Roles of pilin and PilC in adhesion of Neisseria meningitidis to human epithelial and endothelial cells.

Nassif, Xavier; Béretti, Jean-Luc; Lowy, Jonathan; Stenberg, Paula E.; Ó’Gaora, Peadar; Pfeifer, John D.; Normark, Staffan; So, Magdalene

doi:10.1073/pnas.91.9.3769

Cited by 199 publications

(232 citation statements)

References 19 publications

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“…However the fact that copurification of PilV is reliant on PilC, which is a known fiber-associated protein, strongly suggests that PilC, PilV, and Tfp interact with one another and that PilV pilus association is not merely due to leakage from the cells and nonspecific association. Additionally, it has been found in N. meningitidis that one isoform of PilC (PilC2) is associated with a piliated, nonadherent phenotype (29). Because we have shown that PilC is necessary for the association of PilV with Tfp, we speculate that the lack of adherence imparted by that pilC allele may result from reduced levels of pilus-associated PilV.…”

Section: Pilc and Pilv Content In Pilus Preparations From Adherence-dmentioning

confidence: 87%

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.

120

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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Section: Pilc and Pilv Content In Pilus Preparations From Adherence-dmentioning

confidence: 87%

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.

120

136

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“…Previous studies have shown that non-piliated Mc mutants are dramatically reduced in competence for natural transformation (Nassif et al, 1994;Tønjum et al, 1995). Considering that natural competence for transformation is a highly sensitive marker for pilus expression, we examined the relative competence of Mc strain 44/76-A and its isogenic PilQ mutant derivatives.…”

Section: Characterization Of MC Pilq Transposon Mutantsmentioning

confidence: 99%

Structure and function of repetitive sequence elements associated with a highly polymorphic domain of the Neisseria meningitidis PilQ protein

Tønjum

Caugant²,

Dunham

et al. 1998

Molecular Microbiology

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“…There are two copies of pilC, pilC1 and pilC2, in most strains. In N. gonorrhoeae strain MS11, piliated bacteria that express either PilC1 or PilC2 both adhere to target cells (Jonsson et al, 1994;Rudel et al, 1995b), whereas in N. meningitidis 8013 piliated pilC1 mutants, expressing only PilC2, do not bind to host cells (Nassif et al, 1994).…”

Section: Introductionmentioning

confidence: 99%

Membrane cofactor protein (MCP or CD46) is a cellular pilus receptor for pathogenic Neisseria

Källström

Liszewski

Atkinson

et al. 1997

Molecular Microbiology

325

230

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SummaryPili of Neisseria gonorrhoeae and Neisseria meningitidis mediate binding of the bacteria to human cellsurface receptors. We found that purified pili bound to a 55-to 60-kDa doublet band on SDS-PAGE of separated human epithelial cell extracts. This is a migration pattern typical of membrane cofactor protein (MCP or CD46). MCP is a widely distributed human complement regulatory protein. Attachment of the bacteria to epithelial cells was blocked by polyclonal and monoclonal antibodies directed against MCP, suggesting that this complement regulator is a receptor for piliated Neisseria. We proved this hypothesis by demonstrating that piliated, but not non-piliated, gonococci bound to CHO cells transfected with human MCP-cDNA. We also demonstrated a direct interaction between purified recombinant MCP and piliated Neisseria. Finally, recombinant MCP protein produced in E. coli inhibited attachment of the bacteria to target cells. Taken together, our data show that MCP is a human cell-surface receptor for piliated pathogenic Neisseria.

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Roles of pilin and PilC in adhesion of Neisseria meningitidis to human epithelial and endothelial cells.

Abstract: Pili and piln antigenic variation play important roles in adhesion ofNeisseria mexiRgiidji (MC)

Cited by 199 publications

References 19 publications

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

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

Structure and function of repetitive sequence elements associated with a highly polymorphic domain of the Neisseria meningitidis PilQ protein

Membrane cofactor protein (MCP or CD46) is a cellular pilus receptor for pathogenic Neisseria

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