Genetic Evidence that InhA of Mycobacterium smegmatis Is a Target for Triclosan
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چکیده
منابع مشابه
Biochemical and genetic data suggest that InhA is not the primary target for activated isoniazid in Mycobacterium tuberculosis.
An examination of the pattern of lipid biosynthetic responses to isoniazid (INH) treatment of Mycobacterium tuberculosis and Mycobacterium smegmatis suggests that the mode of action of activated INH differs between these 2 organisms. Transformation of M. smegmatis with inhA on a plasmid construct conferred high-level resistance to INH, while the same construct failed to confer resistance upon M...
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Mycobacterium smegmatis PTCC 1307 (CIP 73.26) was used as a microbial agent to produce androsta-1,4-diene-3,17-dione (ADD) and androst-4-ene-3,17-dione, two useful precursors in the synthesis of steroid drugs. The side chain of cholesterol, as the substrate, was selectively cleaved in the presence of five enzyme inhibitors. An intermediate structure with intact side chain, cholest-4-ene-3-one, ...
متن کاملInhibition of InhA, the enoyl reductase from Mycobacterium tuberculosis, by triclosan and isoniazid.
Structural and genetic studies indicate that the antibacterial compound triclosan, an additive in many personal care products, is an inhibitor of EnvM, the enoyl reductase from Escherichia coli. Here we show that triclosan specifically inhibits InhA, the enoyl reductase from Mycobacterium tuberculosis and a target for the antitubercular drug isoniazid. Binding of triclosan to wild-type InhA is ...
متن کاملinhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis.
Isoniazid (isonicotinic acid hydrazide, INH) is one of the most widely used antituberculosis drugs, yet its precise target of action on Mycobacterium tuberculosis is unknown. A missense mutation within the mycobacterial inhA gene was shown to confer resistance to both INH and ethionamide (ETH) in M. smegmatis and in M. bovis. The wild-type inhA gene also conferred INH and ETH resistance when tr...
متن کاملCharacterization of a Mycobacterium smegmatis mutant that is simultaneously resistant to D-cycloserine and vancomycin.
A mutant of Mycobacterium smegmatis has been isolated that is simultaneously resistant to both D-cycloserine (D-CS) and vancomycin. Genetic complementation with a PBP4 homolog restores sensitivity to both drugs. Resistance to D-CS and vancomycin in this mutant is most likely due to a novel mechanism involving peptidoglycan assembly at the cell surface.
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ژورنال
عنوان ژورنال: Antimicrobial Agents and Chemotherapy
سال: 1999
ISSN: 0066-4804,1098-6596
DOI: 10.1128/aac.43.3.711