4.5 Article

Glutathione disulfide and S-nitrosoglutathione detoxification by Mycobacterium tuberculosis thioredoxin system

Journal

FEBS LETTERS
Volume 583, Issue 19, Pages 3215-3220

Publisher

WILEY
DOI: 10.1016/j.febslet.2009.09.007

Keywords

Mycobacteria; Tuberculosis; Thioredoxin; Glutathione; S-nitrosoglutathione; Mycothiol

Funding

  1. TB VETS Charitable foundation
  2. Pacific Century Graduate Scholarship
  3. University of British Columbia Graduate Fellowship

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Mycobacterium tuberculosis resides within alveolar macrophages. These phagocytes produce reactive nitrogen and oxygen intermediates to combat the invading pathogens. The macrophage glutathione (GSH) pool reduces nitric oxide (NO) to S-nitrosoglutathione (GSNO). Both glutathione disulfide (GSSG) and GSNO possess mycobactericidal activities in vitro. In this study we demonstrate that M. tuberculosis thioredoxin system, comprises of thioredoxin reductase B2 and thioredoxin C reduces the oxidized form of the intracellular mycothiol (MSSM) and is able to efficiently reduce GSSG and GSNO in vitro. Our study suggests that the thioredoxin system provide a general reduction mechanism to cope with oxidative stress associated with the microbe's metabolism as well as to detoxify xenobiotics produced by the host. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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