Functional Analysis of Dna Gyrase Mutant Enzymes Carrying Mutations at Position 88 in the A Subunit Found in Clinical Strains of Mycobacterium Tuberculosis Resistant to Fluoroquinolones.
From: Laboratoire de Bactériologie, Centre National de Référence des Mycobactéries et de la Résistance des Mycobactéries aux Antituberculeux, site Pitié-Salpêtrière, Université Paris 6, Assistance Publique-Hôpitaux de Paris, Paris, France.
Antimicrobial agents and chemotherapy
- Publish Date: Dec 2006
- ISSN: 0066-4804
- Volume: 50
- Issue: 12
- Pages: 4170-3
- Medium: Print
- Language: English
- Citation (JAMA): Matrat Stéphanie, Veziris Nicolas, Mayer Claudine, et al. Functional Analysis of Dna Gyrase Mutant Enzymes Carrying Mutations at Position 88 in the A Subunit Found in Clinical Strains of Mycobacterium Tuberculosis Resistant to Fluoroquinolones.. Antimicrob. Agents Chemother. Dec 2006;50:4170-3
Abstract
We investigated the enzymatic efficiency and inhibition by quinolones of Mycobacterium tuberculosis DNA gyrases carrying the previously described GyrA G88C mutation and the novel GyrA G88A mutation harbored by two multidrug-resistant clinical strains and reproduced by site-directed mutagenesis. Fluoroquinolone MICs and 50% inhibitory concentrations for both mutants were 2- to 43-fold higher than for the wild type, demonstrating that these mutations confer fluoroquinolone resistance in M. tuberculosis.
Mesh Headings (Keywords): Antitubercular Agents, Binding Sites, DNA Gyrase, Drug Resistance, Bacterial, Fluoroquinolones, Humans, Microbial Sensitivity Tests, Models, Molecular, Mutagenesis, Site-Directed, Mutation, Mycobacterium tuberculosis, Protein Structure, Tertiary
Check for Full Text / PubMed Unique Identifier (PMID): 17015625
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