Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1987 Sep;169(9):3879–3885. doi: 10.1128/jb.169.9.3879-3885.1987

Diversity of Chlamydia trachomatis major outer membrane protein genes.

R S Stephens, R Sanchez-Pescador, E A Wagar, C Inouye, M S Urdea
PMCID: PMC213681  PMID: 3040664

Abstract

Genomic DNA libraries were constructed for Chlamydia trachomatis serovars B and C by using BamHI fragments, and recombinants that contained the major outer membrane protein (omp1) gene for each serovar were identified and sequenced. Comparisons between these gene sequences and the gene from serovar L2 demonstrated fewer base pair differences between serovars L2 and B than between L2 and C; this finding is consistent with the serologic and antigenic relationships among these serovars. The translated amino acid sequence for the major outer membrane proteins (MOMPs) contained the same number of amino acids for serovars L2 and B, whereas the serovar C MOMP contained three additional amino acids. The antigenic diversity of the chlamydial MOMP was reflected in four sequence-variable domains, and two of these domains were candidates for the putative type-specific antigenic determinant. The molecular basis of omp1 gene diversity among C. trachomatis serovars was observed to be clustered nucleotide substitutions for closely related serovars and insertions or deletions for distantly related serovars.

Full text

PDF
3879

Selected References

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

  1. Barbour A. G., Amano K., Hackstadt T., Perry L., Caldwell H. D. Chlamydia trachomatis has penicillin-binding proteins but not detectable muramic acid. J Bacteriol. 1982 Jul;151(1):420–428. doi: 10.1128/jb.151.1.420-428.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. 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]
  3. 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]
  4. 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]
  5. Chang J. J., Leonard K., Arad T., Pitt T., Zhang Y. X., Zhang L. H. Structural studies of the outer envelope of Chlamydia trachomatis by electron microscopy. J Mol Biol. 1982 Nov 15;161(4):579–590. doi: 10.1016/0022-2836(82)90409-0. [DOI] [PubMed] [Google Scholar]
  6. Chen R., Krämer C., Schmidmayr W., Henning U. Primary structure of major outer membrane protein I of Escherichia coli B/r. Proc Natl Acad Sci U S A. 1979 Oct;76(10):5014–5017. doi: 10.1073/pnas.76.10.5014. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. 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]
  8. 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]
  9. 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]
  10. Karn J., Brenner S., Barnett L., Cesareni G. Novel bacteriophage lambda cloning vector. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5172–5176. doi: 10.1073/pnas.77.9.5172. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Messing J. New M13 vectors for cloning. Methods Enzymol. 1983;101:20–78. doi: 10.1016/0076-6879(83)01005-8. [DOI] [PubMed] [Google Scholar]
  12. Nano F. E., Barstad P. A., Mayer L. W., Coligan J. E., Caldwell H. D. Partial amino acid sequence and molecular cloning of the encoding gene for the major outer membrane protein of Chlamydia trachomatis. Infect Immun. 1985 May;48(2):372–377. doi: 10.1128/iai.48.2.372-377.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Newhall W. J., Batteiger B., Jones R. B. Analysis of the human serological response to proteins of Chlamydia trachomatis. Infect Immun. 1982 Dec;38(3):1181–1189. doi: 10.1128/iai.38.3.1181-1189.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. 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]
  15. Osborn M. J., Wu H. C. Proteins of the outer membrane of gram-negative bacteria. Annu Rev Microbiol. 1980;34:369–422. doi: 10.1146/annurev.mi.34.100180.002101. [DOI] [PubMed] [Google Scholar]
  16. Perlman D., Halvorson H. O. A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptides. J Mol Biol. 1983 Jun 25;167(2):391–409. doi: 10.1016/s0022-2836(83)80341-6. [DOI] [PubMed] [Google Scholar]
  17. 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]
  18. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Schachter J., Caldwell H. D. Chlamydiae. Annu Rev Microbiol. 1980;34:285–309. doi: 10.1146/annurev.mi.34.100180.001441. [DOI] [PubMed] [Google Scholar]
  20. Shine J., Dalgarno L. The 3'-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. Proc Natl Acad Sci U S A. 1974 Apr;71(4):1342–1346. doi: 10.1073/pnas.71.4.1342. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. 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]
  22. 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]
  23. 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]
  24. 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]
  25. 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]
  26. Warner B. D., Warner M. E., Karns G. A., Ku L., Brown-Shimer S., Urdea M. S. Construction and evaluation of an instrument for the automated synthesis of oligodeoxyribonucleotides. DNA. 1984 Oct;3(5):401–411. doi: 10.1089/dna.1984.3.401. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES