1887

Abstract

The cell surfaces of two serovars were explored by immune electron microscopy with monoclonal antibodies that recognize a number of chlamydial outer-membrane components. Species, subspecies and serovar-reactive epitopes on the major outer-membrane protein (MOMP) of a lymphogranuloma venereum biovar strain, L/434/Bu, and a trachoma biovar strain, F/UW-6/Cx, were exposed on the surfaces of both elementary bodies (EBs) and reticulate bodies (RBs). Three epitopes on MOMP were inaccessible on EBs and RBs of both strains. These included a genus-reactive, species-reactive, and a subspecies-reactive epitope. In contrast, genus-specific epitopes on lipopolysaccharide (LPS) were not detected on the EB surface, but were clearly expressed on RBs of both L/434/Bu and F/UW-6/Cx chlamydiae. Antibodies specific for the 60 kDa and 12 kDa cysteine-rich outer-membrane proteins did not react with surface epitopes on either EBs or RBs. These data provide evidence that MOMP is a major surface antigen of both morphological forms, whereas some portions of the LPS molecule are exposed on the RB surface but become inaccessible to antibody after conversion to the infectious EB form.

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1989-01-01
2021-05-10
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References

  1. Barbour A. G., Amano K. -I., Hackstadt T., Perry L., Caldwell H. D. 1982; Chlamydia trachomatis has penicillin-binding proteins but not detectable muramic acid. Journal of Bacteriology 151:420–428
    [Google Scholar]
  2. Barenfanger J., Macdonald A. B. 1974; The role of immunoglobulin in the neutralization of trachoma infectivity. Journal of Immunology 113:1607–1617
    [Google Scholar]
  3. Batteiger B. E., Newhall V, Terho P., Wilde C. E.III Jones R. B. 1986; Antigenic analysis of the major outer membrane protein of Chlamydia trachomatis with murine monoclonal antibodies. Infection and Immunity 53:530–533
    [Google Scholar]
  4. Bavoil P., Ohlin A., Schachter J. 1984; Role of disulfide bonding in outer membrane structure and permeability in Chlamydia trachomatis. Infection and Immunity 44:479–485
    [Google Scholar]
  5. Beesley J. E. 1984; Recent advances in microbiological immunocytochemistry. In Immunolabelling for Electron Microscopy pp. 289–303 Polak J. M., Vamdell I. M. Edited by Amsterdam: Elsevier Science Publishers;
    [Google Scholar]
  6. Beesley J. E., Day S. E. J., Betts M. P., Thorley C. M. 1984; Immunocytochemicallabelling of Bacteroidesnodosus pili using an immunogold technique. Journal of General Microbiology 130:1481–1487
    [Google Scholar]
  7. Benson J. R., Hare P. E. 1975; O-phthalaldehyde: fluorogenic detection of primary amines in the picomole range. Comparison with fluorescamine and ninhydrin. Proceedings of the National Academy of Sciences of the United States of America 72:619–622
    [Google Scholar]
  8. Byrne G. I., Moulder J. W. 1978; Parasite- specified phagocytosis of Chlamydia psittaci and Chlamydia trachomatis by L and HeLa cells. Infection and Immunity 19:598–606
    [Google Scholar]
  9. Caldwell H. D., Hitchcock P. J. 1984; Monoclonal antibody against a genus-specific antigen of Chlamydia species: location of the epitope on chlamydial lipopolysaccharide. Infection and Immunity 44:306–314
    [Google Scholar]
  10. Caldwell H. D., Perry L. J. 1982; Neutralization of Chlamydia trachomatis infectivity with antibodies to the major outer membrane protein. Infection and Immunity 38:745–754
    [Google Scholar]
