Gene conversion involving the pilin structural gene correlates with pilus+ ⇄ pilus− changes in Neisseria gonorrhoeae

Swanson, John; Bergström, Sven; Robbins, Kenneth E.; Barrera, O; Corwin, Dan; Koomey, Michael

doi:10.1016/0092-8674(86)90449-6

Cited by 178 publications

(161 citation statements)

References 13 publications

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“…Pilus phase variation in N. gonorrhoeae can result from recombination between pilS loci and the pilE locus, producing defective pilin gene products. Such defective pilins are immunologically reactive, but are not assembled into pili, giving rise to a non-piliated phenotype (Bergstrom et ul., 1986;Haas et al, 1987;Swanson et al, 1986). Such non-piliated gonococcal variants can readily revert to the piliated phenotype.…”

Section: Discussionmentioning

confidence: 99%

Identification of Epitopes Recognized by Monoclonal Antibodies SM1 and SM2 Which React with All Pili of Neisseria gonorrhoeae but Which Differentiate between Two Structural Classes of Pili Expressed by Neisseria meningitidis and the Distribution of Their Encoding Sequences in the Genomes of Neisseria spp.

Virji

Heckels²,

Potts³

et al. 1989

Microbiology

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The pili expressed by all isolates of Neisseria gonorrhoeae react with two monoclonal antibodies, SM1 and SM2. In contrast, although many isolates of Neisseria meningitidis also express pili (class I) which react with antibodies SM1 and SM2, a proportion express pili (class 11) which fail to react. In order to define the epitopes recognized by these antibodies, a series of overlapping peptides corresponding to the amino acid sequence of conserved regions of gonococcal pili have been synthesized. The minimum epitope recognized by antibody SM1 was found to comprise a linear peptide EYYLN, corresponding to residues 49-53 of mature pilin. In contrast, antibody SM2 reacted with a number of peptides from around the cysteine residue (Cys 1) at position 120, suggesting that an extended region may contribute to a conformational epitope recognized by this antibody in the native protein. The identification of the two epitopes defines structural differences between the classes of pili expessed by meningococci. In order to determine the distribution of pilin gene sequences in Neisseria we used as hybridization probes an oligonucleotide (PS 1) with the sequence 5'-GAGTATTACCTGAATCA-3' which spans the coding region for the SMl epitope, and a fragment of the 3' end of the gonococcal pilE gene which contains conserved sequences flanking the two Cys codons and encodes the SM2 epitope. All strains of N . gonorrhoeae and N. meningitidis tested, regardless of piliation phenotype, harboured DNA sequences homologous to those encoding the carboxy-terminus of meningococcal class I pilin. Furthermore, all gonococci and all meningocococci producing class I pili hybridized with oligonucleotide probe PS 1. Non-reverting non-piliated derivatives of previously class I pilus-producing strains showed reduced hybridization signals with this probe, but nevertheless retained sequences homologous to the coding sequence for the SMl epitope. However, meningococci producing class I1 pili could be divided into two groups on the basis of their reaction with the PS1 probe: half the strains tested failed to react, which is consistent with our previous analysis of silent class I pilin sequences; the remainder reacted (relatively weakly) with the probe, suggesting that the silentpil sequences in these strains extend further towards the 5' end of the pilin gene than in strains studied previously. Some strains of Neisseria lactarnica reacted weakly with both types of probe but failed to produce SM1-reactive pili. In contrast,

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Section: Discussionmentioning

confidence: 99%

Identification of Epitopes Recognized by Monoclonal Antibodies SM1 and SM2 Which React with All Pili of Neisseria gonorrhoeae but Which Differentiate between Two Structural Classes of Pili Expressed by Neisseria meningitidis and the Distribution of Their Encoding Sequences in the Genomes of Neisseria spp.

Virji

Heckels²,

Potts³

et al. 1989

Microbiology

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“…Bacterial strains and growth conditions N. gonorrhoeae MS11 mk (P þ ) and MS11 mk (P ¹ n) (Swanson et al, 1986) were obtained from Dr M. Koomey. The MS11 mk (P þ ) strain sample used in our studies is designated MS11 mk (P þ )-u. Piliated and non-piliated variants were distinguished by colony morphology under a binocular microscope.…”

Section: Methodsmentioning

confidence: 99%

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

Källström

Liszewski

Atkinson

et al. 1997

Molecular Microbiology

326

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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“…gonorrhoeae MS11 (Pϩ) and MS11 (P-n) were gifts from M. Koomey (33). Piliated and nonpiliated variants were distinguished by colony morphology under a binocular microscope.…”

Section: Bacterial Strains and Growth Conditionsmentioning

confidence: 99%

A Novel Interaction Between Type IV Pili ofNeisseria gonorrhoeaeand the Human Complement Regulator C4b-Binding Protein

Blom

Rytkönen

Vásquez

et al. 2001

The Journal of Immunology

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C4b-binding protein (C4BP) is an important plasma inhibitor of the classical pathway of complement activation. Several bacterial pathogens bind C4BP, which may contribute to their virulence. In the present report we demonstrate that isolated type IV pili from Neisseria gonorrhoeae bind human C4BP in a dose-dependent and saturable manner. C4BP consists of seven identical α-chains and one β-chain linked together with disulfide bridges. We found that pili bind to the α-chain of C4BP, which is composed of eight homologous complement control protein (CCP) domains. From the results of an inhibition assay with C4b and a competition assay in which we tested mutants of C4BP lacking individual CCPs, we concluded that the binding area for pili is localized to CCP1 and CCP2 of the α-chain. The binding between pili and C4BP was abolished at 0.25 M NaCl, implying that it is based mostly on ionic interactions, similarly to what have been observed for C4b-C4BP binding. Furthermore, the N-terminal part of PilC, a structural component of pili, appeared to be responsible for binding of C4BP. Membrane cofactor protein, previously shown to be a receptor for pathogenic N. gonorrhoeae on the surface of epithelial cells, competed with C4BP for binding to pili only at high concentrations, suggesting that different parts of pili are involved in these two interactions. Accordingly, high concentrations of C4BP were required to inhibit binding of N. gonorrhoeae to Chang conjunctiva cells, and no inhibition of binding was observed with cervical epithelial cells.

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Gene conversion involving the pilin structural gene correlates with pilus+ ⇄ pilus− changes in Neisseria gonorrhoeae

Cited by 178 publications

References 13 publications

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

A Novel Interaction Between Type IV Pili ofNeisseria gonorrhoeaeand the Human Complement Regulator C4b-Binding Protein

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