1887

Abstract

The activation of catalase genes in response to oxidative stress may contribute to the intracellular survival of mycobacteria. In this report, the nucleotide sequence of a mycobacterial catalase gene is described. The deduced protein sequence of this gene (M185) was 60% identical to the hydroperoxidase I (HPI) protein, 59% identical to the (HPI) catalase, and 47% identical to a peroxidase. The M185 protein, expressed in , has also been shown to have peroxidase and catalase activities. Furthermore, Southern blot hybridizations, which demonstrated that a M185 gene probe hybridizes with chromosomal DNA from thirteen different strains of mycobacteria, suggest that this catalase-peroxidase gene is prevalent in the mycobacterial genus. The availability of catalase gene probes should permit an evaluation, at the molecular level, of the role of catalase in mycobacterial pathogenesis.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-138-11-2363
1992-11-01
2024-05-04
Loading full text...

Full text loading...

/deliver/fulltext/micro/138/11/mic-138-11-2363.html?itemId=/content/journal/micro/10.1099/00221287-138-11-2363&mimeType=html&fmt=ahah

References

  1. Beaman L., Beaman B. L. 1984; The role of oxygen and its derivatives in microbial pathogenesis and host defense. Annual Review of Microbiology 38:127–148
    [Google Scholar]
  2. Beers R. F., Sizer I. W. 1952; A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. Journal of Biological Chemistry 195:133–140
    [Google Scholar]
  3. Bloom B. R., Godal T. 1983; Selective primary stategies for control of disease in the developing world. Reviews of Irifectious Diseases 5:765
    [Google Scholar]
  4. Christman M. F., Morgan R. W., Jacobson F. S., AMES B. N. 1985; Positive control of a regulon for defenses against oxidative stress and some heat shock proteins in Salmonella typhimurium. Cell 41:753–762
    [Google Scholar]
  5. Collins M. E., Patki A., Wall S., Nolan S. A., Goodjer J., Woodward M. J., Dale J. W. 1990; Cloning and characterization of the gene for the ’19 kDa’ antigen of Mycobacterium bovis. Journal of General Microbiology 136:1429–1436
    [Google Scholar]
  6. Devereux J., Haerberli P., Smithies O. 1984; A comprehensive set of sequence analysis programs for VAX. Nucleic Acids Research 12:387–395
    [Google Scholar]
  7. Diaz G. A., Wayne L. G. 1974; Isolation and characterization of catalase produced by Mycobacterium tuberculosis. American Review of Respiratory Disease 110:312–319
    [Google Scholar]
  8. Gangadhram P.R. J. 1984 Drug resistance in mycobacteria. Boca Raton: CRC Press, Inc;
    [Google Scholar]
  9. Gangadharam P. R. J., Pratt P. K. 1984; Susceptibility of Mycobacterium intracellulare to hydrogen peroxide. American Review of Respiratory Disease 130:309–311
    [Google Scholar]
  10. Gold L., Pribnow D., Schneider T., Shinedling S., Singer B., Stormo G. 1981; Translational initiation in prokaryotes. Annual Review of Microbiology 35:365–403
    [Google Scholar]
  11. Greenberg J. T., Demple B. 1989; A global response induced in Escherichia coli by redox-cycling agents overlaps with that induced by peroxide stress. Journal of Bacteriology 171:3933–3939
    [Google Scholar]
  12. Gruft H., Gaafar H. A. 1974; Multiple catalases of mycobacteria: differences in molecular weight. American Review of Respiratory Disease 110:320–323
    [Google Scholar]
  13. Horsbaugh C.R. 1991; Mycobacterium avium complex infection in the Acquired Immunodeficiency Syndrome. New England Journal of Medicine 324:1332–1338
    [Google Scholar]
  14. Jackett P. S., Aber V. R., Mitchison R. D. A., Lowrie D. B. 1981a; The contribution of hydrogen peroxide resistance to the virulence of Mycobacterium tuberculosis during the first six days after intravenous infection of normal and BCG-vaccinated guinea pigs. British Journal of Experimental Pathology 62:34–40
    [Google Scholar]
  15. Jackett P. S., Andrew P. W., Aber V. R., Lowrie D. B. 1981b; Hydrogen peroxide and superoxide release by alveolar macrophages from normal and BCG-vaccinated guinea pigs after intravenous challenge with Mycobacterium tuberculosis. British Journal of Experimental Pathology 62:419–428
    [Google Scholar]
  16. Kochi A. 1991; The global tuberculosis situation and the new contivl strategy of the world health organization. Tubercle 72:1–6
    [Google Scholar]
  17. Loewen P. C., Stauffer G. V. 1990; Nucleotide sequence of kat G of Salmonella typhimurium LT2 and characterization of its product, hydroperoxidase I. Molecular and General Genetics 224:147–151
    [Google Scholar]
