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Lipid biochemistry takes a stand against tuberculosis

Nature Medicine volume 6, pages 977–978 (2000)Cite this article

Although several excellent drugs are available to treat tuberculosis, their mechanisms are not well understood. Identification of the target of the tuberculosis drug pyrazinamide underscores the role that lipids play in disease pathogenesis, and reveals new avenues for drug design (pages 1043–1047).

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Figure 1: Fatty acid synthesis in mycobacteria.

References

  1. Zimhony, O., Cox, J.S., Welch, J.T., Vilchèze C. & Jacobs, W.R., Jr. Pyrazinamide inhibits the eukaryotic like fatty acid synthetase I (FASI) of Mycobacterium tuberculosis. Nature Med. 6, 1043–1047 (2000).

    Article  CAS  Google Scholar 

  2. Cole, S.T. et al. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393, 537–544 (1998).

    Article  CAS  Google Scholar 

  3. Bloch, K. Control mechanisms for fatty acid synthesis in Mycobacterium smegmatis . Adv. Enzymol. 45, 1– 84 (1977).

    CAS  PubMed  Google Scholar 

  4. Brennan, P.J. & Nikaido, H. The envelope of mycobacteria. Annu. Rev. Biochem. 64, 29–63 (1995).

    Article  CAS  Google Scholar 

  5. Banerjee, A. et al. inhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis. Science 263, 227–230 (1994).

    Article  CAS  Google Scholar 

  6. Marrakchi, H., Lanéelle, G. & Quémard, A. InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II . Microbiology 146, 289– 296 (2000).

    Article  CAS  Google Scholar 

  7. Mduli, K. et al. Inhibition of a Mycobacterium tuberculosis beta-ketoacyl ACP synthase by isoniazid. Science 280, 1607–1610 (1998).

    Article  Google Scholar 

  8. Cox, J.S., Chen, B., McNeil, M. & Jacobs, W.R., Jr. Complex lipid determines tissue-specific replication of Mycobacterium tuberculosis in mice. Nature 402, 79– 83 (1999).

    Article  CAS  Google Scholar 

  9. Recht, J., Martinez, A., Torello, S. and Kolter, R. Genetic analysis of sliding mobility in Mycobacterium smegmatis. J. Bacteriol. 182, 4348–4351 (2000).

    Article  CAS  Google Scholar 

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  1. National Institute for Medical Research, Mill Hill, NW7 1AA, London, UK

    Philip Draper

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  1. Philip Draper
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Draper, P. Lipid biochemistry takes a stand against tuberculosis. Nat Med 6, 977–978 (2000). https://doi.org/10.1038/79670

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