Variations in Surface Protein Composition Associated with Virulence Properties in Opacity Types of Neisseria gonorrhoeae

Lambden, Paul R.; Heckels, John E.; James, Ligimol; Watt, P. J.

doi:10.1099/00221287-114-2-305

Cited by 222 publications

(142 citation statements)

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“…Neisseria gonorrhoeae P9 variants were grown on clear typing medium as previously described (Lambden et al, 1979). Colonies of P9-2 (u pili) and P9-20 Vpili) (Lambden et al, 1980) were picked, purified by repeated single colony isolation and stored in liquid nitrogen.…”

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confidence: 99%

The Preparation and Properties of and Pili from Variants of Neisseria gonorrhoeae P9

1981

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The a and p type pili produced by variants of Neisseria gonorrhoeae P9 were isolated and characterized. The two types of pili showed clear differences in morphology, buoyant density (a, 1.292 g ml-l; p, 1.282 g ml-I) and isoelectric point (a, PI 5.2; p, PI 4.3). Amino acid analysis of a and / 3 pili showed that their overall composition was similar with the exception that p pili had a higher content of glutamate and alanine residues. A high degree of structural homology was seen in two-dimensional peptide maps of tryptic hydrolysates of a and /? pili.The molecular differences between a and p pili were reflected in their antigenic activity and in their ability to attach to human cells. The binding of a pili to buccal epithelial cells was pH dependent with a maximum binding of 49% at pH 6.5, whereas the attachment of p pili showed no pH optimum. The binding of pili to erythrocytes differed from binding to buccal epithelial cells in that attachment of both pili was identical with no pH optimum. Data from attachment of pili to human cells suggest that erythrocytes lack receptors for binding gonococcal pili.

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confidence: 99%

The Preparation and Properties of and Pili from Variants of Neisseria gonorrhoeae P9

1981

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“…Rather, it must reflect either the preferred expression or the enhanced survival of variants that express a protein II other than PIIa. Relatively little is known about either the comparative survival abilities of different PII variants in vitro (12) or their differential expression of their P.II repertoire. Although all protein II genes are switched on-off by gain or loss of pentameric repeats in its leader peptide-encoding portion (26,27), different P.II genes switch on-off at very different frequencies among cells in a given strain (19, 32, Swanson, J ., unpublished results) .…”

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“…Protein II' in vitro exhibit striking aggregation, and this might enhance colonization in vivo if it promotes the retention of newly multiplied organisms at infected mucosal loci . In addition, several studies have demonstrated heightened attachment of protein II+ gonococci to eukaryotic cells in vitro (12)(13)(14)(15). One report suggests that, after their attachment to HeLa cells, some P.II+ variants are detached more readily than others (15) .…”

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“…These observations say that protein II expression relates to gonococcal pathogenicity, but they do not tell how. Certain protein II species promote attachment o£ gonococci to tissue culture cells (5,(12)(13)(14) . Colonization of HeLa cells by gonococci is also enhanced by the diminished detachment that is displayed by organisms that express particular protein II species (15).…”

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Expression of outer membrane protein II by gonococci in experimental gonorrhea.

Swanson

Barrera

Sola

et al. 1988

The Journal of Experimental Medicine

150

132

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Neisseria gonorrhoeae infects mucosae ofhumans whose urogenital epithelia are most commonly involved . The infectious aptitudes of these bacteria are likely dictated by their surface components which, except for pili, have poorly defined roles in pathogenesis. Pilus * gonococci infect the human male urethra, whereas pilus -variants do not (1, 2, Boslego, J., J. M. Koomey, and J. Swanson, unpublished results) . Pilus expression promotes adherence ofgonococci to human cells in vitro (3-6), and analogous, pilus-mediated adherence in vivo to mucosal epithelium likely accounts for correlation between pilus' phenotype of gonococci and their virulence.Expression of outer membrane protein II by gonococci markedly influences their surface properties, as deduced from the colonial opacity and intercellular adherence differences of protein II -vs. protein II' organisms (7); however, the pathogenic relevance of protein II production is not understood. Variants within a given strain synthesize several distinct protein II moieties . Expression of protein II moieties is variable for gonococci in vivo among different individuals or in separate sites of an individual (8-11) . Protein II' gonococci are isolated regularly from a male's urethra and frequently from the cervix of an infected female, depending on menstrual timing, use of oral contraceptives, etc. (8, 10). But protein II -organisms populate an infected female's fallopian tubes, regardless of which protein II phenotypes reside in her cervix (11). These observations say that protein II expression relates to gonococcal pathogenicity, but they do not tell how. Certain protein II species promote attachment o£ gonococci to tissue culture cells (5,(12)(13)(14) . Colonization of HeLa cells by gonococci is also enhanced by the diminished detachment that is displayed by organisms that express particular protein II species (15). Interactions between gonococci and peripheral blood neutrophils in vitro are also influenced by elaboration of certain protein II species (16-18).The protein II repertoire expressed by a given strain consists of several structurally related polypeptides whose common and unique portions are membrane buried and surface exposed, respectively (19)(20)(21)(22)(23)(24)(25). This repertoire is encoded by a multi-J . Sola was sponsored by the National Institutes of Health summer student program . Address correspondence to