  11. Caldwell H. D., Kromhout J., Schachter J. 1981; Purification and partial characterization of the major outer membrane protein of Chlamydia trachomatis. Infection and Immunity 31:1161–1176
    [Google Scholar]
  12. Clark R. B., Nachamkin I., Schatzki P. F., Dalton H. P. 1982; Localization of distinct surface antigens of Chlamydia trachomatis HAR-13 by immune electron microscopy with monoclonal antibodies. Infection and Immunity 38:1273–1278
    [Google Scholar]
  13. Eissenberg L. G., Wyrick P. B. 1981; Inhibition of phagolysosome fusion is localized to Chlamydia psittaci- laden vacuoles. Infection and Immunity 32:889–896
    [Google Scholar]
  14. Eissenberg L. G., Wyrick P. B., Davis C. H., Rumpp J. W. 1983; Chlamydia psittaci elementary body envelopes: ingestion and inhibition of phagolysosome fusion. Infection and Immunity 40:741–751
    [Google Scholar]
  15. Friis R. R. 1972; Interaction of L cells and Chlamydia psittaci: entry of the parasite and host responses to its development. Journal of Bacteriology 110:706–721
    [Google Scholar]
  16. Hackstadt T. 1986; Identification and properties of chlamydial polypeptides that bind eucaryotic cell surface components. Journal of Bacteriology 165:13–20
    [Google Scholar]
  17. Hackstadt T., Caldwell H. D. 1985; Effect of proteolytic cleavage of surface-exposed proteins on infectivity of Chlamydia trachomatis. Infection and Immunity 48:546–551
    [Google Scholar]
  18. Hatch T. P., Allan I., Pearce J. H. 1984; Structural and polypeptide differences between envelopes of infective and reproductive life cycle forms of Chlamydia spp. Journal of Bacteriology 157:13–20
    [Google Scholar]
  19. Hatch T. P., Miceli M., Sublett J. E. 1986; Synthesis of disulfide-bonded outer membrane proteins during the developmental cycle of Chlamydia psittaci and Chlamydia trachomatis. Journal of Bac-teriology 165:379–385
    [Google Scholar]
  20. Jones R. B., Bruins S. C., Newhall V. W. J. 1983; Comparison of reticulate and elementary body antigens in detection of antibodies against Chlamydia trachomatis by an enzyme-linked immunosorbent assay. Journal of Clinical Microbiology 17:466–471
    [Google Scholar]
  21. Kuo C. -C., Chi E. Y. 1987; Ultrastructural study of Chlamydia trachomatis surface antigens by immunogold staining with monoclonal antibodies. Infection and Immunity 55:1324–1328
    [Google Scholar]
  22. Kuo C. -C., Grayson J. T. 1976; Interaction of Chlamydia trachomatis organisms and HeLa 229 cells. Infection and Immunity 13:1103–1109
    [Google Scholar]
  23. Lawn A. M., Blyth W. A., Taverne J. 1973; Interactions of TRIC agents with macrophages and BHK-21 cells observed by electron microscopy. Journal of Hygiene 71:515–528
    [Google Scholar]
  24. Levy N. J., Moulder J. W. 1982; Attachment of cell walls of Chlamydia psittaci to mouse fibroblasts (L cells). Infection and Immunity 17:1059–1065
    [Google Scholar]
  25. Lucero M. E., Kuo C. -C. 1985; Neutralization of Chlamydia trachomatis cell culture infection by serovar-specific monoclonal antibodies. Infection and Immunity 50:595–597
    [Google Scholar]
  26. Mouton C., Lamonde L. 1984; Immunogold electron microscopy of surface antigens of oral bacteria. Canadian Journal of Microbiology 30:1008–1013
    [Google Scholar]
  27. Newhall V. 1987; Biosynthesis and disulfide cross-linking of outer membrane components during the growth cycle of Chlamydia trachomatis. Infection and Immunity 55:162–168
    [Google Scholar]
  28. Newhall V, Basinski M. B. 1986; Purification and structural characterization of chlamydial outer membrane proteins. In Chlamydial Infections pp. 93–96 Oriel D., Ridgway F., Schachter J., Taylor-Robinson D., Ward M. Edited by Cambridge: Cambridge University Press;
