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. 1986 Feb;165(2):602–607. doi: 10.1128/jb.165.2.602-607.1986

Chlamydia trachomatis elementary bodies possess proteins which bind to eucaryotic cell membranes.

W M Wenman, R U Meuser
PMCID: PMC214461  PMID: 3511037

Abstract

Chlamydia trachomatis proteins were electrophoresed and then transferred to nitrocellulose paper to detect chlamydial proteins which bind to eucaryotic cell membranes. Resolved polypeptides of C. trachomatis serovars J and L2 were reacted with iodinated HeLa cell membranes and autoradiographed. Infectious elementary bodies of both serovars possess 31,000- and 18,000-dalton proteins which bind to HeLa cells. In contrast, noninfectious reticulate bodies do not possess eucaryotic cell-binding proteins. Both proteins are antigenic when reacted with hyperimmune rabbit antisera in immunoblots and antisera raised against the 31,000- and 18,000-dalton proteins are inhibitory to chlamydia-host cell association. In addition, these antisera exhibit neutralizing activity. Our data suggest that these putative chlamydial adhesins play a key role in the early steps of chlamydia-host cell interaction and that antibody directed against them may be protective.

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Selected References

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

  1. Barenfanger J., MacDonald A. B. The role of immunoglobulin in the neutralization of trachoma infectivity. J Immunol. 1974 Nov;113(5):1607–1617. [PubMed] [Google Scholar]
  2. Bose S. K., Paul R. G. Purification of Chlamydia trachomatis lymphogranuloma venereum elementary bodies and their interaction with HeLa cells. J Gen Microbiol. 1982 Jun;128(6):1371–1379. doi: 10.1099/00221287-128-6-1371. [DOI] [PubMed] [Google Scholar]
  3. Byrne G. I. Requirements for ingestion of Chlamydia psittaci by mouse fibroblasts (L cells). Infect Immun. 1976 Sep;14(3):645–651. doi: 10.1128/iai.14.3.645-651.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Caldwell H. D., Perry L. J. Neutralization of Chlamydia trachomatis infectivity with antibodies to the major outer membrane protein. Infect Immun. 1982 Nov;38(2):745–754. doi: 10.1128/iai.38.2.745-754.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. 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]
  6. Eschenbruch M., Bürk R. R. Experimentally improved reliability of ultrasensitive silver staining of protein in polyacrylamide gels. Anal Biochem. 1982 Sep 1;125(1):96–99. doi: 10.1016/0003-2697(82)90387-6. [DOI] [PubMed] [Google Scholar]
  7. Ey P. L., Prowse S. J., Jenkin C. R. Isolation of pure IgG1, IgG2a and IgG2b immunoglobulins from mouse serum using protein A-sepharose. Immunochemistry. 1978 Jul;15(7):429–436. doi: 10.1016/0161-5890(78)90070-6. [DOI] [PubMed] [Google Scholar]
  8. FURNESS G., GRAHAM D. M., REEVE P. The titration of trachoma and inclusion blennorrhoea viruses in cell cultures. J Gen Microbiol. 1960 Dec;23:613–619. doi: 10.1099/00221287-23-3-613. [DOI] [PubMed] [Google Scholar]
  9. Hackstadt T., Caldwell H. D. Effect of proteolytic cleavage of surface-exposed proteins on infectivity of Chlamydia trachomatis. Infect Immun. 1985 May;48(2):546–551. doi: 10.1128/iai.48.2.546-551.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hatch T. P., Allan I., Pearce J. H. Structural and polypeptide differences between envelopes of infective and reproductive life cycle forms of Chlamydia spp. J Bacteriol. 1984 Jan;157(1):13–20. doi: 10.1128/jb.157.1.13-20.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hayman E. G., Engvall E., A'Hearn E., Barnes D., Pierschbacher M., Ruoslahti E. Cell attachment on replicas of SDS polyacrylamide gels reveals two adhesive plasma proteins. J Cell Biol. 1982 Oct;95(1):20–23. doi: 10.1083/jcb.95.1.20. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Holmes K. K. The Chlamydia epidemic. JAMA. 1981 May 1;245(17):1718–1723. [PubMed] [Google Scholar]
  13. Howard L. V. Neutralization of Chlamydia trachomatis in cell culture. Infect Immun. 1975 Apr;11(4):698–703. doi: 10.1128/iai.11.4.698-703.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. JENKIN H. M. Preparation and properties of cell walls of the agent of meningopneumonitis. J Bacteriol. 1960 Nov;80:639–647. doi: 10.1128/jb.80.5.639-647.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  16. 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]
  17. Lee C. K. Interaction between a trachoma strain of Chlamydia trachomatis and mouse fibroblasts (McCoy cells) in the absence of centrifugation. Infect Immun. 1981 Feb;31(2):584–591. doi: 10.1128/iai.31.2.584-591.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Levy N. J., Moulder J. W. Attachment of cell walls of Chlamydia psittaci to mouse fibroblasts (L cells). Infect Immun. 1982 Sep;37(3):1059–1065. doi: 10.1128/iai.37.3.1059-1065.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Morrison M. Lactoperoxidase-catalyzed iodination as a tool for investigation of proteins. Methods Enzymol. 1980;70(A):214–220. doi: 10.1016/s0076-6879(80)70051-4. [DOI] [PubMed] [Google Scholar]
  20. Oblas B., Boyd N. D., Singer R. H. Analysis of receptor-ligand interactions using nitrocellulose gel transfer: application to Torpedo acetylcholine receptor and alpha-bungarotoxin. Anal Biochem. 1983 Apr 1;130(1):1–8. doi: 10.1016/0003-2697(83)90641-3. [DOI] [PubMed] [Google Scholar]
  21. Peeling R., Maclean I. W., Brunham R. C. In vitro neutralization of Chlamydia trachomatis with monoclonal antibody to an epitope on the major outer membrane protein. Infect Immun. 1984 Nov;46(2):484–488. doi: 10.1128/iai.46.2.484-488.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Schachter J. Chlamydial infections (third of three parts). N Engl J Med. 1978 Mar 9;298(10):540–549. doi: 10.1056/NEJM197803092981005. [DOI] [PubMed] [Google Scholar]
  23. Söderlund G., Kihlström E. Attachment and internalization of a Chlamydia trachomatis lymphogranuloma venereum strain by McCoy cells: kinetics of infectivity and effect of lectins and carbohydrates. Infect Immun. 1983 Dec;42(3):930–935. doi: 10.1128/iai.42.3.930-935.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. 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]
  25. Ward M. E., Murray A. Control mechanisms governing the infectivity of Chlamydia trachomatis for HeLa cells: mechanisms of endocytosis. J Gen Microbiol. 1984 Jul;130(7):1765–1780. doi: 10.1099/00221287-130-7-1765. [DOI] [PubMed] [Google Scholar]
  26. Williams D. M., Schachter J., Grubbs B., Sumaya C. V. The role of antibody in host defense against the agent of mouse pneumonitis. J Infect Dis. 1982 Feb;145(2):200–205. doi: 10.1093/infdis/145.2.200. [DOI] [PubMed] [Google Scholar]

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