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. 1989 Jul;57(7):1979–1983. doi: 10.1128/iai.57.7.1979-1983.1989

T-cell recognition of the 18-kilodalton antigen of Mycobacterium leprae.

H M Dockrell 1, N G Stoker 1, S P Lee 1, M Jackson 1, K A Grant 1, N F Jouy 1, S B Lucas 1, R Hasan 1, R Hussain 1, K P McAdam 1
PMCID: PMC313830  PMID: 2659530

Abstract

The 18-kilodalton (kDa) antigen of Mycobacterium leprae was expressed as a fusion protein with a 2-kDa leader peptide and used in proliferation assays with peripheral blood cells. Fifty percent of untreated tuberculoid leprosy patients and 93% of long-term leprosy contacts responded to the recombinant protein in lymphocyte transformation tests. Comparison of the stimulation indices in the two groups showed that the contacts responded more strongly than the tuberculoid leprosy patients. Seventy percent of Mycobacterium bovis BCG-vaccinated European donors responded, although with low stimulation indices. The isolation of 18-kDa antigen-responsive T-cell lines from a BCG-vaccinated British donor confirmed that the 18-kDa antigen contains at least one cross-reactive epitope. These results indicate that the 18-kDa protein is an important antigen in the immune response to leprosy.

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1979

Selected References

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

  1. Abe M., Minagawa F., Yoshino Y., Ozawa T., Saikawa K., Saito T. Fluorescent leprosy antibody absorption (FLA-ABS) test for detecting subclinical infection with Mycobacterium leprae. Int J Lepr Other Mycobact Dis. 1980 Jun;48(2):109–119. [PubMed] [Google Scholar]
  2. 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]
  3. Booth R. J., Harris D. P., Love J. M., Watson J. D. Antigenic proteins of Mycobacterium leprae. Complete sequence of the gene for the 18-kDa protein. J Immunol. 1988 Jan 15;140(2):597–601. [PubMed] [Google Scholar]
  4. Britton W. J., Garsia R. J., Hellqvist L., Watson J. D., Basten A. The characterization and immunoreactivity of a 70 kD protein common to Mycobacterium leprae and Mycobacterium bovis (BCG). Lepr Rev. 1986 Dec;57 (Suppl 2):67–75. [PubMed] [Google Scholar]
  5. Godal T. Growing points in leprosy research. 3. Immunological detection of sub-clinical infection in leprosy. Lepr Rev. 1974 Mar;45(1):22–30. doi: 10.5935/0305-7518.19740006. [DOI] [PubMed] [Google Scholar]
  6. Henderson L. E., Oroszlan S., Konigsberg W. A micromethod for complete removal of dodecyl sulfate from proteins by ion-pair extraction. Anal Biochem. 1979 Feb;93(1):153–157. [PubMed] [Google Scholar]
  7. 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]
  8. Klatser P. R., Hartskeerl R. A., van Schooten W. C., Kolk A. H., van Rens M. M., de Wit M. Y. Characterization of the 36 K antigen of Mycobacterium leprae. Lepr Rev. 1986 Dec;57 (Suppl 2):77–81. doi: 10.5935/0305-7518.19860057. [DOI] [PubMed] [Google Scholar]
  9. Lamb J. R., Ivanyi J., Rees A. D., Rothbard J. B., Howland K., Young R. A., Young D. B. Mapping of T cell epitopes using recombinant antigens and synthetic peptides. EMBO J. 1987 May;6(5):1245–1249. doi: 10.1002/j.1460-2075.1987.tb02360.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Lamb J. R., Rees A. D. Antigen specificity and function of human T lymphocyte clones reactive with mycobacteria. Br Med Bull. 1988 Jul;44(3):600–610. doi: 10.1093/oxfordjournals.bmb.a072270. [DOI] [PubMed] [Google Scholar]
  11. Mustafa A. S., Gill H. K., Nerland A., Britton W. J., Mehra V., Bloom B. R., Young R. A., Godal T. Human T-cell clones recognize a major M. leprae protein antigen expressed in E. coli. Nature. 1986 Jan 2;319(6048):63–66. doi: 10.1038/319063a0. [DOI] [PubMed] [Google Scholar]
