Abstract
The transposon TnphoA was used to generate fusions between phoA, the gene for alkaline phosphatase (PhoA), and genes encoding proteins that are secreted by Vibrio cholerae. One of the PhoA+ mutants isolated showed a dramatic reduction in its ability to colonize the intestines of suckling mice. This mutant no longer produced a 20.5-kDa protein (TcpA) that we show is the major subunit of a V. cholerae pilus. Amino-terminal sequence analysis of the TcpA pilus subunit showed that it shares amino acid homology with the pilins produced by several other pathogenic bacteria. The TcpA pilus was coordinately expressed with cholera toxin under various culture conditions, and this effect appeared to be dependent on the transcriptional activator encoded by the toxR gene. We conclude that the toxR gene plays a central role in the transcriptional regulation of multiple virulence genes of V. cholerae.
MeSH Terms
Alkaline Phosphatase/genetics
Amino Acid Sequence
Cholera Toxin/genetics
Fimbriae, Bacterial/physiology,ultrastructure
Gene Expression Regulation
Genes
Genes, Bacterial
Microscopy, Electron
Mutation
Species Specificity
Vibrio cholerae/enzymology,genetics,ultrastructure
Chemicals
Cholera Toxin
Alkaline Phosphatase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Taylor R K
Miller V L
Furlong D B
Mekalanos J J
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