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“…Gonococci expressing PII proteins are generally isolated from infections localized to the surface mucosa, whereas organisms recovered from disseminated infections often lack PII proteins (6,7). The possession of certain PII proteins has been associated with resistance to antibiotics and steroid hormones (12,19), altered-serum resistance (8,12), increased sensitivity to serum proteases (2), and increased adherence to buccal epithelial cells (12) and phagocytic cells (18).…”

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Genetic transformation of genes for protein II in Neisseria gonorrhoeae

Schwalbe¹,

Cannon²

1986

J Bacteriol

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The protein II (PII) outer membrane proteins of Neisseria gonorrhoeae are a family of heat-modifiable proteins that are subject to phase variation, in which the synthesis of different PI' species is turned on The PII proteins of the gonococcus are a family 'of heat-modifiable outer membrane proteins with apparent molecular masses ranging from 24,000'to 30,000 daltons (28). They were initially described as proteins present in the outer membrane of dark-colored (opaque) colony variants and absent in light (transparent) variants of the same strain (28, 30). The gonococcus reversibly oscillates between on and off states of expression of PII proteins in a type of phase variation (11,29). The proteins are apparently not crucial to viability, since in all strains studied there are colony variants that do not express PII proteins.'PII proteins also demonstrate antigenic variation, whereby the synthesis of antigenically different PII proteins of a strain is turned on and off. At least seven distinct'PII species have been described in one gonococcal strain, and an organism can express from zero to at least three PII proteins at one time (22). Gonococci expressing PII proteins are generally isolated from infections localized to the surface mucosa, whereas organisms recovered from disseminated infections often lack PII proteins (6, 7). The possession of certain PII proteins has been associated with resistance to antibiotics and steroid hormones (12, 19), altered-serum resistance (8, 12), increased sensitivity to serum proteases (2), and increased adherence to buccal epithelial cells (12) and phagocytic cells (18).Little is known about the genes for PII proteins or about the mechanisms that regulate PII protein expression. Within a gonococcal population, variants that differ in PII protein profiles (detected by differences in colony opacity) occur at a frequency of approximately 10-3 per cell per generation (16). Switching of 'PII proteins occurs in a nonrandom sequence (1,29). Studies with cloned genes for PII proteins showed that there are multiple' copies of PII-related se-* Corresponding author. quences in the gonococcal chromosome and that structural alterations in DNA accomnpany changes in PIT protein expression (26, 27).Studies on the physical characterization of PIT genes would be complemented by studies on the genetics of PII proteins in the gonococcus itself. However, since the presence of PII proteins does not confer a selectable phenotype on the gonococcus, it has been difficult to apply traditional genetic approaches to the study of PII genes. We have done experiments involving the genetic transformation of PII genes in which transformants expressing a donor-specific PII protein were detected with monoclonal antibodies (MAb) specific for the PII proteins of the donor. This approach has allowed us to investigate the linkage relationships of genes for PII proteins and to determine that the state of expression of a donor PH gene affects the outcome of genetic transformation experiments. We also report that varian...

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Variations in Surface Protein Composition Associated with Virulence Properties in Opacity Types of Neisseria gonorrhoeae

Cited by 222 publications

References 7 publications

The Preparation and Properties of and Pili from Variants of Neisseria gonorrhoeae P9

The Preparation and Properties of and Pili from Variants of Neisseria gonorrhoeae P9

Expression of outer membrane protein II by gonococci in experimental gonorrhea.

Genetic transformation of genes for protein II in Neisseria gonorrhoeae

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