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

FppA, a Novel Pseudomonas aeruginosa Prepilin Peptidase Involved in Assembly of Type IVb Pili

Sophie de Bentzmann, Marianne Aurouze, Geneviève Ball, and Alain Filloux^*

Laboratoire d'Ingénierie des Systèmes Macromoléculaires, CNRS-IBSM-UPR9027, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France

Received 10 March 2006/ Accepted 21 April 2006

Several subclasses of type IV pili have been described according to the characteristics of the structural prepilin subunit. Whereas molecular mechanisms of type IVa pilus assembly have been well documented for Pseudomonas aeruginosa and involve the PilD prepilin peptidase, no type IVb pili have been described in this microorganism. One subclass of type IVb prepilins has been identified as the Flp prepilin subfamily. Long and bundled Flp pili involved in tight adherence have been identified in Actinobacillus actinomycetemcomitans, for which assembly was due to a dedicated machinery encoded by the tad-rcp locus. A similar flp-tad-rcp locus containing flp, tad, and rcp gene homologues was identified in the P. aeruginosa genome. The function of these genes has been investigated, which revealed their involvement in the formation of extracellular Flp appendages. We also identified a gene (designated by open reading frame PA4295) outside the flp-tad-rcp locus, that we named fppA, encoding a novel prepilin peptidase. This is the second enzyme of this kind found in P. aeruginosa; however, it appears to be truncated and is similar to the C-terminal domain of the previously characterized PilD peptidase. In this study, we show that FppA is responsible for the maturation of the Flp prepilin and belongs to the aspartic acid protease family. We also demonstrate that FppA is required for the assembly of cell surface appendages that we called Flp pili. Finally, we observed an Flp-dependent bacterial aggregation process on the epithelial cell surface and an increased biofilm phenotype linked to Flp pilus assembly.

S.D. and M.A. contributed equally to this work.

This article has been cited by other articles:

• Boyd, J. M., Dacanay, A., Knickle, L. C., Touhami, A., Brown, L. L., Jericho, M. H., Johnson, S. C., Reith, M. (2008). Contribution of Type IV Pili to the Virulence of Aeromonas salmonicida subsp. salmonicida in Atlantic Salmon (Salmo salar L.). Infect. Immun. 76: 1445-1455 [Abstract] [Full Text]  
• Clock, S. A., Planet, P. J., Perez, B. A., Figurski, D. H. (2008). Outer Membrane Components of the Tad (Tight Adherence) Secreton of Aggregatibacter actinomycetemcomitans. J. Bacteriol. 190: 980-990 [Abstract] [Full Text]  
• Evans, K. J., Lambert, C., Sockett, R. E. (2007). Predation by Bdellovibrio bacteriovorus HD100 Requires Type IV Pili. J. Bacteriol. 189: 4850-4859 [Abstract] [Full Text]  
• Ruer, S., Stender, S., Filloux, A., de Bentzmann, S. (2007). Assembly of Fimbrial Structures in Pseudomonas aeruginosa: Functionality and Specificity of Chaperone-Usher Machineries. J. Bacteriol. 189: 3547-3555 [Abstract] [Full Text]  
• Szabo, Z., Stahl, A. O., Albers, S.-V., Kissinger, J. C., Driessen, A. J. M., Pohlschroder, M. (2007). Identification of Diverse Archaeal Proteins with Class III Signal Peptides Cleaved by Distinct Archaeal Prepilin Peptidases. J. Bacteriol. 189: 772-778 [Abstract] [Full Text]  
• Tomich, M., Fine, D. H., Figurski, D. H. (2006). The TadV Protein of Actinobacillus actinomycetemcomitans Is a Novel Aspartic Acid Prepilin Peptidase Required for Maturation of the Flp1 Pilin and TadE and TadF Pseudopilins.. J. Bacteriol. 188: 6899-6914 [Abstract] [Full Text]