1887

Abstract

is a leading cause of sexually transmitted diseases and a number of strategies have been developed to produce vaccines to prevent its transmission. The purpose of this study was to map the neutralizing epitopes of major outer-membrane protein (MOMP) serovar K by using anti-MOMP antibodies and synthetic peptides. Seven anti-MOMP monoclonal antibodies and three polyclonal antisera were produced and characterized. Their fine specificity was defined by direct binding assay on 15 peptides of 10 amino acid residues, overlapping by five residues, corresponding to the four variable domains (VDI-VDIV: residues 64-85, 139-160, 224-237 and 287-319) of MOMP serovar K. Our data confirmed that a neutralizing epitope is found in VDIV, defined by peptides K12 and K13. This epitope is TTLNPTIAG, which has never been reported as a neutralizing epitope of serovar K. Another neutralizing epitope, defined by peptide K2, has been identified in VDI. This epitope is in the same position as VAGLEK, a peptide with neutralizing activity found in serovar A, but they are not identical because antibodies against peptide K2 do not bind to this epitope. No neutralizing epitope was found in the two other variable domains (VDII and III). In summary, two neutralizing sites, one in variable domain I and one in variable domain IV, were identified in serovar K.

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1994-09-01
2024-10-14
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References

  1. Baehr W., Zhang Y.Z., Joseph T., Su H., Nano F.E., Everett K.D.E., Caldwell H.D. Mapping antigenic domains expressed by Chlamydia trachomatis major outer membrane genes. Proc Natl Acad Set USA 1988; 85:4000–4004
    [Google Scholar]
  2. Brossay L., Villeneuve A., Paradis G., Mourad W., Cote L., Hebert J. Mimicry of a neutralizing epitope of the major outer membrane protein of Chlamydia trachomatis by anti-idiotypic antibodies. Infect Immun 1994; 62:341–347
    [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; 31:1161–1176
    [Google Scholar]
  4. Conlan J.W., Clarke I.N., Ward M.E. Epitope mapping with solid-phase peptides: identification of type-, subspecies-, species-, and genus-reactive antibody binding domains on the major outer membrane protein of Chlamydia trachomatis. Mol Microbiol 1988; 2:673–679
    [Google Scholar]
  5. Conlan J.W., Ferris S., Clarke I.N., Ward M.E. Surface-exposed epitopes on the major outer membrane protein of Chlamydia trachomatis defined with peptide antisera. J Gen Microbiol 1989; 135:3219–3228
    [Google Scholar]
  6. Geysen H.M., Meloen R.H., Barteling S.J. Use of peptide synthesis to probe viral antigens for epitopes to a resolution of a single amino acid. Proc Natl Acad Sci USA 1984; 81:3998–4002
    [Google Scholar]
  7. Geysen H.M., Rodda S.J., Mason T.J., Tribbick G., Schoofs P.G. Strategies for epitope analysis using peptide synthesis. J Immunol Methods 1987; 102:259–274
    [Google Scholar]
  8. Grayston J.T., Wang S.P. New knowledge of chlamydiae and the diseases they cause. J Infect Dis 1975; 132:87–104
    [Google Scholar]
  9. Grayston J.T., Kim K.S.W., Alexander E.R., Wang S.-P. Protective studies in monkeys with trivalent and monovalent trachoma vaccines. In Trachoma and Related Disorders Caused by Chlamydial Agents 1971 Edited by Nichols R.L. Amsterdam: Excerpta Medica; pp 377–385
    [Google Scholar]
  10. Jawetz E., Rose L., Hanna L., Thygeson P. Experimental inclusion conjunctivitis in man. Measurements of infectivity and resistance. J Am Med Assoc 1965; 194:620–632
    [Google Scholar]
  11. Lucero M.E., Kuo C.C. Neutralization of Chlamydia trachomatis cell culture infection by serovar specific monoclonal antibodies. Infect Immun 1985; 50:590–597
    [Google Scholar]
  12. McGhee J.R., Mestecky J. In defense of mucosal surfaces: development of novel vaccines for IgA responses protective at the portals of entry of microbial pathogens. Infect Dis Clinics of North America 1990; 4:315–341
    [Google Scholar]
  13. Murray E.S., Charbonnet L.T., MacDonald A.B. Immunity to chlamydial infections of the eye. I. The role of circulatory and secretory antibodies in resistance to reinfection with guinea pig inclusion conjunctivitis. J Immunol 1973; 110:1518–1525
