1887

Abstract

A species-specific monoclonal IgM antibody (mAb) 9BF8 directed against the major outer membrane protein (MOMP) of neutralized several chlamydial serovars in a complement-independent manner. The presence of Mg ions negated the neutralization in serovars F, L1 and L2, but not in serovars A, B, E, D and K. The ability of monovalent Fab-fragments of this mAb to neutralize chlamydial infectivity in a Mg-independent manner suggested that conformational alterations on the chlamydial surface induced by the cation hindered the IgM but allowed the smaller Fab fragment access to its epitope. In order to determine the chlamydial component that binds Mg, elementary bodies (EB) of serovars E and L1 were treated with EDTA at pHs 8 and 9. The infectivity of the treated EB and the amount of released LPS were determined. Only after EDTA treatment at pH 9, as the LPS release increased, did the binding of the mAb on the chlamydial surface become Mg-independent. The infectivity of the EB was almost completely lost after such a treatment. These results suggest that the chlamydial LPS has the potential to modulate the exposure of antigenic sites on the MOMP, when it is cross-linked by Mg. They further imply that serovars protected by Mg and those that are not differ in the surface topology of one particular MOMP epitope, but are antigenically very similar. This difference might be of considerable importance .

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1992-06-01
2021-05-13
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References

  1. Asbell M. A., Eagon R. G. 1966; The role of multivalent cations in the organization and structure of bacterial cell walls. Biochemical and Biophysical Research Communications 22:664–671
    [Google Scholar]
  2. Bavoil P., Stephens R. S., Falkow S. 1990; A soluble 60 kDa antigen of Chlamydia spp. is a homologue of Escherichia coli GroEL. Molecular Microbiology 4:461–469
    [Google Scholar]
  3. Bidlack J. M., Mabie P. C. 1986; Preparation of Fab fragments from a mouse monoclonal IgM. Journal of Immunological Methods 9:157–162
    [Google Scholar]
  4. Birkelund S., Lundemose A. G., Christiansen G. 1988; Chemical cross-linking of Chlamydia trachomatis . Infection and Immunity 56:654–659
    [Google Scholar]
  5. Birkelund S., Lundemose A. G., Christiansen G. 1989; Immunoelectron microscopy of lipopolysaccharide in Chlamydia trachomatis . Infection and Immunity 57:3250–3253
    [Google Scholar]
  6. 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]
  7. Goswami P. C, Vretou E., Bose S. K. 1990; Extensive heterogeneity of the protein composition of Chlamydia trachomatis following serial passage in two different cell lines. Journal of General Microbiology 136:1623–1629
    [Google Scholar]
  8. Hackstadt T. 1988; Steric hindrance of antibody binding to surface proteins of Coxiella burnetii by Phase I lipopolysaccharide. Infection and Immunity 56:802–807
    [Google Scholar]
  9. Hackstadt T. 1991; Purification and N-terminal amino acid sequences of Chlamydia trachomatis histone analogs. Journal of Bacteriology 173:7046–7049
    [Google Scholar]
  10. Hancock R. E. W. 1991; Bacterial outer membranes: evolving concepts. ASM News 57:175–182
    [Google Scholar]
  11. Karimi S. T., Schloemer R. H., Wilde C. E. Ill 1989; Accumulation of chlamydial lipopolysaccharide antigen in the plasma membranes of infected cells. Infection and Immunity 57:1780–1785
    [Google Scholar]
  12. Leive L. 1965; Release of lipopolysaccharide by EDTA treatment of Escherichia coli. . Biochemical and Biophysical Research Communications 21:290–296
    [Google Scholar]