  18. Loewen P. C., Swatala J., Triggs-Raine B. L. 1985; Catalase HPI and HPII in Escherichia coli are induced independently. Archives of Biochemistry and Biophysics 243:144–149
    [Google Scholar]
  19. Loprasert S., Negro S., Okada H. 1989; Cloning, nucleotide sequence and expression in Escherichia coli of Bacillus stearothermophilus peroxidase gene (perA). Journal of Bacteriology 171:4871–4875
    [Google Scholar]
  20. Lowrie D. B. 1983; The macrophage and mycobacterial infections. Transactions of the Royal Society of Tropical Medicine 77:646–655
    [Google Scholar]
  21. Matsuo K., Yamaguchi R., Yamazaki R. A., Tasaka H., Yamada T. 1988; Cloning and expression of the Mycobacterium bovis BCG gene for extracellular α antigen. Journal of Bacteriology 170:3847–3854
    [Google Scholar]
  22. Morris S. L., Rouse D. A., Hussong D., Chaparas S. D. 1988; Isolation and characterization of a recombinant Jgtl 1 bacteriophage which expresses an immunoreactive Mycobacterium intracellulare protein in Escherichia coli. Infection and Immunity 56:3026–3031
    [Google Scholar]
  23. Morris S. L., Rouse D. A., Hussong D., Chaparas S. D. 1990; Isolation and characterization of recombinant Jgtl1 bacteriophages expressing four different Mycobacterium intracellulare antigens. Infection and Immunity 58:17–20
    [Google Scholar]
  24. Nair J., Rouse D. A., Morris S. L. 1992; Nucleotide sequence analysis and serologic characterization of the Mycobacterium intracellulare homologue of the Mycobacterium tuberculosis 19 kDa antigen. Molecular Microbiology 6:1431–1439
    [Google Scholar]
  25. O’brien S., Jackett P. S., Lowrie D. B., Andrew P. W. 1991; Guinea pig alveolar macrophages kill Mycobacterium tuberculosis in vitro, but killing is independent of susceptibility to hydrogen peroxide or triggering of the respiratory burst. Microbial Pathogenesis 10:199–207
    [Google Scholar]
  26. Von Ossowski I., Mulvey M. R., Lero P.A., Borys A., Loewen P. C. 1991; Nucleotide sequence of Escherichia coli katE, which encodes catalase HPII. Journal of Bacteriology 173:514–520
    [Google Scholar]
  27. Patel B. K. R., Banerjee D. K., Butcher P. P. 1991; Extraction and characterization of mRNA from mycobacteria: implication for virulence gene identification. Journal of Microbiological Methods 13:99–111
    [Google Scholar]
  28. Rouse D. A., Morris S. L., Karpas A. B., Mackall J.C., Probst P. G., Chaparas S. D. 1991; Immunological characterization of recombinant antigens isolated from a Mycobacterium avium λgt11 expression library by using monoclonal antibody probes. Infection and Immunity 59:2595–2600
    [Google Scholar]
  29. Sambrook J., Fritsch E., Maniatis T. 1989 Molecular Cloning: a Laboratory Manual,, 2nd edn. NY: Cold Spring Harbor, Cold Spring Harbor Press;
    [Google Scholar]
  30. Shinnick T. M. 1987; The 65 kilodalton antigen of Mycobacterium tuberculosis. Journal of Bacteriology 169:1080–1088
    [Google Scholar]
  31. Shinnick T. M., Plikaytis B. B., Hyche A. D., Landingham R. M., Walker L. L. 1989; The Mycobacterium tuberculosis BCG-a protein has homology to the Escherichia coli GroES protein. Nucleic Acids Research 17:125–4
    [Google Scholar]
  32. Stover C. K., De La Cruz V. F., Fuerst T. R., Burlein J. E., Benson L.A., Bennett L. T., Bansal G. P., Young J. E., Lee M. H., Hatfull G. F., Snapper S. B., Barletta R. G., Jacobs W. R., Bloom B. R. 1991; New use of BCG for recombinant vaccines. Nature, London 351:456–460
    [Google Scholar]
  33. Tartaglia T. A., Storz G., Ames B. N. 1989; Identification and molecular analysis of oxyR-regulated promoters important for the bacterial adaption to oxidative stress. Journal of Molecular Biology 210:709–719
    [Google Scholar]
  34. Triggs-Raine B. L., Dable B. W., Mulvey M. R., Sorlez P.A., Loewen P. C. 1988; Nucleotide sequence of katG, encoding catalase HPI of Escherichia coli. Journal of Bacteriology 170:4415–4419
    [Google Scholar]
  35. Walker L., Lowrie D. B. 1981; Killing of Mycobacterium microti by immunologically activated macrophages. Nature, London 293:69–70
    [Google Scholar]
  36. Wayne L. G., Diaz G. A. 1982; Serological, taxonomic and kinetic studies of the T and M classes of mycobacterial catalases. International Journal of Systematic Bacteriology 32:296–304
    [Google Scholar]
  37. Young L. S. 1988; Mycobacterium avium complex infection. Journal of Infectious Diseases 157:863–867
    [Google Scholar]
  38. Zhang Y., Heym B., Allen B., Young D., COLE S. 1992; The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis. Nature, London 358:591–593
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-138-11-2363
Loading
/content/journal/micro/10.1099/00221287-138-11-2363
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error