UC Santa Cruz

Vibrio cholerae is a human pathogen that is responsible for the diarrheal disease cholera. V. cholerae is able to persist in the aquatic environment due to its ability to form biofilm as a means of protection from environmental assaults. Biofilms are a surface-associated growth form where aggregated cells are encased by an extracellular matrix made of exopolysaccharides (EPS), extracellular and surface-associated proteins, and extracellular DNA. Biofilm-associated proteins have diverse roles in biofilm formation and have been shown to be important for biofilm survival and growth. We identified the V. cholerae biofilm matrix proteome and identified a previously uncharacterized biofilm matrix protein which we termed VbpA (Vibrio biofilm protein A). We found that VbpA is present both in periplasm and in extracellular matrix; the lack of VbpA drastically alters V. cholerae biofilm architecture, signifying that VbpA plays an important role in biofilm assembly. Further characterization of VbpA revealed how it impacts known matrix proteins and biofilm architecture. We also compared the biofilm matrix and cellular proteome of the rugose strain and the vbpA mutant. This analysis showed that the lack of VbpA does not result in global changes to the proteome. A better understanding of the function of this protein can provide insight into possible targets for disrupting V. cholerae biofilms, preventing the survival and transmission of the pathogen.