the biofilm. This proteolysis, which is carried out by the hemagglutinin/protease and accessory proteases, yields the 22-kDa C-terminal polypeptide RbmA*. RbmA* remains biofilm-associated. Unlike full-length RbmA, the association of RbmA* with cells is no longer VPS-dependent, likely due to an electropositive surface revealed by proteolysis. We provide evidence that this proteolysis event plays a role in recruitment of VPS(-) cells to the biofilm surface. Based on our findings, we propose that association of RbmA with the matrix reinforces the biofilm structure and leads to limited proteolysis of RbmA to RbmA*. RbmA*, in turn, promotes recruitment of cells that have not yet initiated VPS synthesis to the biofilm surface. The assignment of two functions to RbmA, separated by a proteolytic event that depends on matrix association, dictates an iterative cycle in which reinforcement of recently added biofilm layers precedes the recruitment of new VPS(-) cells to the biofilm.
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