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Journal of Bacteriology, September 2009, p. 5669-5679, Vol. 191, No. 18
0021-9193/09/$08.00+0     doi:10.1128/JB.00632-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Characterization of Two Outer Membrane Proteins, FlgO and FlgP, That Influence Vibrio cholerae Motility{triangledown}

Raquel M. Martinez, Madushini N. Dharmasena, Thomas J. Kirn, and Ronald K. Taylor*

Department of Microbiology and Immunology, Dartmouth Medical School, Hanover, New Hampshire 03755

Received 13 May 2009/ Accepted 6 July 2009

Vibrio cholerae is highly motile by the action of a single polar flagellum. The loss of motility reduces the infectivity of V. cholerae, demonstrating that motility is an important virulence factor. FlrC is the sigma-54-dependent positive regulator of flagellar genes. Recently, the genes VC2206 (flgP) and VC2207 (flgO) were identified as being regulated by FlrC via a microarray analysis of an flrC mutant (D. C. Morris, F. Peng, J. R. Barker, and K. E. Klose, J. Bacteriol. 190:231-239, 2008). FlgP is reported to be an outer membrane lipoprotein required for motility that functions as a colonization factor. The study reported here focuses on the characterization of flgO, the first gene in the flgOP operon. We show that FlgO and FlgP are important for motility, as strains with mutations in the flgOP genes have reduced motility phenotypes. The flgO and flgP mutant populations display fewer motile cells as well as reduced numbers of flagellated cells. The flagella produced by the flgO and flgP mutant strains are shorter in length than the wild-type flagella, which can be restored by inhibiting rotation of the flagellum. FlgO is an outer membrane protein that localizes throughout the membrane and not at the flagellar pole. Although FlgO and FlgP do not specifically localize to the flagellum, they are required for flagellar stability. Due to the nature of these motility defects, we established that the flagellum is not sufficient for adherence; rather, motility is the essential factor required for attachment and thus colonization by V. cholerae O1 of the classical biotype. This study reveals a novel mechanism for which the outer membrane proteins FlgO and FlgP function in motility to mediate flagellar stability and influence attachment and colonization.

* Corresponding author. Mailing address: Dartmouth Medical School, Department of Microbiology and Immunology, HB7550, Hanover, NH 03755. Phone: (603) 650-1632. Fax: (603) 650-1318. E-mail: ronald.k.taylor{at}dartmouth.edu

{triangledown} Published ahead of print on 10 July 2009.

Journal of Bacteriology, September 2009, p. 5669-5679, Vol. 191, No. 18
0021-9193/09/$08.00+0     doi:10.1128/JB.00632-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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