Abstract
Vibrio cholerae biofilms contain exopolysaccharide and three matrix proteins RbmA, RbmC and Bap1. While much is known about exopolysaccharide regulation, little is known about the mechanisms by which the matrix protein components of biofilms are regulated. VrrA is a conserved, 140-nt sRNA of V. cholerae, whose expression is controlled by sigma factor σE. In this study, we demonstrate that VrrA negatively regulates rbmC translation by pairing to the 5′ untranslated region of the rbmC transcript and that this regulation is not stringently dependent on the RNA chaperone protein Hfq. These results point to VrrA as a molecular link between the σE-regulon and biofilm formation in V. cholerae. In addition, VrrA represents the first example of direct regulation of sRNA on biofilm matrix component, by-passing global master regulators.
Highlights
Vibrio cholerae inhabits aquatic environments and when it enters the human intestine, e. g., through ingestion of contaminated food or water, it causes the severe diarrheal disease, cholera
We showed that VrrA mutant variants covering the VrrA region from residues 69–78 was responsible to base-pair with 59 untranslated regions (UTR) of ompT mRNA [36]
Results from this study add a new class of regulators, sRNAs, as a direct regulator of a biofilm matrix component
Summary
Vibrio cholerae inhabits aquatic environments and when it enters the human intestine, e. g., through ingestion of contaminated food or water, it causes the severe diarrheal disease, cholera. In V. cholerae, formation of biofilm requires production of exopolysaccharide (VPS) and the biofilm matrix proteins RbmA, RbmC and Bap1 [14,15,16,17,18]. These matrix proteins appear to be involved at particular steps during the biofilm formation process. RbmA is involved in the initial cell-cell adhesion step and serves as a tether, forming flexible linkages between cells and the extracellular matrix [18,19]; Bap facilitates adherence of the developing biofilm to surfaces; and the heterogeneous mixtures of VPS, RbmC and Bap appear to form envelopes to encase the cell clusters [18]. Without RbmC, incorporation of VPS through the biofilms is significantly reduced, suggesting an essential role for RbmC in maintaining the mature biofilm structure [18]
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