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. 1987 Oct;55(10):2378–2382. doi: 10.1128/iai.55.10.2378-2382.1987

Genes for immunodominant protein antigens are highly homologous in Mycobacterium tuberculosis, Mycobacterium africanum, and the vaccine strain Mycobacterium bovis BCG.

M C Lu 1, M H Lien 1, R E Becker 1, H C Heine 1, A M Buggs 1, D Lipovsek 1, R Gupta 1, P W Robbins 1, C M Grosskinsky 1, S C Hubbard 1, et al.
PMCID: PMC260716  PMID: 2820881

Abstract

The relatedness of immunodominant protein antigens in Mycobacterium tuberculosis, M. africanum, and M. bovis BCG was investigated by comparing the genes that encode major protein antigens in M. tuberculosis with their counterparts in the other two mycobacteria. Genes encoding homologs of M. tuberculosis major protein antigens were isolated from M. africanum and M. bovis BCG by constructing lambda gt11 recombinant DNA expression libraries and screening them with murine monoclonal antibodies and DNA probes. The antibodies were directed against four major protein antigens of M. tuberculosis with molecular masses of 71, 65, 19, and 14 kilodaltons. The isolated M. africanum and M. bovis BCG DNA clones were mapped with restriction endonucleases, and the maps of the mycobacterial genes were confirmed by Southern analysis of mycobacterial genomic DNA. The restriction maps of DNA containing the four genes in M. tuberculosis, M. africanum, and M. bovis BCG are identical, indicating that the immunodominant proteins that they encode are highly homologous in the three mycobacteria. Thus, the immunity against tuberculosis engendered by M. bovis BCG vaccination could be provided, at least in part, by the immune response to these homologous antigens.

