Neisseria PilC protein identified as type-4 pilus tip-located adhesin

Rudel, Thomas; Scheuerpflug, Ina; Meyer, Thomas F.

doi:10.1038/373357a0

Cited by 304 publications

(258 citation statements)

References 26 publications

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“…The cytoplasmic protein PilT is essential for retraction, but dispensable for pilus assembly (Wolfgang et al, 1998). The putative type IVpilus-associated adhesin PilC (Jönsson et al, 1994) is thought to act by binding to epithelial receptors suggested to be CD46- (Rudel et al, 1995) and C4B-binding protein (Winther-Larsen et al, 2001). PilC also plays a role in type IV pilus dynamics by acting as a mediator of pilus homeostasis, and promotes the processivity of organelle elongation in the presence of PilT.…”

Section: Introductionmentioning

confidence: 99%

Topology of the outer-membrane secretin PilQ from Neisseria meningitidis

et al. 2006

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Neisseria meningitidis is the causative agent of epidemic meningococcal meningitis and septicaemia. Type IV pili are surface organelles that mediate a variety of functions, including adhesion, twitching motility, and competence for DNA binding and uptake in transformation. The secretin PilQ is required for type IV pilus expression at the cell surface, and forms a dodecameric cage-like macromolecular complex in the meningococcal outer membrane. PilQ-null mutants are devoid of surface pili, and prevailing evidence suggests that the PilQ complex facilitates extrusion and retraction of type IV pili across the outer membrane. Defining the orientation of the meningococcal PilQ complex in the membrane is a prerequisite for understanding the structure-function relationships of this important protein in pilus biology. In order to begin to define the topology of the PilQ complex in the outer membrane, polyhistidine insertions in N-and C-terminal regions of PilQ were constructed, and their subcellular locations examined. Notably, the insertion epitopes at residues 205 and 678 were located within the periplasm, whereas residue 656 was exposed at the outer surface of the outer membrane. Using electron microscopy with Ni-NTA gold labelling, it was demonstrated that the insertion at residue 205 within the N-terminus mapped to a site on the arm-like features of the 3D structure of the PilQ multimer. Interestingly, mutation of the same region gave rise to an increase in vancomycin permeability through the PilQ complex. The results yield novel information on the PilQ N-terminal location and function in the periplasm, and reveal a complex organization of the membrane-spanning secretin in vivo.

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Section: Introductionmentioning

confidence: 99%

Topology of the outer-membrane secretin PilQ from Neisseria meningitidis

et al. 2006

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“…They also contribute to other phenotypes, including autoagglutination, competence for natural transformation, and twitching motility (6). Tfp-mediated gonococcal adherence appears not to be directly associated with the pilin subunit protein PilE but rather is most strongly correlated with the expression of the less abundant PilC protein, which copurifies with Tfp (7,8).…”

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confidence: 99%

Neisseria gonorrhoeae PilV, a type IV pilus-associated protein essential to human epithelial cell adherence

Winther‐Larsen

Hegge

Wolfgang

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

121

136

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Type IV pili (Tfp) of Neisseria gonorrhoeae, the Gram-negative etiologic agent of gonorrhea, facilitate colonization of the human host. Tfp are assumed to play a key role in the initial adherence to human epithelial cells by virtue of the associated adhesin protein PilC. To examine the structural and functional basis for adherence in more detail, we identified potential genes encoding polypeptides sharing structural similarities to PilE (the Tfp subunit) within the N. gonorrhoeae genome sequence database. We show here that a fiber subunit-like protein, termed PilV, is essential to organelle-associated adherence but dispensable for Tfp biogenesis and other pilus-related phenotypes, including autoagglutination, competence for natural transformation, and twitching motility. The adherence defect in pilV mutants cannot be attributed to reduced levels of piliation, defects in fiber anchoring to the bacterial cell surface, or to unstable pilus expression related to organelle retraction. PilV is expressed at low levels relative to PilE and copurifies with Tfp fibers in a PilC-dependent fashion. Purified Tfp from pilV mutants contain PilC adhesin at reduced levels. Taken together, these data support a model in which PilV functions in adherence by promoting the functional display of PilC in the context of the pilus fiber.

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“…Two other homologous proteins, PilC1 and PilC2, are also involved in pilus assembly and adhesion (Nassif et al, 1994;Rudel et al, 1995;Rahman et al, 1997).…”

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confidence: 99%

Down‐regulation of pili and capsule of Neisseria meningitidis upon contact with epithelial cells is mediated by CrgA regulatory protein

Deghmane¹,

Giorgini²,

Larribe³

et al. 2002

Molecular Microbiology

131

146

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SummaryThe initial attachment of Neisseria meningitidis to the target cell surface appears to be largely pilus dependent in capsulated bacteria. Intimate adhesion subsequently occurs to permit colonization. We recently reported that insertional inactivation of the crgA gene, which encodes a transcriptional regulator belonging to the LysR family, decreased meningococcal adhesion to epithelial cells and abolished intimate adhesion. In this report, we analyse expression of the pilE and sia genes, which are involved in the biosynthesis of pili and capsule respectively, during bacteria-host cell interactions. Western blotting, transcriptional fusion and reverse transcriptase polymerase chain reaction (RT-PCR) analysis showed that the expression of these genes was downregulated during intimate adhesion. DNA-binding assays, footprinting and RT-PCR analysis indicated that this downregulation was directly mediated by the CrgA protein. The pilE and sia promoters were found to have a CrgA binding motif in common. These results strongly suggest that N. meningitidis displays an adaptive response upon cell contact. CrgA may play a central regulatory role in meningococcal adhesion, particularly in switching from initial to intimate adhesion by downregulating the bacterial surface structures that hinder this adhesion.

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Neisseria PilC protein identified as type-4 pilus tip-located adhesin

Cited by 304 publications

References 26 publications

Topology of the outer-membrane secretin PilQ from Neisseria meningitidis

Topology of the outer-membrane secretin PilQ from Neisseria meningitidis

Neisseria gonorrhoeae PilV, a type IV pilus-associated protein essential to human epithelial cell adherence

Down‐regulation of pili and capsule of Neisseria meningitidis upon contact with epithelial cells is mediated by CrgA regulatory protein

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