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Journal of Bacteriology, July 2002, p. 3605-3613, Vol. 184, No. 13
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.13.3605-3613.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Differential Regulation of Twitching Motility and Elastase Production by Vfr in Pseudomonas aeruginosa

Scott A. Beatson,1,2,{dagger} Cynthia B. Whitchurch,1,{ddagger} Jennifer L. Sargent,1,{ddagger} Roger C. Levesque,3 and John S. Mattick1,2*

ARC Special Research Centre for Functional and Applied Genomics, Institute for Molecular Bioscience,1 Department of Biochemistry, University of Queensland, Brisbane, Queensland 4072, Australia,2 Health and Life Sciences Research Center, Université Laval, Quebec, Quebec, Canada3

Received 31 January 2002/ Accepted 11 April 2002

Vfr, a homolog of Escherichia coli cyclic AMP (cAMP) receptor protein, has been shown to regulate quorum sensing, exotoxin A production, and regA transcription in Pseudomonas aeruginosa. We identified a twitching motility-defective mutant that carries a transposon insertion in vfr and confirmed that vfr is required for twitching motility by construction of an independent allelic deletion-replacement mutant of vfr that exhibited the same phenotype, as well as by the restoration of normal twitching motility by complementation of these mutants with wild-type vfr. Vfr-null mutants exhibited severely reduced twitching motility with barely detectable levels of type IV pili, as well as loss of elastase production and altered pyocyanin production. We also identified reduced-twitching variants of quorum-sensing mutants (PAK lasI::Tc) with a spontaneous deletion in vfr (S. A. Beatson, C. B. Whitchurch, A. B. T. Semmler, and J. S. Mattick, J. Bacteriol., 184:3598-3604, 2002), the net result of which was the loss of five residues (EQERS) from the putative cAMP-binding pocket of Vfr. This allele (Vfr{Delta}EQERS) was capable of restoring elastase and pyocyanin production to wild-type levels in vfr-null mutants but not their defects in twitching motility. Furthermore, structural analysis of Vfr and Vfr{Delta}EQERS in relation to E. coli CRP suggests that Vfr is capable of binding both cAMP and cyclic GMP whereas Vfr{Delta}EQERS is only capable of responding to cAMP. We suggest that Vfr controls twitching motility and quorum sensing via independent pathways in response to these different signals, bound by the same cyclic nucleotide monophosphate-binding pocket.

* Corresponding author. Mailing address: Institute for Molecular Bioscience, University of Queensland, Brisbane, QLD 4072, Australia. Phone: 61-7-3365-4446. Fax: 61-7-3365-8813. E-mail: j.mattick{at}imb.uq.edu.au.

{dagger} Present address: Department of Human Anatomy and Genetics, University of Oxford, Oxford OX1 3QX, United Kingdom.

{ddagger} Present address: Department of Medicine, University of California San Francisco, San Francisco, CA 94143-0654.

Journal of Bacteriology, July 2002, p. 3605-3613, Vol. 184, No. 13
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.13.3605-3613.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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