Skip to main content
PMC home page
Infection and Immunity logoLink to Infection and Immunity
. 1982 Dec;38(3):1181–1189. doi: 10.1128/iai.38.3.1181-1189.1982

Analysis of the human serological response to proteins of Chlamydia trachomatis.

W J Newhall, B Batteiger, R B Jones
PMCID: PMC347873  PMID: 6185424

Abstract

Sera from individuals with culture-proven genital infection with Chlamydia trachomatis were analyzed for the presence of antibodies to chlamydial proteins by an immunoelectrophoretic transfer method. Protein antigens from representative strains of the 15 known serotypes were resolved by gel electrophoresis and transferred to a nitrocellulose solid support before being probed with serum. Sera from infected patients reacted with many different proteins. Most of these sera reacted with a 60,000- and a 62,000-molecular-weight protein which were present in each of the C. trachomatis serotypes and clinical isolates analyzed. In contrast, reactions with the major outer membrane protein were frequently observed but were usually weak. Sera from control groups of children, cloistered nuns, and college women, who were presumed not to have had prior chlamydial infections, did not usually have antibodies against the 60,000- or 62,000-molecular-weight protein, but did react with the major outer membrane protein and a 29,000-molecular-weight protein. These observations may have implications for the development of serodiagnostic tests as well as the identification of candidate antigens for vaccine development.

Full text

PDF
1182

Images in this article

1183Image
on p.1183
1184Image
on p.1184
1185Image
on p.1185
1185Image
on p.1185
1186Image
on p.1186

Selected References

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

  1. Bittner M., Kupferer P., Morris C. F. Electrophoretic transfer of proteins and nucleic acids from slab gels to diazobenzyloxymethyl cellulose or nitrocellulose sheets. Anal Biochem. 1980 Mar 1;102(2):459–471. doi: 10.1016/0003-2697(80)90182-7. [DOI] [PubMed] [Google Scholar]
  2. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  3. Caldwell H. D., Kromhout J., Schachter J. Purification and partial characterization of the major outer membrane protein of Chlamydia trachomatis. Infect Immun. 1981 Mar;31(3):1161–1176. doi: 10.1128/iai.31.3.1161-1176.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Caldwell H. D., Kuo C. C., Kenny G. E. Antigenic analysis of Chlamydiae by two-dimensional immunoelectrophoresis. II. A trachoma-LGV-specific antigen. J Immunol. 1975 Oct;115(4):969–975. [PubMed] [Google Scholar]
  5. Caldwell H. D., Kuo C. C. Serologic diagnosis of Lymphogranuloma venereum by counterimmunoelectrophoresis with a Chlamydia trachomatis protein antigen. J Immunol. 1977 Feb;118(2):442–445. [PubMed] [Google Scholar]
  6. Caldwell H. D., Schachter J. Antigenic analysis of the major outer membrane protein of Chlamydia spp. Infect Immun. 1982 Mar;35(3):1024–1031. doi: 10.1128/iai.35.3.1024-1031.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Dhir S. P., Hakomori S., Kenny G. E., Grayston J. T. Immunochemical studies on chlamydial group antigen (presence of a 2-keto-3-deoxycarbohydrate as immunodominant group). J Immunol. 1972 Jul;109(1):116–122. [PubMed] [Google Scholar]
  8. Fraker P. J., Speck J. C., Jr Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphrenylglycoluril. Biochem Biophys Res Commun. 1978 Feb 28;80(4):849–857. doi: 10.1016/0006-291x(78)91322-0. [DOI] [PubMed] [Google Scholar]
  9. Hatch T. P., Vance D. W., Jr, Al-Hossainy E. Identification of a major envelope protein in Chlamydia spp. J Bacteriol. 1981 Apr;146(1):426–429. doi: 10.1128/jb.146.1.426-429.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  11. Laskey R. A., Mills A. D. Enhanced autoradiographic detection of 32P and 125I using intensifying screens and hypersensitized film. FEBS Lett. 1977 Oct 15;82(2):314–316. doi: 10.1016/0014-5793(77)80609-1. [DOI] [PubMed] [Google Scholar]
  12. Newhall W. J., Wilde C. E., 3rd, Sawyer W. D., Haak R. A. High-molecular-weight antigenic protein complex in the outer membrane of Neisseria gonorrhoeae. Infect Immun. 1980 Feb;27(2):475–482. doi: 10.1128/iai.27.2.475-482.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Sacks D. L., Rota T. R., MacDonald A. B. Separation and partial characterization of a type-specific antigen from Chlamydia trachomatis. J Immunol. 1978 Jul;121(1):204–208. [PubMed] [Google Scholar]
  14. Salari S. H., Ward M. E. Polypeptide composition of Chlamydia trachomatis. J Gen Microbiol. 1981 Apr;123(2):197–207. doi: 10.1099/00221287-123-2-197. [DOI] [PubMed] [Google Scholar]
  15. Schachter J., Caldwell H. D. Chlamydiae. Annu Rev Microbiol. 1980;34:285–309. doi: 10.1146/annurev.mi.34.100180.001441. [DOI] [PubMed] [Google Scholar]
  16. Schaffner W., Weissmann C. A rapid, sensitive, and specific method for the determination of protein in dilute solution. Anal Biochem. 1973 Dec;56(2):502–514. doi: 10.1016/0003-2697(73)90217-0. [DOI] [PubMed] [Google Scholar]
  17. Stephens R. S., Tam M. R., Kuo C. C., Nowinski R. C. Monoclonal antibodies to Chlamydia trachomatis: antibody specificities and antigen characterization. J Immunol. 1982 Mar;128(3):1083–1089. [PubMed] [Google Scholar]
  18. Thomas B. J., Reeve P., Oriel J. D. Simplified serological test for antibodies to Chlamydia trachomatis. J Clin Microbiol. 1976 Jul;4(1):6–10. doi: 10.1128/jcm.4.1.6-10.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Wang S. P., Grayston J. T., Alexander E. R. Trachoma vaccine studies in monkeys. Am J Ophthalmol. 1967 May;63(5 Suppl):1615–1630. doi: 10.1016/0002-9394(67)94155-4. [DOI] [PubMed] [Google Scholar]
  21. Wang S. P., Grayston J. T. Human serology in Chlamydia trachomatis infection with microimmunofluorescence. J Infect Dis. 1974 Oct;130(4):388–397. doi: 10.1093/infdis/130.4.388. [DOI] [PubMed] [Google Scholar]
  22. Wang S. P., Kuo C. C., Grayston J. T. A simplified method for immunological typing of trachoma-inclusion conjunctivitis-lymphogranuloma venereum organisms. Infect Immun. 1973 Mar;7(3):356–360. doi: 10.1128/iai.7.3.356-360.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Yong E. C., Chinn J. S., Caldwell H. D., Kuo C. C. Reticulate bodies as single antigen in Chlamydia trachomatis serology with microimmunofluorescence. J Clin Microbiol. 1979 Sep;10(3):351–356. doi: 10.1128/jcm.10.3.351-356.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Infection and Immunity are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES