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. 1984 Jul 1;160(1):208–221. doi: 10.1084/jem.160.1.208

Strain-specific and common epitopes of gonococcal pili

PMCID: PMC2187432  PMID: 6203999

Abstract

The antigenic structure of gonococcal pilin, strain MS11 (Tr), was investigated by assaying the binding of antisera engendered by intact pili from strains MS11 and R10 and their two major cyanogen bromide- generated fragments, CNBr-2 (residues 9-92) and CNBr-2 (residues 93- 159), to synthetic peptides corresponding to the amino acid sequence of MS11 pilin. Four peptides were synthesized corresponding to regions of sequence variation between MS11 and R10 gonococcal pilin. Antisera against the homologous pilus filament and against its CNBr-3 fragment bind peptides equivalent to residues 121-134 and 135-151, which comprise the 30 amino acid disulfide loop near the carboxyl terminus of the protein. Heterologous pili antisera did not bind these peptides. Absorption studies proved that each peptide contained an independent, strain-specific epitope. Synthetic peptides corresponding to regions of identical sequence between MS11 and R10 pilin were used in similar binding experiments to localize a weakly immunogenic, common determinant between residues 48 and 60. less than 15% of the antibodies raised against intact pili were directed at this site. Antisera raised against MS11 or R10 CNBr-2 bind a separate peptide, residues 69-80. This region is immunogenic only as a fragment, not in the intact pilus filament.

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Selected References

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

  1. Båga M., Normark S., Hardy J., O'Hanley P., Lark D., Olsson O., Schoolnik G., Falkow S. Nucleotide sequence of the papA gene encoding the Pap pilus subunit of human uropathogenic Escherichia coli. J Bacteriol. 1984 Jan;157(1):330–333. doi: 10.1128/jb.157.1.330-333.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Chothia C., Levitt M., Richardson D. Structure of proteins: packing of alpha-helices and pleated sheets. Proc Natl Acad Sci U S A. 1977 Oct;74(10):4130–4134. doi: 10.1073/pnas.74.10.4130. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Chou P. Y., Fasman G. D. Empirical predictions of protein conformation. Annu Rev Biochem. 1978;47:251–276. doi: 10.1146/annurev.bi.47.070178.001343. [DOI] [PubMed] [Google Scholar]
  4. Engvall E. Enzyme immunoassay ELISA and EMIT. Methods Enzymol. 1980;70(A):419–439. doi: 10.1016/s0076-6879(80)70067-8. [DOI] [PubMed] [Google Scholar]
  5. Hopp T. P., Woods K. R. Prediction of protein antigenic determinants from amino acid sequences. Proc Natl Acad Sci U S A. 1981 Jun;78(6):3824–3828. doi: 10.1073/pnas.78.6.3824. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. James-Holmquest A. N., Swanson J., Buchanan T. M., Wende R. D., Williams R. P. Differential attachment by piliated and nonpiliated Neisseria gonorrhoeae to human sperm. Infect Immun. 1974 May;9(5):897–902. doi: 10.1128/iai.9.5.897-902.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Kaiser E., Colescott R. L., Bossinger C. D., Cook P. I. Color test for detection of free terminal amino groups in the solid-phase synthesis of peptides. Anal Biochem. 1970 Apr;34(2):595–598. doi: 10.1016/0003-2697(70)90146-6. [DOI] [PubMed] [Google Scholar]
  8. Kuntz I. D. Tertiary structure in carboxypeptidase. J Am Chem Soc. 1972 Nov 29;94(24):8568–8572. doi: 10.1021/ja00779a046. [DOI] [PubMed] [Google Scholar]
  9. Levitt M. A simplified representation of protein conformations for rapid simulation of protein folding. J Mol Biol. 1976 Jun 14;104(1):59–107. doi: 10.1016/0022-2836(76)90004-8. [DOI] [PubMed] [Google Scholar]
  10. Levitt M., Chothia C. Structural patterns in globular proteins. Nature. 1976 Jun 17;261(5561):552–558. doi: 10.1038/261552a0. [DOI] [PubMed] [Google Scholar]
  11. Pearce W. A., Buchanan T. M. Attachment role of gonococcal pili. Optimum conditions and quantitation of adherence of isolated pili to human cells in vitro. J Clin Invest. 1978 Apr;61(4):931–943. doi: 10.1172/JCI109018. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Richardson J. S. The anatomy and taxonomy of protein structure. Adv Protein Chem. 1981;34:167–339. doi: 10.1016/s0065-3233(08)60520-3. [DOI] [PubMed] [Google Scholar]
  13. Rose G. D. Prediction of chain turns in globular proteins on a hydrophobic basis. Nature. 1978 Apr 13;272(5654):586–590. doi: 10.1038/272586a0. [DOI] [PubMed] [Google Scholar]
  14. Rose G. D., Roy S. Hydrophobic basis of packing in globular proteins. Proc Natl Acad Sci U S A. 1980 Aug;77(8):4643–4647. doi: 10.1073/pnas.77.8.4643. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Rose G. D., Young W. B., Gierasch L. M. Interior turns in globular proteins. Nature. 1983 Aug 18;304(5927):654–657. doi: 10.1038/304654a0. [DOI] [PubMed] [Google Scholar]
  16. Sastry P. A., Pearlstone J. R., Smillie L. B., Paranchych W. Amino acid sequence of pilin isolated from pseudomonas aeruginosa PAK. FEBS Lett. 1983 Jan 24;151(2):253–256. doi: 10.1016/0014-5793(83)80080-5. [DOI] [PubMed] [Google Scholar]
  17. Schoolnik G. K., Fernandez R., Tai J. Y., Rothbard J., Gotschlich E. C. Gonococcal pili. Primary structure and receptor binding domain. J Exp Med. 1984 May 1;159(5):1351–1370. doi: 10.1084/jem.159.5.1351. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Schoolnik G. K., Tai J. Y., Gotschlich E. C. A pilus peptide vaccine for the prevention of gonorrhea. Prog Allergy. 1983;33:314–331. [PubMed] [Google Scholar]
  19. Svanborg Edén C., Gotschlich E. C., Korhonen T. K., Leffler H., Schoolnik G. Aspects on structure and function of pili on uropathogenic Escherichia coli. Prog Allergy. 1983;33:189–202. doi: 10.1159/000318330. [DOI] [PubMed] [Google Scholar]
  20. Swanson J., Kraus S. J., Gotschlich E. C. Studies on gonococcus infection. I. Pili and zones of adhesion: their relation to gonococcal growth patterns. J Exp Med. 1971 Oct 1;134(4):886–906. doi: 10.1084/jem.134.4.886. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Swanson J. Studies on gonococcus infection. IV. Pili: their role in attachment of gonococci to tissue culture cells. J Exp Med. 1973 Mar 1;137(3):571–589. doi: 10.1084/jem.137.3.571. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Yoshitake S., Yamada Y., Ishikawa E., Masseyeff R. Conjugation of glucose oxidase from Aspergillus niger and rabbit antibodies using N-hydroxysuccinimide ester of N-(4-carboxycyclohexylmethyl)-maleimide. Eur J Biochem. 1979 Nov;101(2):395–399. doi: 10.1111/j.1432-1033.1979.tb19731.x. [DOI] [PubMed] [Google Scholar]

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