28 Factor That Is Secreted through the Sheathed Polar Flagellum
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
54- and
28-dependent transcription. In other bacteria,
28 transcriptional activity is controlled by an anti-
28 factor, FlgM. We demonstrate that the V. cholerae FlgM homologue (i) physically interacts with
28, (ii) has a repressive effect on some V. cholerae
28-dependent flagellar promoters, and (iii) is secreted through the polar sheathed flagellum, consistent with anti-
28 activity. Interestingly, FlgM does not have a uniform repressive effect on all
28-dependent promoters, as determined by measurement of
28-dependent transcription in cells either lacking FlgM (
flgM) or incapable of secretion (
fliF). Further analysis of a
fliF strain revealed that this flagellar assembly block causes a decrease in class III (FlrC- and
54-dependent) and class IV (
28-dependent), but not class II (FlrA- and
54-dependent), flagellar transcription. V. cholerae flgM and fliA (encodes
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-
28 factor and that the sheathed flagellum is competent for secretion of nonstructural proteins.
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