    [Google Scholar]
  14. Nichols R.L., Oertley R.E., Fraser C.E.O., MacDonald A.B., McComb D.E. Immunity to chlamydial infections of the eye. VI. Homologous neutralization of trachoma infectivity for the owl monkey conjunctivae by eye secretions from humans with trachoma. J Infect Dis 1973; 127:429–432
    [Google Scholar]
  15. Peeling R.W., 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; 46:484–488
    [Google Scholar]
  16. Peterson E.M., Cheng X., Markoff B.A., Fielder T.J., De La Maza L.M. Functional and structural mapping of Chlamydia trachomatis species-specific major outer membrane epitopes by use of neutralizing monoclonal antibodies. Infect Immun 1991; 59:4147–4153
    [Google Scholar]
  17. Qu Z., Cheng X., De La Maza L.M., Peterson E.M. Characterization of a neutralizing monoclonal antibody directed at variable domain I of the major outer membrane protein of Chlamydia trachomatis C-complex serovars. Infect Immun 1993; 61:1365–1370
    [Google Scholar]
  18. Sabet S.F., Simmons J., Caldwell H.D. Enhancement of Chlamydia trachomatis infectious progeny by cultivation of HeLa 229 cells treated with DEAE-dextran and cycloheximide. J Clin Microbiol 1984; 20:217–222
    [Google Scholar]
  19. Schachter J. Epidemiology of Chlamydia trachomatis infection. In Medical Urology II 1983 Edited by de la Maza L.M., Peterson E.M. New York: Elsevie; pp 111–120
    [Google Scholar]
  20. 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; 128:1083–1089
    [Google Scholar]
  21. Stephens R.S., Mullenbach G., Sanchez P.R., Agabian N. Sequence analysis of the major outer membrane protein gene from Chlamydia trachomatis serovar L2. J Bacteriol 1986; 168:1277–1282
    [Google Scholar]
  22. Stephens R.S., Sanchez P.R., Wagar E.A., Inouye C., Urdea M.S. Diversity of Chlamydia trachomatis major outer membrane protein genes. J Bacteriol 1987; 169:3879–3885
    [Google Scholar]
  23. Stephens R.S., Wagar E.A., Schoolnik G.K. High-resolution mapping of serovar-specific and common antigenic determinants of the major outer membrane protein of Chlamydia trachomatis. J Exp Med 1988; 167:817–831
    [Google Scholar]
  24. Su H., Caldwell H.D. Immunogenicity of a chimeric peptide corresponding to T helper and B cell epitopes of the Chlamydia trachomatis major outer membrane protein. J Exp Med 1992; 175:227–235
    [Google Scholar]
  25. Su H., Morrison R.P., Watkins N.G., Caldwell H.D. Identification and characterization of T helper cell epitopes of the major outer membrane protein of Chlamydia trachomatis. I Exp Med 1990a; 172:203–212
    [Google Scholar]
  26. Su H., Watkins N.G., Zhang Y.X., Caldwell H.D. Chlamydia trachomatis-host cell interactions: role of the chlamydial major outer membrane protein as an adhesin. Infect Immun 1990b; 58:1017–1025
    [Google Scholar]
  27. Wang S.-P., Grayston L.T., Alexander E.R. Trachoma vaccine Studies in monkeys. Am J Ophthalmol 1967; 63:1615
    [Google Scholar]
  28. Yuan Y., Zhang Y.X., Watkins N.G., Caldwell H.D. Nucleoi idc and deduced amino acid sequences for the four variable domain, of the major outer membrane proteins of the 15 Chlamydza trachomatis serovars. Infect Immun 1989; 57:1040–1049
    [Google Scholar]
  29. Zhang Y.X., Stewart S., Joseph T., Taylor H.R., Caldwell H.D. Protective monoclonal antibodies recognize epitopes located on the major outer membrane protein of Chlamydia trachomatis. J Immunol 1987; 138:575–581
    [Google Scholar]
  30. Zhang Y.X., Stewart S.J., Caldwell H.D. Protective monoclonal antibodies to Chlamydia trachomatis serovar- and serogroup-specific major outer membrane protein determinants. Infect Immun 1989; 57:636–638
    [Google Scholar]
  31. Zhong G.M., Brunham R.C. Immunoaccessible peptide sequences of the major outer membrane protein from Chlamydia trachomafis serovar C. Infect Immun 1990; 58:3438–3441
    [Google Scholar]
  32. Zhong G.M., Brunham R.C. Antigenic determinants of the chlamydia1 major outer membrane protein resolved at a single amino acid level. Infect Immun 1991; 59:1141–1147
    [Google Scholar]
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