This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Dussurget, O.
Right arrow Articles by Marchal, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Dussurget, O.
Right arrow Articles by Marchal, G.

 Previous Article  |  Next Article 

Infection and Immunity, January 2001, p. 529-533, Vol. 69, No. 1
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.1.529-533.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Role of Mycobacterium tuberculosis Copper-Zinc Superoxide Dismutase

Olivier Dussurget,1,* Graham Stewart,2 Olivier Neyrolles,2 Pascale Pescher,1 Douglas Young,2 and Gilles Marchal1

Unité de Physiopathologie de l'Infection, Institut Pasteur, 75724 Paris Cedex 15, France,1 and Department of Infectious Diseases and Microbiology, Imperial College School of Medicine, St. Mary's Campus, London W2 1PG, United Kingdom2

Received 10 April 2000/Returned for modification 15 May 2000/Accepted 21 September 2000

Superoxide dismutases (SODs) play an important role in protection against oxidative stress and have been shown to contribute to the pathogenicity of many bacterial species. To determine the function of the mycobacterial copper and zinc-cofactored SOD (CuZnSOD), we constructed and characterized Mycobacterium tuberculosis and Mycobacterium bovis BCG CuZnSOD null mutants. Both strains were more sensitive to superoxides and hydrogen peroxide than were their respective parental strains. The survival of M. bovis BCG in unstimulated as well as activated mouse bone marrow-derived macrophages was not affected by the loss of CuZnSOD. The survival of CuZnSOD deficient-M. tuberculosis in guinea pig tissues was comparable to that of its parental strain. These results indicate that the mycobacterial CuZnSOD is not essential for intracellular growth within macrophages and does not detectably contribute to the pathogenicity of M. tuberculosis.

* Corresponding author. Mailing address: Institut Pasteur, 28 rue du Dr Roux, 75724 Paris Cedex 15, France. Phone: 33.1.40.61.30.31. Fax: 33.1.45.68.87.06. E-mail: odussur{at}pasteur.fr.

Infection and Immunity, January 2001, p. 529-533, Vol. 69, No. 1
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.1.529-533.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Grare, M., Dailloux, M., Simon, L., Dimajo, P., Laurain, C. (2008). Efficacy of Dry Mist of Hydrogen Peroxide (DMHP) against Mycobacterium tuberculosis and use of DMHP for Routine Decontamination of Biosafety Level 3 Laboratories. J. Clin. Microbiol. 46: 2955-2958 [Abstract] [Full Text]  
  • Hall, L., Otter, J. A., Chewins, J., Wengenack, N. L. (2007). Use of Hydrogen Peroxide Vapor for Deactivation of Mycobacterium tuberculosis in a Biological Safety Cabinet and a Room. J. Clin. Microbiol. 45: 810-815 [Abstract] [Full Text]  
  • Kurtz, S., McKinnon, K. P., Runge, M. S., Ting, J. P.-Y., Braunstein, M. (2006). The SecA2 Secretion Factor of Mycobacterium tuberculosis Promotes Growth in Macrophages and Inhibits the Host Immune Response. Infect. Immun. 74: 6855-6864 [Abstract] [Full Text]  
  • Grover, A., Sharma, R. (2006). Identification and Characterization of a Major Zn(II) Resistance Determinant of Mycobacterium smegmatis.. J. Bacteriol. 188: 7026-7032 [Abstract] [Full Text]  
  • Passalacqua, K. D., Bergman, N. H., Herring-Palmer, A., Hanna, P. (2006). The Superoxide Dismutases of Bacillus anthracis Do Not Cooperatively Protect against Endogenous Superoxide Stress. J. Bacteriol. 188: 3837-3848 [Abstract] [Full Text]  
  • Karavolos, M. H., Horsburgh, M. J., Ingham, E., Foster, S. J. (2003). Role and regulation of the superoxide dismutases of Staphylococcus aureus. Microbiology 149: 2749-2758 [Abstract] [Full Text]  
  • Smith, I. (2003). Mycobacterium tuberculosis Pathogenesis and Molecular Determinants of Virulence. Clin. Microbiol. Rev. 16: 463-496 [Abstract] [Full Text]  
  • Shi, L., Jung, Y.-J., Tyagi, S., Gennaro, M. L., North, R. J. (2003). Expression of Th1-mediated immunity in mouse lungs induces a Mycobacterium tuberculosis transcription pattern characteristic of nonreplicating persistence. Proc. Natl. Acad. Sci. USA 100: 241-246 [Abstract] [Full Text]  
  • Bulatovic, V. M., Wengenack, N. L., Uhl, J. R., Hall, L., Roberts, G. D., Cockerill, F. R. III, Rusnak, F. (2002). Oxidative Stress Increases Susceptibility of Mycobacterium tuberculosis to Isoniazid. Antimicrob. Agents Chemother. 46: 2765-2771 [Abstract] [Full Text]  
  • Bong, C. T. H., Fortney, K. R., Katz, B. P., Hood, A. F., Mateo, L. R. S., Kawula, T. H., Spinola, S. M. (2002). A Superoxide Dismutase C Mutant of Haemophilus ducreyi Is Virulent in Human Volunteers. Infect. Immun. 70: 1367-1371 [Abstract] [Full Text]  
  • Sansone, A., Watson, P. R., Wallis, T. S., Langford, P. R., Kroll, J. S. (2002). The role of two periplasmic copper- and zinc-cofactored superoxide dismutases in the virulence of Salmonella choleraesuis. Microbiology 148: 719-726 [Abstract] [Full Text]  
  • EDWARDS, K. M., CYNAMON, M. H., VOLADRI, R. K. R., HAGER, C. C., DESTEFANO, M. S., THAM, K. T., LAKEY, D. L., BOCHAN, M. R., KERNODLE, D. S. (2001). Iron-cofactored Superoxide Dismutase Inhibits Host Responses to Mycobacterium tuberculosis. Am. J. Respir. Crit. Care Med. 164: 2213-2219 [Abstract] [Full Text]  
  • Tullius, M. V., Harth, G., Horwitz, M. A. (2001). High Extracellular Levels of Mycobacterium tuberculosis Glutamine Synthetase and Superoxide Dismutase in Actively Growing Cultures Are Due to High Expression and Extracellular Stability Rather than to a Protein-Specific Export Mechanism. Infect. Immun. 69: 6348-6363 [Abstract] [Full Text]  
  • Piddington, D. L., Fang, F. C., Laessig, T., Cooper, A. M., Orme, I. M., Buchmeier, N. A. (2001). Cu,Zn Superoxide Dismutase of Mycobacterium tuberculosis Contributes to Survival in Activated Macrophages That Are Generating an Oxidative Burst. Infect. Immun. 69: 4980-4987 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»