  13. Luederitz O., Freudenberg Μ. Α., Galanos C., Lehmann V., Rietshel Ε. Th., Shaw D. H. 1982; Lipopolysaccharides of Gram-negative bacteria. Current Topics in Membrane Transport 17:79–151
    [Google Scholar]
  14. Marvin H. J. P, Ter Beest Μ. B., Without B. 1989; Release of outer membrane fragments from wild-type Escherichia coli and from several E. coli lipopolysaccharide mutants by EDTA and heat shock treatments. Journal of Bacteriology 171:5262–5267
    [Google Scholar]
  15. Mearns G., Richmond S. J., Storey C. C. 1988; Sensitive immune dot blot for diagnosis of Chlamydia trachomatis infection. Journal of Clinical Microbiology 26:1810–1813
    [Google Scholar]
  16. Morrison R. P., Belland R. J., Lyng K., Caldwell H. D. 1989; Chlamydial disease pathogenesis. The 57 kD chlamydial hypersensitivity antigen is a stress response protein. Journal of Experimental Medicine 170:1271–1283
    [Google Scholar]
  17. Nakane P. K., Kawaoi A. 1974; Peroxidase-labeled antibody: A new method of conjugation. Journal of Histochemistry and Cytochemistry 22:1084–1091
    [Google Scholar]
  18. Narita T., Manire G. P. 1976; Protein-carbohydrate-lipid complex isolated from the cell envelope of Chlamydia psittaci in alkaline buffer and ethylenediaminetetraacetate. Journal of Bacteriology 125:308–316
    [Google Scholar]
  19. Narita T., Wyrick P. B., Manire G. P. 1976; Effect of alkali on the structure of cell envelopes of Chlamydia psittaci elementary bodies. Journal of Bacteriology 125:300–307
    [Google Scholar]
  20. Nurminen Μ., Rietschel E. T., Brade H. 1985; Chemical characterization of Chlamydia trachomatis lipopolysaccharide. Infection and Immunity 48:573–575
    [Google Scholar]
  21. Peeling R., Maclean I. W., Brunham R. 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]
  22. Peterson E. M., Zhong G. M., Carlson E., De La Maza L. M. 1988; Protective role of magnesium in the neutralization by antibodies of Chlamydia trachomatis infectivity. Infection and Immunity 56:885–891
    [Google Scholar]
  23. Pouletty P., Martin J., Catalan F., Garcia-Gonzalez M., Morellet I., Bettinger S., Kadouche J. 1988; Optimization of a rapid test by using fluorescein-conjugated monoclonal antibodies for detection of Chlamydia trachomatis in clinical specimens. Journal of Clinical Microbiology 26:267–270
    [Google Scholar]
  24. Taylor H. R., Prendergast R. 1987; Attempted oral immunization with chlamydial lipopolysaccharide ml-unit vaccine. Investigations in Ophthalmology and Visual Sciences 21:422–433
    [Google Scholar]
  25. Vretou E., Goswami P. C., Bose S. K. 1989; Adherence of multiple serovars of Chlamydia trachomatis to a common receptor on HeLa and McCoy cells is mediated by thermolabile protein(s). Journal of General Microbiology 135:3229–3237
    [Google Scholar]
  26. Vretou E., Spiliopoulou D., Psarrou E. 1991; Topological studies on the major outer membrane protein of Chlamydia trachomatis with an adherence-inhibiting monoclonal antibody. Molecular recognition in host-parasite interactions Abstract no. 21 Porvoo: FEMS Symposium;
    [Google Scholar]
  27. Vretou E., Mendis Α., Psarrou E., Tsoumaris L., Conidou G., Spiliopoulou D. 1992; Unusual prevalence of the rare serovar Da of Chlamydia trachomatis in Greece detected by monoclonal antibodies. Sexually Transmitted Diseases 19: in the Press
    [Google Scholar]
  28. Zhang Y.-X., Stewart S., Joseph T., Taylor H. R., Caldwell H. D. 1987; Protective monoclonal antibodies recognize epitopes located on the major outer membrane protein of Chlamydia trachomatis . Journal of Immunology 138:575–581
    [Google Scholar]
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