The Role of Outer Membrane Proteins in the Survival of Neisseria gonorrhoeae P9 within Guinea-pig Subcutaneous Chambers

McBride, H.; Lambden, Paul R.; Heckels, John E.; Watt, P. J.

doi:10.1099/00221287-126-1-63

Cited by 17 publications

(10 citation statements)

References 13 publications

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“…We believe that all eight or nine P,ll genes are probably functional, despite the fact that our screening of colony variants revealed the existence of only six P,ll proteins (Barritt ef at., 1987), There may be multiple P,ll proteins not distinguishable by the criteria we used in screening. Alternatively, expression of some P.ll proteins may be favoured only under specific growth conditions, such as those found in vivo (McBride et at., 1981).…”

Section: Discussionmentioning

confidence: 99%

Recombination among Protein II genes of Neisseria gonorrhoeae generates new coding sequences and increases structural variability in the Protein II family

Connell

Black

Kawula

et al. 1988

Molecular Microbiology

111

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Expression of Neisseria gonorrhoeae Protein II (P.II) is subject to phase variation and antigenic variation. The P.II proteins made by one strain possess both unique and conserved antigenic determinants. To study the mechanism of antigenic variation, we cloned several P.II genes, using as probes a panel of monoclonal antibodies (MAbs) specific for unique determinants. The DNA sequences of three P.II genes showed that they shared a conserved framework, with two short hypervariable (HV) regions being responsible for most of the differences among them. We demonstrated that unique epitopes recognized by the MAbs were at least partially encoded by one of the HV regions. Moreover, we found that reassortment of the two HV regions among P.II genes occurs, generating increased structural and antigenic variability in the P.II protein family.

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Section: Discussionmentioning

confidence: 99%

Recombination among Protein II genes of Neisseria gonorrhoeae generates new coding sequences and increases structural variability in the Protein II family

Connell

Black

Kawula

et al. 1988

Molecular Microbiology

111

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“…The surface components of gonococci have been under vigorous investigation in attempts to expand our knowledge about the biology of this organism and to find potential vaccine antigens for gonorrhea. Most antigens studied to date exhibit extensive structural and antigenic variations, e.g., pili (10,19,22), protein I, the major outer membrane protein with porin function (15,31,35), the heat-modifiable proteins II, which are associated with colony opacity (5,13,40), and lipopolysaccharide (1). In contrast, protein III exhibits a conserved structure (16) yet induces blocking antibodies that interfere with the bactericidal effects of other specific antibodies (26).…”

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confidence: 99%

Cloning and DNA sequence of the omc gene encoding the outer membrane protein-macromolecular complex from Neisseria gonorrhoeae

1989

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The omc gene, encoding the outer membrane protein-macromolecular complex (OMP-MC), was cloned in two pieces from Neisseria gonorrhoeae 2686. The 5' fragment of the omc gene included a promoter sequence, as indicated by its unregulated expression in Escherichia coli. Attempts to reconstruct an intact omc gene were unsuccessful, suggesting that expression of the complete OMP-MC protein was toxic to E. coli. Complete sequence determination revealed a coding sequence of 2,133 nucleotides; the deduced amino acid sequence indicated a mature protein of 687 amino acids with an NH2-terminal signal peptide of 24 amino acids. Analysis of the deduced amino acid sequence revealed that the NH2-terminal half of OMP-MC is generally hydrophilic, while the COOH-terminal portion contains alternating hydrophobic and hydrophilic regions. Serological analyses demonstrated that the NH2-terminal portion of OMP-MC is exposed on the gonococcal surface and the COOH-terminal portion is membrane associated.

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“…Recent work has shown that even in a single strain surface antigens are capable of considerable variations in vitro (Swanson, 1978; and probably in vivo (James & Swanson, 1977;McBride et al, 1981). Colonial variants of the same strain have been shown to produce pili with altered morphology and subunit molecular weight (Penn et al, 1980;Salit et al, 1980), which show differences in their attachment to epithelial cells (Lambden et al, 1981 b).…”

Section: Introductionmentioning

confidence: 99%

Antigenic Variation of Outer Membrane Protein II in Colonial Variants of Neisseria gonorrhoeae P9

Diaz

Heckels

1982

Microbiology

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Antibodies were detected by an enzyme-linked immunosorbent assay (ELISA) in sera from rabbits immunized with outer membranes from colonial opacity variants of Neisseria gonorrhoeae P9. ELISA-inhibition experiments with purified antigens revealed approximately equal proportions of antibodies directed against each of the three major surface antigens, lipopolysaccharide, the major outer membrane protein (protein I) and protein 11, the variable protein associated with colonial opacity. Inhibition experiments with intact gonococci showed considerable surface antigenic diversity which could be correlated with differences between the protein I1 species present. Despite their considerable structural homology, different protein I1 species from colonial variants of the same strain showed little cross-reactivity with specific anti-protein I1 sera, thus demonstrating the considerable variation in that part of the antigen which is exposed on the surface of the gonococcus and is closely involved in pathogenic mechanisms.

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The Role of Outer Membrane Proteins in the Survival of Neisseria gonorrhoeae P9 within Guinea-pig Subcutaneous Chambers

Cited by 17 publications

References 13 publications

Recombination among Protein II genes of Neisseria gonorrhoeae generates new coding sequences and increases structural variability in the Protein II family

Recombination among Protein II genes of Neisseria gonorrhoeae generates new coding sequences and increases structural variability in the Protein II family

Cloning and DNA sequence of the omc gene encoding the outer membrane protein-macromolecular complex from Neisseria gonorrhoeae

Antigenic Variation of Outer Membrane Protein II in Colonial Variants of Neisseria gonorrhoeae P9

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