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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Camacho, Luis R. Yun, Chang-soo Williams, Kerstin J. Schnappinger, Dirk Tahlan, Kapil Pethe, Kevin Ehrt, Sabine Xu, Xia Dowd, Cynthia S. Park, Tae-ho Boshoff, Helena I. M. Barry, Clifton E. |
| Description | Author Affiliation: Boshoff HI ( Tuberculosis Research Section, Laboratory of Clinical Infectious Diseases, NIAID, National Institutes of Health, Bethesda, Maryland 20892, USA. HBOSHOFF@niaid.nih.gov) |
| Abstract | Despite the presence of genes that apparently encode NAD salvage-specific enzymes in its genome, it has been previously thought that Mycobacterium tuberculosis can only synthesize NAD de novo. Transcriptional analysis of the de novo synthesis and putative salvage pathway genes revealed an up-regulation of the salvage pathway genes in vivo and in vitro under conditions of hypoxia. [14C]Nicotinamide incorporation assays in M. tuberculosis isolated directly from the lungs of infected mice or from infected macrophages revealed that incorporation of exogenous nicotinamide was very efficient in in vivo-adapted cells, in contrast to cells grown aerobically in vitro. Two putative nicotinic acid phosphoribosyltransferases, PncB1 (Rv1330c) and PncB2 (Rv0573c), were examined by a combination of in vitro enzymatic activity assays and allelic exchange studies. These studies revealed that both play a role in cofactor salvage. Mutants in the de novo pathway died upon removal of exogenous nicotinamide during active replication in vitro. Cell death is induced by both cofactor starvation and disruption of cellular redox homeostasis as electron transport is impaired by limiting NAD. Inhibitors of NAD synthetase, an essential enzyme common to both recycling and de novo synthesis pathways, displayed the same bactericidal effect as sudden NAD starvation of the de novo pathway mutant in both actively growing and nonreplicating M. tuberculosis. These studies demonstrate the plasticity of the organism in maintaining NAD levels and establish that the two enzymes of the universal pathway are attractive chemotherapeutic targets for active as well as latent tuberculosis. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 28 |
| Volume Number | 283 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2008-07-11 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Genome, Bacterial Physiology Mycobacterium Tuberculosis Enzymology NAD Metabolism Pentosyltransferases Animals Homeostasis Lung Microbiology Macrophages Mice Mutation Genetics Oxidation-Reduction Transcription, Genetic Tuberculosis Research Support, N.I.H., Intramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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