  12. Mustafa A. S. Identification of T-cell-activating recombinant antigens shared among three candidate antileprosy vaccines, killed M. leprae, M. bovis BCG, and mycobacterium w. Int J Lepr Other Mycobact Dis. 1988 Jun;56(2):265–273. [PubMed] [Google Scholar]
  13. Nagao R. T., Czarnecka E., Gurley W. B., Schöffl F., Key J. L. Genes for low-molecular-weight heat shock proteins of soybeans: sequence analysis of a multigene family. Mol Cell Biol. 1985 Dec;5(12):3417–3428. doi: 10.1128/mcb.5.12.3417. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Nerland A. H., Mustafa A. S., Sweetser D., Godal T., Young R. A. A protein antigen of Mycobacterium leprae is related to a family of small heat shock proteins. J Bacteriol. 1988 Dec;170(12):5919–5921. doi: 10.1128/jb.170.12.5919-5921.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. 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]
  16. Ottenhoff T. H., Klatser P. R., Ivanyi J., Elferink D. G., de Wit M. Y., de Vries R. R. Mycobacterium leprae-specific protein antigens defined by cloned human helper T cells. Nature. 1986 Jan 2;319(6048):66–68. doi: 10.1038/319066a0. [DOI] [PubMed] [Google Scholar]
  17. Rothbard J. B., Taylor W. R. A sequence pattern common to T cell epitopes. EMBO J. 1988 Jan;7(1):93–100. doi: 10.1002/j.1460-2075.1988.tb02787.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Rüther U., Müller-Hill B. Easy identification of cDNA clones. EMBO J. 1983;2(10):1791–1794. doi: 10.1002/j.1460-2075.1983.tb01659.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Shinnick T. M., Vodkin M. H., Williams J. C. The Mycobacterium tuberculosis 65-kilodalton antigen is a heat shock protein which corresponds to common antigen and to the Escherichia coli GroEL protein. Infect Immun. 1988 Feb;56(2):446–451. doi: 10.1128/iai.56.2.446-451.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Sinigaglia F., Guttinger M., Kilgus J., Doran D. M., Matile H., Etlinger H., Trzeciak A., Gillessen D., Pink J. R. A malaria T-cell epitope recognized in association with most mouse and human MHC class II molecules. Nature. 1988 Dec 22;336(6201):778–780. doi: 10.1038/336778a0. [DOI] [PubMed] [Google Scholar]
  21. Stoker N. G., Grant K. A., Dockrell H. M., Howard C. R., Jouy N. F., McAdam K. P. High level expression of genes cloned in phage lambda gt11. Gene. 1989 May 15;78(1):93–99. doi: 10.1016/0378-1119(89)90317-x. [DOI] [PubMed] [Google Scholar]
  22. Van Schooten W. C., Ottenhoff T. H., Klatser P. R., Thole J., De Vries R. R., Kolk A. H. T cell epitopes on the 36K and 65K Mycobacterium leprae antigens defined by human T cell clones. Eur J Immunol. 1988 Jun;18(6):849–854. doi: 10.1002/eji.1830180604. [DOI] [PubMed] [Google Scholar]
  23. Young D. B., Lamb J. R. T lymphocytes respond to solid-phase antigen: a novel approach to the molecular analysis of cellular immunity. Immunology. 1986 Oct;59(2):167–171. [PMC free article] [PubMed] [Google Scholar]
  24. Young D., Lathigra R., Hendrix R., Sweetser D., Young R. A. Stress proteins are immune targets in leprosy and tuberculosis. Proc Natl Acad Sci U S A. 1988 Jun;85(12):4267–4270. doi: 10.1073/pnas.85.12.4267. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Young R. A., Mehra V., Sweetser D., Buchanan T., Clark-Curtiss J., Davis R. W., Bloom B. R. Genes for the major protein antigens of the leprosy parasite Mycobacterium leprae. Nature. 1985 Aug 1;316(6027):450–452. doi: 10.1038/316450a0. [DOI] [PubMed] [Google Scholar]

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