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Selected References

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

  1. Bloom B. R., Godal T. Selective primary health care: strategies for control of disease in the developing world. V. Leprosy. Rev Infect Dis. 1983 Jul-Aug;5(4):765–780. doi: 10.1093/clinids/5.4.765. [DOI] [PubMed] [Google Scholar]
  2. Coates A. R., Hewitt J., Allen B. W., Ivanyi J., Mitchison D. A. Antigenic diversity of Mycobacterium tuberculosis and Mycobacterium bovis detected by means of monoclonal antibodies. Lancet. 1981 Jul 25;2(8239):167–169. doi: 10.1016/s0140-6736(81)90355-x. [DOI] [PubMed] [Google Scholar]
  3. Collins D. M., De Lisle G. W. DNA restriction endonuclease analysis of Mycobacterium bovis and other members of the tuberculosis complex. J Clin Microbiol. 1985 Apr;21(4):562–564. doi: 10.1128/jcm.21.4.562-564.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Collins D. M., De Lisle G. W. DNA restriction endonuclease analysis of Mycobacterium tuberculosis and Mycobacterium bovis BCG. J Gen Microbiol. 1984 Apr;130(4):1019–1021. doi: 10.1099/00221287-130-4-1019. [DOI] [PubMed] [Google Scholar]
  5. Emmrich F., Thole J., van Embden J., Kaufmann S. H. A recombinant 64 kilodalton protein of Mycobacterium bovis bacillus Calmette-Guerin specifically stimulates human T4 clones reactive to mycobacterial antigens. J Exp Med. 1986 Apr 1;163(4):1024–1029. doi: 10.1084/jem.163.4.1024. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Fine P. Leprosy and tuberculosis--an epidemiological comparison. Tubercle. 1984 Jun;65(2):137–153. doi: 10.1016/0041-3879(84)90067-9. [DOI] [PubMed] [Google Scholar]
  7. Gillis T. P., Buchanan T. M. Production and partial characterization of monoclonal antibodies to Mycobacterium leprae. Infect Immun. 1982 Jul;37(1):172–178. doi: 10.1128/iai.37.1.172-178.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Husson R. N., Young R. A. Genes for the major protein antigens of Mycobacterium tuberculosis: the etiologic agents of tuberculosis and leprosy share an immunodominant antigen. Proc Natl Acad Sci U S A. 1987 Mar;84(6):1679–1683. doi: 10.1073/pnas.84.6.1679. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kaufmann S. H., Hug E., Väth U., De Libero G. Specific lysis of Listeria monocytogenes-infected macrophages by class II-restricted L3T4+ T cells. Eur J Immunol. 1987 Feb;17(2):237–246. doi: 10.1002/eji.1830170214. [DOI] [PubMed] [Google Scholar]
  10. Lamb J. R., Ivanyi J., Rees A., Young R. A., Young D. B. The identification of T cell epitopes in Mycobacterium tuberculosis using human T lymphocyte clones. Lepr Rev. 1986 Dec;57 (Suppl 2):131–137. [PubMed] [Google Scholar]
  11. Luelmo F. BCG vaccination. Am Rev Respir Dis. 1982 Mar;125(3 Pt 2):70–72. doi: 10.1164/arrd.1982.125.3P2.70. [DOI] [PubMed] [Google Scholar]
  12. Oftung F., Mustafa A. S., Husson R., Young R. A., Godal T. Human T cell clones recognize two abundant Mycobacterium tuberculosis protein antigens expressed in Escherichia coli. J Immunol. 1987 Feb 1;138(3):927–931. [PubMed] [Google Scholar]
  13. Pitchenik A. E., Cole C., Russell B. W., Fischl M. A., Spira T. J., Snider D. E., Jr Tuberculosis, atypical mycobacteriosis, and the acquired immunodeficiency syndrome among Haitian and non-Haitian patients in south Florida. Ann Intern Med. 1984 Nov;101(5):641–645. doi: 10.7326/0003-4819-101-5-641. [DOI] [PubMed] [Google Scholar]
  14. Shinnick T. M., Sweetser D., Thole J., van Embden J., Young R. A. The etiologic agents of leprosy and tuberculosis share an immunoreactive protein antigen with the vaccine strain Mycobacterium bovis BCG. Infect Immun. 1987 Aug;55(8):1932–1935. doi: 10.1128/iai.55.8.1932-1935.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Snider D. E., Jr, Jones W. D., Good R. C. The usefulness of phage typing Mycobacterium tuberculosis isolates. Am Rev Respir Dis. 1984 Dec;130(6):1095–1099. doi: 10.1164/arrd.1984.130.6.1095. [DOI] [PubMed] [Google Scholar]
  16. Thole J. E., Dauwerse H. G., Das P. K., Groothuis D. G., Schouls L. M., van Embden J. D. Cloning of Mycobacterium bovis BCG DNA and expression of antigens in Escherichia coli. Infect Immun. 1985 Dec;50(3):800–806. doi: 10.1128/iai.50.3.800-806.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. 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]
  18. Wallace R. J., Jr, Swenson J. M., Silcox V. A., Good R. C., Tschen J. A., Stone M. S. Spectrum of disease due to rapidly growing mycobacteria. Rev Infect Dis. 1983 Jul-Aug;5(4):657–679. doi: 10.1093/clinids/5.4.657. [DOI] [PubMed] [Google Scholar]
  19. Young D. B., Kent L., Young R. A. Screening of a recombinant mycobacterial DNA library with polyclonal antiserum and molecular weight analysis of expressed antigens. Infect Immun. 1987 Jun;55(6):1421–1425. doi: 10.1128/iai.55.6.1421-1425.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Young R. A., Bloom B. R., Grosskinsky C. M., Ivanyi J., Thomas D., Davis R. W. Dissection of Mycobacterium tuberculosis antigens using recombinant DNA. Proc Natl Acad Sci U S A. 1985 May;82(9):2583–2587. doi: 10.1073/pnas.82.9.2583. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. 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]
  22. Young R. A., Davis R. W. Yeast RNA polymerase II genes: isolation with antibody probes. Science. 1983 Nov 18;222(4625):778–782. doi: 10.1126/science.6356359. [DOI] [PubMed] [Google Scholar]

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