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Journal of Bacteriology, November 2006, p. 7531-7541, Vol. 188, No. 21
0021-9193/06/$08.00+0     doi:10.1128/JB.00263-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Helicobacter pylori FlhB Function: the FlhB C-Terminal Homologue HP1575 Acts as a "Spare Part" To Permit Flagellar Export When the HP0770 FlhBCC Domain Is Deleted{dagger}

Matthew E. Wand,1,{ddagger} R. Elizabeth Sockett,2 Katy J. Evans,2 Neil Doherty,1 Paul M. Sharp,2 Kim R. Hardie,3 and Klaus Winzer3*

Institute of Infection, Immunity and Inflammation, Queen's Medical Centre, Nottingham, NG7 2UH, United Kingdom,1 Institute of Genetics, School of Biology, Medical School, University of Nottingham, Queen's Medical Centre, Nottingham, NG7 2UH, United Kingdom,2 Institute of Infection, Immunity and Inflammation, Centre for Biomolecular Sciences, University Park, University of Nottingham, Nottingham NG7 2RD, United Kingdom3

Received 20 February 2006/ Accepted 1 August 2006

In Helicobacter pylori 26695, a gene annotated HP1575 encodes a putative protein of unknown function which shows significant similarity to part of the C-terminal domain of the flagellar export protein FlhB. In Salmonella enterica, this part (FlhBCC) is proteolytically cleaved from the full-length FlhB, a processing event that is required for flagellar protein export and, thus, motility. The role of FlhB (HP0770) and its C-terminal homologue HP1575 was studied in H. pylori using a range of nonpolar deletion mutants defective in HP1575, HP0770, and the CC domain of HP0770 (HP0770CC). Deletion of HP0770 abolished swimming motility, whereas mutants carrying a deletion of either HP1575 or HP0770CC retained their ability to swim. An H. pylori strain containing deletions in both HP1575 and HP0770CC was nonmotile and did not produce flagella, suggesting that at least one of the two proteins had to be present for flagellar assembly to occur. Indeed, motility was restored when HP1575 was reintroduced into this strain immediately downstream of, but not fused to, the truncated HP0770 gene. Thus, HP1575 can functionally replace HP0770CC in this background. Like FlhB in S. enterica, HP0770 appeared to be proteolytically processed at a conserved NPTH processing site. However, mutation of the proline contained within the NPTH site of HP0770 did not affect motility and flagellar assembly, although it clearly interfered with processing when the protein was heterologously produced in Escherichia coli.

* Corresponding author. Mailing address: Institute of Infection, Immunity, and Inflammation, University of Nottingham, Centre for Biomolecular Sciences, Nottingham, NG7 2RD, United Kingdom. Phone: 44 115 84 67954. Fax: 44 115 84 67951. E-mail: Klaus.Winzer{at}nottingham.ac.uk.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.

{ddagger} Present address: Peter Medawar Building for Pathogen Research, University of Oxford, South Parks Road, Oxford, OX1 3SY, United Kingdom.

Journal of Bacteriology, November 2006, p. 7531-7541, Vol. 188, No. 21
0021-9193/06/$08.00+0     doi:10.1128/JB.00263-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Douillard, F. P., Ryan, K. A., Hinds, J., O'Toole, P. W. (2009). Effect of FliK mutation on the transcriptional activity of the {sigma}54 sigma factor RpoN in Helicobacter pylori. Microbiology 155: 1901-1911 [Abstract] [Full Text]  
  • Smith, T. G., Pereira, L., Hoover, T. R. (2009). Helicobacter pylori FlhB processing-deficient variants affect flagellar assembly but not flagellar gene expression. Microbiology 155: 1170-1180 [Abstract] [Full Text]  


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