    [Google Scholar]
  29. Newhall V, Batteiger B., Jones R. B. 1982; Analysis of the human serological response to proteins of Chlamydia trachomatis. Infection and Immunity 38:1181–1189
    [Google Scholar]
  30. Newhall V, Mail L. B., Wilde C. E.III Jones R. B. 1985; Purification and antigenic relatedness of proteins II of Neisseria gonorrhoeae. Infection and Immunity 49:576–580
    [Google Scholar]
  31. Newhall V, Terho P., Wilde C. E.III Batteiger B. E., Jones R. B. 1986; Serovar determination of Chlamydia trachomatis isolates by using type-specific monoclonal antibodies. Journal of Clinical Microbiology 23:333–338
    [Google Scholar]
  32. Peeling R., Maclean I. W., Brunham R. C. 1984; In vitro neutralization of Chlamydia trachomatis with monoclonal antibody to an epitope on the major outer membrane protein. Infection and Immunity 46:484–488
    [Google Scholar]
  33. Reeve P., Taverne J. 1962; Some properties of the complement-fixing antigens of trachoma and inclusion blenorrhea and the relationship of the antigens to the development cycle. Journal of General Microbiology 27:501–508
    [Google Scholar]
  34. Richmond S. J., Stirling P. 1981; Localization of chlamydial group antigen in McCoy cell monolayers infected with Chlamydia trachomatis or Chlamydia psittaci. Infection and Immunity 34:561–570
    [Google Scholar]
  35. Robinson E. N.Jr Mcgee Z. A., Kaplan J., Hammond M. E., Larson J. K., Buchanan T. M., Schoolnik G. K. 1984; Ultrastructural localization of specific gonococcal macromolecules with antibody-gold sphere immunological probes. Infection and Immunity 46:361–366
    [Google Scholar]
  36. Salari S. H., Ward M. E. 1981; Polypeptide composition of Chlamydia trachomatis. Journal of General Microbiology 123:197–207
    [Google Scholar]
  37. Stephens R. S., Tam M. R., Kuo C. -C., Nowinski R. C. 1982; Monoclonal antibodies to Chlamydia trachomatis: antibody specificities and antigen characterization. Journal of Immunology 128:1083–1089
    [Google Scholar]
  38. Stirling P., Richmond S. J. 1980; Production of outer membrane blebs during chlamydial replication. FEMS Microbiology Letters 9:103–105
    [Google Scholar]
  39. Wang S. -P., Grayston J. T. 1971; Classification of TRIC and related strains with microimmunofluorescence. In Trachoma and Related Disorders Caused by Chlamydial Agents pp. 305–321 Nichols R. L. Edited by Amsterdam: Excerpta Medica;
    [Google Scholar]
  40. Ward M. E., Murray A. 1984; Control mechanisms governing the infectivity of Chlamydia trachomatis for HeLa cells: mechanisms of endocytosis. Journal of General Microbiology 130:1765–1780
    [Google Scholar]
  41. Wenman W. M., Meuser R. U. 1986; Chlamydia trachomutis elementary bodies possess proteins which bind to eucaryotic cell membranes. Journal of Bacteriology 165:602–607
    [Google Scholar]
  42. Wilde C. E.III Karimi S. T., Haak R. A. 1986; Cell surface alterations during chlamydial infection. In Microbiology-1986 pp. 96–98 Washington, DC:: American Society for Microbiology.;
    [Google Scholar]
  43. Williams W. D., Schachter J., Grubbs B., Sumaya C. V. 1982; The role of antibody in host defense against the agent of mouse pneumonitis. Journal of Infectious Diseases 145:200–205
    [Google Scholar]
  44. Yong E. C., Chinn J. S., Caldwell H. D., Kuo C. -C. 1979; Reticulate bodies as single antigen in Chlamydia trachomatis serology with microimmunofluorescence. Journal of Clinical Microbiology 10:351–356
    [Google Scholar]
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