1887

Abstract

A 36 kDa antigen of was purified by phenol biphasic partition followed by preparative SDS-PAGE. The purified antigen appeared as a single band in SDS-PAGE and eluted as a single peak in ion-exchange chromatography. The antigen comprised epitopes which were cross-reactive with , as well as a species-specific epitope (recognized by MAb F47–9). Different treatments of the 36 kDa antigen suggested it to be largely protein in nature; the amino acid composition of 81% of the antigen was determined. A majority of sera from leprosy patients contained antibodies recognizing the 36 kDa antigen.

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1988-06-01
2021-05-12
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References

  1. Britton W. J., Hellqvist L., Basten A., Raison R. L. 1985; Mycobacterium leprae antigens involved in human immune responses. I. Identification of four antigens by monoclonal antibodies. Journal of Immunology 135:4171–4177
    [Google Scholar]
  2. Chakrabarty A. K., Maire M. A., Lambert P. H. 1982; SDS-PAGE analysis of M. leprae protein antigens reacting with antibodies from sera from lepromatous patients and infected armadillos. Clinical and Experimental Immunology 49:523–531
    [Google Scholar]
  3. Cho S. N., Yanagihara D. L., Hunter S. W., Gelber R. H., Brennan P. J. 1983; Serological specificity of phenolic glycoliμld I from M. lepraeand use in serodiagnosis of leprosy. Infection and Immunity 41:1077–1083
    [Google Scholar]
  4. Douglas J. T., Steven L. M., Cellona R. V., Fajardo T., Abalos R. M., Madarang M. G. 1987; Serological reactivity among contacts of lepromatous patients in Cebu Philippines. Abstracts of the US-Japan Leprosy Research Meeting20–22July 1987
    [Google Scholar]
  5. Edge A. S. B., Faltynek C. R., Hof L., Reichert L. E. Jr Weber P. 1981; Deglycosylation of glycoproteins by trifluoromethane-sulfonic acid. Analytical Biochemistry 118:131–137
    [Google Scholar]
  6. Engers H. D., Abe M., Bloom B. R., Mehra V., Britton W., Buchanan T. M., Khanolkar S. R., Young D. B., Closs O., Gillis T., Harboe M., Ivanyi J., Kolk A. H. J., Shepard C. C. 1985; Result of a World Health Organisation-sponsored workshop on monoclonal antibodies to M. leprae. Infection and Immunity 48:603–605
    [Google Scholar]
  7. GÖrg A., Postel W., Weser J., GÜnther S., Strahler J. R., Hanash S. M., Somerlot L. 1987; Elimination of point streaking on silver stained two-dimensional gels by the addition of iodoacetamide to the equilibration buffer. Electrophoresis 8:122–124
    [Google Scholar]
  8. Hunter S. W., Gaylord H., Brennan P. J. 1986; Structure and antigenicity of the phosphorylated lipopolysaccharide antigens from the leprosy and tubercle bacilli. Journal of Biological Chemistry 261:12345–12351
    [Google Scholar]
  9. Ivanyi J., Sinha S., Aston R., Cussell D., Keen M., Sengupta U. 1983; Definition of species- specific and cross-reactive antigenic determinants of Mycobacterium leprae using monoclonal antibodies. Clinical and Experimental Immunology 52:528–536
    [Google Scholar]
  10. Klatser P. R., Van Rens M. M., Eggelte T. A. 1984; Immunochemical characterization of Mycobacterium leprae antigens by the SDS-polyacrylamide gel electrophoresis immunoperoxidase technique (SGIP) using patients’ sera. Clinical and Experimental Immunology 56:537–544
    [Google Scholar]
  11. Klatser P. R., De Wit M. Y. L., Kolk A. H. J. 1985; An ELISA-inhibition test using monoclonal antibody for the serology of leprosy. Clinical and Experimental Immunology 62:468–473
    [Google Scholar]
  12. Klatser P. R., Hartskeerl R. A., Van Schooten W. C. A., Kolk A. H. J., Van Rens M. M., De Wit M. Y. L. 1987; Characterization of the 36 K antigen of M. leprae. Leprosy Review 57: (supplement 2) 77–81
    [Google Scholar]
  13. Kolk A. H. J., Ho M. L., Klatser P. R., Eggelte T. A., Kuijper S., De Jonge S., Van Leeuwen J. 1984; Production and characterization of monoclonal antibodies to Mycobacterium tuberculosis, M. bovis (BCG) and M. leprae. Clinical and Experimental Immunology 58:511–521
    [Google Scholar]
  14. Laemmli U. K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature; London: 226680–685
    [Google Scholar]
  15. Ottenhoff T. H. M., Klatser P. R., Ivanyi J., Elferink D. G., De Wit M. Y. L., De Vries R. R. P. 1986a; Mycobacterium leprae-specific protein antigens defined by cloned human helper T cells. Nature; London: 31966–68
    [Google Scholar]
  16. Ottenhoff T. H. M., Elferink D. G., Klatser P. R., De Vries R. R. P. 1986b; Cloned suppressor T-cells from a lepromatous leprosy patient suppress Mycobacterium leprae reactive helper T cells. Nature; London: 322:462–467
    [Google Scholar]
  17. Ridley D. S., Jopling W. H. 1966; Classification of leprosy according to immunity, a five-group system. International Journal of Leprosy 34:255–273
    [Google Scholar]
  18. Tsai C. M., Frasch E. 1982; A sensitive silver stain for detecting lipopolysaccharides in polyacrylamide gels. Analytical Biochemistry 119:115–119
    [Google Scholar]
  19. Vennegoor C., Calafat J., Hageman PH., Van Buitenen F., Janssen H., Kolk A., RÜmke PH. 1985; Biochemical characterization and cellular localization of a formalin-resistant melanoma-associated antigen reacting with monoclonal antibody NKI/C-3. International Journal of Cancer 35:287–295
    [Google Scholar]
  20. Weber K., Pringle J. R., Osborn M. 1972; Measurement of molecular weights by electrophoresis on SDS-acrylamide gel. Methods in Enzymology 26:3–27
    [Google Scholar]
  21. Westphal O., Jann K. 1965 In Methods in Carbohydrate Chemistry pp. 83–91 Whistler R. L. Edited by New York: Academic Press;
    [Google Scholar]
  22. World Health Organization 1980; Purification of M. leprae. Report of the Fifth Meeting of the Scientific Working Group on the Immunology of Leprosy (IMMLEP). TDR/IMMLEP-SWG (5)/80·3. Geneva:: WHO;
  23. Young R. A., Mehra V., Sweetser D., Buchanan T., Clark-Curtiss J., Davis R. W., Bloom B. R. 1985; Genes for the major protein antigens of Mycobacterium leprae. Nature; London: 316450–452
    [Google Scholar]
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