This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Chiang, S. L.
Right arrow Articles by Mekalanos, J. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chiang, S. L.
Right arrow Articles by Mekalanos, J. J.

 Previous Article  |  Next Article 

Infection and Immunity, February 1999, p. 976-980, Vol. 67, No. 2
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

rfb Mutations in Vibrio cholerae Do Not Affect Surface Production of Toxin-Coregulated Pili but Still Inhibit Intestinal Colonization

Su L. Chiang, and John J. Mekalanos*

Department of Microbiology and Molecular Genetics and Shipley Institute of Medicine, Harvard Medical School, Boston, Massachusetts 02115

Received 24 August 1998/Returned for modification 27 October 1998/Accepted 9 November 1998

The toxin-coregulated pilus (TCP) of Vibrio cholerae is essential for colonization. It was recently reported that rfb mutations in V. cholerae 569B cause the translocation arrest of the structural subunit of TCP, raising the possibility that the colonization defects of lipopolysaccharide mutants are due to effects on TCP biogenesis. However, an rfbB gene disruption in either V. cholerae O395 or 569B has no apparent effect on surface TCP production as assessed by immunoelectron microscopy and CTX phage transduction, and an rfbD::Tn5lac mutant of O395 also shows no defect in TCP expression. We conclude that the colonization defect associated with rfb mutations is unrelated to defects in TCP assembly.

* Corresponding author. Mailing address: Department of Microbiology and Molecular Genetics and Shipley Institute of Medicine, Harvard Medical School, 200 Longwood Ave., Boston, MA 02115. Phone: (617) 432-0767. Fax: (617) 738-7664. E-mail: jmekalan{at}warren.med.harvard.edu.

Infection and Immunity, February 1999, p. 976-980, Vol. 67, No. 2
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Schild, S., Nelson, E. J., Camilli, A. (2008). Immunization with Vibrio cholerae Outer Membrane Vesicles Induces Protective Immunity in Mice. Infect. Immun. 76: 4554-4563 [Abstract] [Full Text]  
  • Ho, T. D., Waldor, M. K. (2007). Enterohemorrhagic Escherichia coli O157:H7 gal Mutants Are Sensitive to Bacteriophage P1 and Defective in Intestinal Colonization. Infect. Immun. 75: 1661-1666 [Abstract] [Full Text]  
  • Schild, S., Lamprecht, A.-K., Reidl, J. (2005). Molecular and Functional Characterization of O Antigen Transfer in Vibrio cholerae. J. Biol. Chem. 280: 25936-25947 [Abstract] [Full Text]  
  • Brown, I. I., Häse, C. C. (2001). Flagellum-Independent Surface Migration of Vibrio cholerae and Escherichia coli. J. Bacteriol. 183: 3784-3790 [Abstract] [Full Text]  
  • Nesper, J., Lauriano, C. M., Klose, K. E., Kapfhammer, D., Krai{beta}, A., Reidl, J. (2001). Characterization of Vibrio cholerae O1 El Tor galU and galE Mutants: Influence on Lipopolysaccharide Structure, Colonization, and Biofilm Formation. Infect. Immun. 69: 435-445 [Abstract] [Full Text]  
  • Nesper, J., Kapfhammer, D., Klose, K. E., Merkert, H., Reidl, J. (2000). Characterization of Vibrio cholerae O1 Antigen as the Bacteriophage K139 Receptor and Identification of IS1004 Insertions Aborting O1 Antigen Biosynthesis. J. Bacteriol. 182: 5097-5104 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»