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. 1983 Nov 1;158(5):1459–1472. doi: 10.1084/jem.158.5.1459

Gonococcal pilus subunit size heterogeneity correlates with transitions in colony piliation phenotype, not with changes in colony opacity

PMCID: PMC2187137  PMID: 6138388

Abstract

The apparent subunit sizes for pili of gonococci (Gc) have been visualized by using either Iodogen 125I-labeled whole Gc or immunoblotting with antipilus antiserum. These methods permitted definition of pilus subunit sizes for Gc of a given strain that had undergone changes either in piliation phenotype or in colonial opacity/protein II phenotype. The results indicate that pilus subunit size does not change coincident with changes in colony opacity/protein II phenotypes; but change in pilus subunit size is seen after a change in piliation phenotype (P+ leads to P++, and vice versa). Marked diversity in pilus subunit sizes is found for Gc of individual strains when P+ derivatives of P- colonies are compared. This diversity extends to pilus subunits of Gc found in single colonies; two distinct pilus forms were demonstrated for Gc residing in several single colonies. These findings show that Gc of a given strain are able to express any of a number of different pilus subunit size forms.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Apicella M. A. Serogrouping of Neisseria gonorrhoeae: identification of four immunologically distinct acidic polysaccharides. J Infect Dis. 1976 Oct;134(4):377–383. doi: 10.1093/infdis/134.4.377. [DOI] [PubMed] [Google Scholar]
  2. Buchanan T. M. Antigenic heterogeneity of gonococcal pili. J Exp Med. 1975 Jun 1;141(6):1470–1475. doi: 10.1084/jem.141.6.1470. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Duckworth M., Jackson D., Zak K., Heckels J. E. Structural variations in pili expressed during gonococcal infection. J Gen Microbiol. 1983 May;129(5):1593–1596. doi: 10.1099/00221287-129-5-1593. [DOI] [PubMed] [Google Scholar]
  4. Judd R. C. 125I-peptide mapping of protein III isolated from four strains of Neisseria gonorrhoeae. Infect Immun. 1982 Aug;37(2):622–631. doi: 10.1128/iai.37.2.622-631.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Lambden P. R. Biochemical comparison of pili from variants of Neisseria gonorrhoeae P9. J Gen Microbiol. 1982 Sep;128(9):2105–2111. doi: 10.1099/00221287-128-9-2105. [DOI] [PubMed] [Google Scholar]
  6. Lambden P. R., Robertson J. N., Watt P. J. Biological properties of two distinct pilus types produced by isogenic variants of Neisseria gonorrhoeae P9. J Bacteriol. 1980 Jan;141(1):393–396. doi: 10.1128/jb.141.1.393-396.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Meyer T. F., Mlawer N., So M. Pilus expression in Neisseria gonorrhoeae involves chromosomal rearrangement. Cell. 1982 Aug;30(1):45–52. doi: 10.1016/0092-8674(82)90010-1. [DOI] [PubMed] [Google Scholar]
  8. Robertson J. N., Vincent P., Ward M. E. The preparation and properties of gonococcal pili. J Gen Microbiol. 1977 Sep;102(1):169–177. doi: 10.1099/00221287-102-1-169. [DOI] [PubMed] [Google Scholar]
  9. Salit I. E., Blake M., Gotschlich E. C. Intra-strain heterogeneity of gonococcal pili is related to opacity colony variance. J Exp Med. 1980 Mar 1;151(3):716–725. doi: 10.1084/jem.151.3.716. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Sandstrom E. G., Chen K. C., Buchanan T. M. Serology of Neisseria gonorrhoeae: coagglutination serogroups WI and WII/III correspond to different outer membrane protein I molecules. Infect Immun. 1982 Nov;38(2):462–470. doi: 10.1128/iai.38.2.462-470.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Stead A., Main J. S., Ward M. E., Watt P. J. Studies on lipopolysaccharides isolated from strains of Neisseria gonorrhoeae. J Gen Microbiol. 1975 May;88(1):123–131. doi: 10.1099/00221287-88-1-123. [DOI] [PubMed] [Google Scholar]
  12. Swanson J., Barrera O. Immunological characteristics of gonococcal outer membrane protein II assessed by immunoprecipitation, immunoblotting, and coagglutination. J Exp Med. 1983 May 1;157(5):1405–1420. doi: 10.1084/jem.157.5.1405. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Swanson J. Colony opacity and protein II compositions of gonococci. Infect Immun. 1982 Jul;37(1):359–368. doi: 10.1128/iai.37.1.359-368.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Swanson J., Mayer L. W., Tam M. R. Antigenicity of Neisseria gonorrhoeae outer membrane protein(s) III detected by immunoprecipitation and Western blot transfer with a monoclonal antibody. Infect Immun. 1982 Nov;38(2):668–672. doi: 10.1128/iai.38.2.668-672.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Swanson J. Studies on gonococcus infection. XII. Colony color and opacity varienats of gonococci. Infect Immun. 1978 Jan;19(1):320–331. doi: 10.1128/iai.19.1.320-331.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Swanson J. Studies on gonococcus infection. XVIII. 125I-labeled peptide mapping of the major protein of the gonococcal cell wall outer membrane. Infect Immun. 1979 Mar;23(3):799–810. doi: 10.1128/iai.23.3.799-810.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Tramont E. C., Hodge W. C., Gilbreath M. J., Ciak J. Differences in attachment antigens of gonococci in reinfection. J Lab Clin Med. 1979 May;93(5):730–735. [PubMed] [Google Scholar]
  18. Tramont E. C. Specificity of inhibition of epithelial cell adhesion of Neisseria gonorrhoeae. Infect Immun. 1976 Aug;14(2):593–595. doi: 10.1128/iai.14.2.593-595.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]

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