Pseudomonas aeruginosa Type IV Pilus Expression in Neisseria gonorrhoeae : Effects of Pilin Subunit Composition on Function and Organelle Dynamics
- 15 September 2007
- journal article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 189 (18) , 6676-6685
- https://doi.org/10.1128/jb.00407-07
Abstract
Type IV pili (TFP) play central roles in the expression of many phenotypes including motility, multicellular behavior, sensitivity to bacteriophages, natural genetic transformation, and adherence. In Neisseria gonorrhoeae, these properties require ancillary proteins that act in conjunction with TFP expression and influence organelle dynamics. Here, the intrinsic contributions of the pilin protein itself to TFP dynamics and associated phenotypes were examined by expressing the Pseudomonas aeruginosa PilA(PAK) pilin subunit in N. gonorrhoeae. We show here that, although PilA(PAK) pilin can be readily assembled into TFP in this background, steady-state levels of purifiable fibers are dramatically reduced relative those of endogenous pili. This defect is due to aberrant TFP dynamics as it is suppressed in the absence of the PilT pilus retraction ATPase. Functionally, PilA(PAK) pilin complements gonococcal adherence for human epithelial cells but only in a pilT background, and this property remains dependent on the coexpression of both the PilC adhesin and the PilV pilin-like protein. Since P. aeruginosa pilin only moderately supports neisserial sequence-specific transformation despite its assembly proficiency, these results together suggest that PilA(PAK) pilin functions suboptimally in this environment. This appears to be due to diminished compatibility with resident proteins essential for TFP function and dynamics. Despite this, PilA(PAK) pili support retractile force generation in this background equivalent to that reported for endogenous pili. Furthermore, PilA(PAK) pili are both necessary and sufficient for bacteriophage PO4 binding, although the strain remains phage resistant. Together, these findings have significant implications for TFP biology in both N. gonorrhoeae and P. aeruginosa.Keywords
This publication has 53 references indexed in Scilit:
- Substitutions in the N‐terminal alpha helical spine of Neisseria gonorrhoeae pilin affect Type IV pilus assembly, dynamics and associated functionsMolecular Microbiology, 2006
- Laboratory and clinical Pseudomonas aeruginosa strains do not bind glycosphingolipids in vitro or during type IV pili-mediated initial host cell attachmentMicrobiology, 2006
- A conserved set of pilin‐like molecules controls type IV pilus dynamics and organelle‐associated functions in Neisseria gonorrhoeaeMolecular Microbiology, 2005
- Low-Level Pilin Expression Allows for Substantial DNA Transformation Competence in Neisseria gonorrhoeaeInfection and Immunity, 2003
- Type II Protein Secretion in Pseudomonas aeruginosa : the Pseudopilus Is a Multifibrillar and Adhesive StructureJournal of Bacteriology, 2003
- The product of the pilQ gene is essential for the biogenesis of type IV pili in Neisseria gonorrhoeaeMolecular Microbiology, 1995
- Characterization of the pilF—pilD pilus‐assembly locus of Neisseria gonorrhoeaeMolecular Microbiology, 1995
- Identification and characterization of pilG, a highly conserved pilus‐assembly gene in pathogenic NeisseriaMolecular Microbiology, 1995
- Mapping the surface regions of Pseudomonas aeruginosa PAK pilin: the importance of the C‐terminal region for adherence to human buccal epithelial cellsMolecular Microbiology, 1989
- Stimulation of pilus formation in Pseudomonas aeruginosa by RNA baceeriophage adsorptionBiochemical and Biophysical Research Communications, 1972