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Rusnak, Frank

A5113688941 | I100633361

Mayo Clinic

University of Massachusetts Dartmouth

Citations 25

Oxidative Stress Increases Susceptibility of Mycobacterium tuberculosis to Isoniazid

Antimicrobial Agents and Chemotherapy | October 1, 2002 | Volume: 46 | Issue: 9 | Pages: 2765-2771

10.1128/aac.46.9.2765-2771.2002 | PMID 12183226

ABSTRACT Isoniazid is a first-line antibiotic used in the treatment of infections caused by Mycobacterium tuberculosis . Isoniazid is a prodrug requiring oxidative activation by the catalase-peroxidase hemoprotein, KatG. Resistance to isoniazid can be obtained by point mutations in the katG gene, with one of the most common being a threonine-for-serine substitution at position 315 (S315T). The S315T mutation is found in more than 50% of isoniazid-resistant clinical isolates and results in an ≈200-fold increase in the MIC of isoniazid compared to that for M. tuberculosis H37Rv. In the present study we investigated the hypothesis that superoxide plays a role in KatG-mediated isoniazid activation. Plumbagin and clofazimine, compounds capable of generating superoxide anion, resulted in a lower MIC of isoniazid for M. tuberculosis H37Rv and a strain carrying the S315T mutation. These agents did not cause as great of an increase in isoniazid susceptibility in the mutant strain when the susceptibilities were assessed by using the inhibitory concentration that causes a 50% decrease in growth. These results provide evidence that superoxide can play a role in isoniazid activation. Since clofazimine alone has antitubercular activity, the observation of synergism between clofazimine and isoniazid raises the interesting possibility of using both drugs in combination to treat M. tuberculosis infections.
Structure of the Bacteriophage λ Ser/Thr Protein Phosphatase with Sulfate Ion Bound in Two Coordination Modes,

Biochemistry | July 26, 2002 | Volume: 39 | Issue: 50 | Pages: 15365-15374

10.1021/bi0021030 | PMID 11112522

Purification, Characterization, and Preliminary Crystallographic Study of Copper-Containing Nitrous Oxide Reductase fromPseudomonas nautica617

Biochemistry | July 26, 2002 | Volume: 39 | Issue: 14 | Pages: 3899-3907

10.1021/bi9926328 | PMID 10747777

Spectroscopic Comparison of the Heme Active Sites in WT KatG and Its S315T Mutant

Biochemistry | July 26, 2002 | Volume: 39 | Issue: 32 | Pages: 9984-9993

10.1021/bi0006870 | PMID 10933819

Isoniazid Oxidation by Mycobacterium tuberculosis KatG:  A Role for Superoxide Which Correlates with Isoniazid Susceptibility

Journal of the American Chemical Society | July 26, 2002 | Volume: 121 | Issue: 41 | Pages: 9748-9749

10.1021/ja992590a

Binding of 15N-Labeled Isoniazid to KatG and KatG(S315T):  Use of Two-Spin [zz]-Order Relaxation Rate for 15N−Fe Distance Determination

Journal of the American Chemical Society | July 26, 2002 | Volume: 121 | Issue: 47 | Pages: 10962-10966

10.1021/ja9918674

The Transition State of the Phosphoryl-Transfer Reaction Catalyzed by the Lambda Ser/Thr Protein Phosphatase

Journal of the American Chemical Society | July 26, 2002 | Volume: 121 | Issue: 27 | Pages: 6382-6390

10.1021/ja990667p

Interaction of Bacteriophage λ Protein Phosphatase with Mn(II):  Evidence for the Formation of a [Mn(II)]2 Cluster

Biochemistry | July 26, 2002 | Volume: 38 | Issue: 21 | Pages: 6943-6952

10.1021/bi982606u | PMID 10346916

Evidence for Differential Binding of Isoniazid byMycobacteriumtuberculosisKatG and the Isoniazid-Resistant Mutant KatG(S315T)

Biochemistry | July 26, 2002 | Volume: 37 | Issue: 45 | Pages: 15825-15834

10.1021/bi982023k | PMID 9843388

Determinants of Calcineurin Binding to Model Membranes

Biochemistry | July 26, 2002 | Volume: 36 | Issue: 44 | Pages: 13579-13585

10.1021/bi9716027 | PMID 9354626