Abstract
The principal surface protein antigen of Chlamydia trachomatis is the major outer membrane protein (MOMP). The MOMP is antigenically complex. Among the 15 serovars of C. trachomatis, mAbs define serovar-, subspecies-, and species-specific determinants on MOMP. The molecular basis of the antigenic diversity of these proteins is reflected in amino acid variable sequence domains. We have mapped the dominant topographic antigenic determinants of MOMP that are defined by mAbs. Using recombinant DNA approaches we have identified the linear distribution of two antigenic domains. One domain contains a serovar- specific determinant and the other contains subspecies- and species- specific determinants. These antigenic domains correspond to two amino acid sequence variable domains. Synthetic peptides were immunogenic and these resolved the serovar-specific determinant within a 14-amino acid peptide. The subspecies- and species-specific determinants were overlapping within a 16-amino acid peptide.
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Selected References
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- Bavoil P., Ohlin A., Schachter J. Role of disulfide bonding in outer membrane structure and permeability in Chlamydia trachomatis. Infect Immun. 1984 May;44(2):479–485. doi: 10.1128/iai.44.2.479-485.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Caldwell H. D., Judd R. C. Structural analysis of chlamydial major outer membrane proteins. Infect Immun. 1982 Dec;38(3):960–968. doi: 10.1128/iai.38.3.960-968.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- Caldwell H. D., Kuo C. C., Kenny G. E. Antigenic analysis of Chlamydiae by two-dimensional immunoelectrophoresis. I. Antigenic heterogeneity between C. trachomatis and C. psittaci. J Immunol. 1975 Oct;115(4):963–968. [PubMed] [Google Scholar]
- 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]
- GRAYSTON J. T., WOOLRIDGE R. L., WANG S. P., YEN C. H., YANG C. Y., CHENG K. H., CHANG I. H. Field studies of protection from infection by experimental trachoma virus vaccine in preschool-aged children on Taiwan. Proc Soc Exp Biol Med. 1963 Mar;112:589–595. doi: 10.3181/00379727-112-28112. [DOI] [PubMed] [Google Scholar]
- Grayston J. T., Wang S. P., Yeh L. J., Kuo C. C. Importance of reinfection in the pathogenesis of trachoma. Rev Infect Dis. 1985 Nov-Dec;7(6):717–725. doi: 10.1093/clinids/7.6.717. [DOI] [PubMed] [Google Scholar]
- Grayston J. T., Wang S. New knowledge of chlamydiae and the diseases they cause. J Infect Dis. 1975 Jul;132(1):87–105. doi: 10.1093/infdis/132.1.87. [DOI] [PubMed] [Google Scholar]
- Hopp T. P., Woods K. R. Prediction of protein antigenic determinants from amino acid sequences. Proc Natl Acad Sci U S A. 1981 Jun;78(6):3824–3828. doi: 10.1073/pnas.78.6.3824. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ma J. J., Chen K. C., Kuo C. C. Identification of conserved regions for species and subspecies specific epitopes on the major outer membrane protein of Chlamydia trachomatis. Microb Pathog. 1987 Oct;3(4):299–307. doi: 10.1016/0882-4010(87)90063-5. [DOI] [PubMed] [Google Scholar]
- Newhall W. J., Jones R. B. Disulfide-linked oligomers of the major outer membrane protein of chlamydiae. J Bacteriol. 1983 May;154(2):998–1001. doi: 10.1128/jb.154.2.998-1001.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- Rothbard J. B., Fernandez R., Schoolnik G. K. Strain-specific and common epitopes of gonococcal pili. J Exp Med. 1984 Jul 1;160(1):208–221. doi: 10.1084/jem.160.1.208. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schmidt M. A., O'Hanley P., Schoolnik G. K. Gal-Gal pyelonephritis Escherichia coli pili linear immunogenic and antigenic epitopes. J Exp Med. 1985 Apr 1;161(4):705–717. doi: 10.1084/jem.161.4.705. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Stephens R. S., Kuo C. C., Newport G., Agabian N. Molecular cloning and expression of Chlamydia trachomatis major outer membrane protein antigens in Escherichia coli. Infect Immun. 1985 Mar;47(3):713–718. doi: 10.1128/iai.47.3.713-718.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Stephens R. S., Mullenbach G., Sanchez-Pescador R., Agabian N. Sequence analysis of the major outer membrane protein gene from Chlamydia trachomatis serovar L2. J Bacteriol. 1986 Dec;168(3):1277–1282. doi: 10.1128/jb.168.3.1277-1282.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Stephens R. S., Sanchez-Pescador R., Wagar E. A., Inouye C., Urdea M. S. Diversity of Chlamydia trachomatis major outer membrane protein genes. J Bacteriol. 1987 Sep;169(9):3879–3885. doi: 10.1128/jb.169.9.3879-3885.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- Tainer J. A., Getzoff E. D., Alexander H., Houghten R. A., Olson A. J., Lerner R. A., Hendrickson W. A. The reactivity of anti-peptide antibodies is a function of the atomic mobility of sites in a protein. Nature. 1984 Nov 8;312(5990):127–134. doi: 10.1038/312127a0. [DOI] [PubMed] [Google Scholar]
- Tam M. R., Stamm W. E., Handsfield H. H., Stephens R., Kuo C. C., Holmes K. K., Ditzenberger K., Krieger M., Nowinski R. C. Culture-independent diagnosis of Chlamydia trachomatis using monoclonal antibodies. N Engl J Med. 1984 May 3;310(18):1146–1150. doi: 10.1056/NEJM198405033101803. [DOI] [PubMed] [Google Scholar]
- Thornton J. M., Edwards M. S., Taylor W. R., Barlow D. J. Location of 'continuous' antigenic determinants in the protruding regions of proteins. EMBO J. 1986 Feb;5(2):409–413. doi: 10.1002/j.1460-2075.1986.tb04226.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- 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]
- Wang S. P., Grayston J. T. Immunologic relationship between genital TRIC, lymphogranuloma venereum, and related organisms in a new microtiter indirect immunofluorescence test. Am J Ophthalmol. 1970 Sep;70(3):367–374. doi: 10.1016/0002-9394(70)90096-6. [DOI] [PubMed] [Google Scholar]
- Wang S. P., Kuo C. C., Barnes R. C., Stephens R. S., Grayston J. T. Immunotyping of Chlamydia trachomatis with monoclonal antibodies. J Infect Dis. 1985 Oct;152(4):791–800. doi: 10.1093/infdis/152.4.791. [DOI] [PubMed] [Google Scholar]
- Woolridge R. L., Grayston J. T., Chang I. H., Yang C. Y., Cheng K. H. Long-term follow-up of the initial (1959-1960) trachoma vaccine field trial on Taiwan. Am J Ophthalmol. 1967 May;63(5 Suppl):1650–1655. doi: 10.1016/0002-9394(67)94159-1. [DOI] [PubMed] [Google Scholar]
- Young R. A., Davis R. W. Efficient isolation of genes by using antibody probes. Proc Natl Acad Sci U S A. 1983 Mar;80(5):1194–1198. doi: 10.1073/pnas.80.5.1194. [DOI] [PMC free article] [PubMed] [Google Scholar]