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Journal of Bacteriology, July 2004, p. 4613-4619, Vol. 186, No. 14
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.14.4613-4619.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

The Vibrio cholerae FlgM Homologue Is an Anti-{sigma}28 Factor That Is Secreted through the Sheathed Polar Flagellum

Nidia E. Correa, Jeffrey R. Barker, and Karl E. Klose*

Department of Microbiology and Immunology, University of Texas Health Science Center, San Antonio, Texas

Received 20 February 2004/ Accepted 8 April 2004

Vibrio cholerae has a single polar sheathed flagellum that propels the cells of this bacterium. Flagellar synthesis, motility, and chemotaxis have all been linked to virulence in this human pathogen. V. cholerae expresses flagellar genes in a hierarchy consisting of {sigma}54- and {sigma}28-dependent transcription. In other bacteria, {sigma}28 transcriptional activity is controlled by an anti-{sigma}28 factor, FlgM. We demonstrate that the V. cholerae FlgM homologue (i) physically interacts with {sigma}28, (ii) has a repressive effect on some V. cholerae {sigma}28-dependent flagellar promoters, and (iii) is secreted through the polar sheathed flagellum, consistent with anti-{sigma}28 activity. Interestingly, FlgM does not have a uniform repressive effect on all {sigma}28-dependent promoters, as determined by measurement of {sigma}28-dependent transcription in cells either lacking FlgM ({Delta}flgM) or incapable of secretion ({Delta}fliF). Further analysis of a {Delta}fliF strain revealed that this flagellar assembly block causes a decrease in class III (FlrC- and {sigma}54-dependent) and class IV ({sigma}28-dependent), but not class II (FlrA- and {sigma}54-dependent), flagellar transcription. V. cholerae flgM and fliA (encodes {sigma}28) mutants were only modestly affected in their ability to colonize the infant mouse intestine, a measure of virulence. Our results demonstrate that V. cholerae FlgM functions as an anti-{sigma}28 factor and that the sheathed flagellum is competent for secretion of nonstructural proteins.

* Corresponding author. Mailing address: Department of Biology, University of Texas San Antonio, 6900 N. Loop 1604 West, San Antonio, TX 78249-0662. Phone: (210) 458-6140. Fax: (210) 458-5658. E-mail: klose{at}utsa.edu.

Journal of Bacteriology, July 2004, p. 4613-4619, Vol. 186, No. 14
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.14.4613-4619.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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