Identification of katG mutations associated with high-level isoniazid resistance in Mycobacterium tuberculosis.
Hiroki Ando, Yuji Kondo, Toshinori Suetake, Emiko Toyota, Seiya Kato, Toru Mori, Teruo Kirikae
Author Information
Hiroki Ando: Department of Infectious Diseases, Research Institute, International Medical Center of Japan, Tokyo, Japan.
Isoniazid (INH) is an effective first-line antituberculosis drug. KatG, a catalase-peroxidase, converts INH to an active form in Mycobacterium tuberculosis, and katG mutations are major causes of INH resistance. In the present study, we sequenced katG of 108 INH-resistant M. tuberculosis clinical isolates. Consequently, 9 novel KatG mutants with a single-amino-acid substitution were found. All of these mutants had significantly lower INH oxidase activities than the wild type, and each mutant showed various levels of activity. Isolates having mutations with relatively low activities showed high-level INH resistance. On the basis of our results and known mutations associated with INH resistance, we developed a new hybridization-based line probe assay for rapid detection of INH-resistant M. tuberculosis isolates.
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Amino Acid Substitution
Antitubercular Agents
Bacterial Proteins
Catalase
Drug Resistance, Bacterial
Escherichia coli
Genetic Testing
Humans
Isoniazid
Microbiological Techniques
Mycobacterium tuberculosis
Oligonucleotide Probes
Plasmids
Point Mutation
Polymorphism, Restriction Fragment Length
Tuberculosis, Pulmonary
Antitubercular Agents
Bacterial Proteins
Oligonucleotide Probes
Catalase
katG protein, Mycobacterium tuberculosis
Isoniazid
