The genetics and biochemistry of isoniazid resistance in mycobacterium tuberculosis

Microbes Infect. 2000 May;2(6):659-69. doi: 10.1016/s1286-4579(00)00359-2.

Abstract

Although the primary targets of activated isoniazid (INH) are proteins involved in the biosynthesis of cell wall mycolic acids, clinical resistance is dominated by specific point mutations in katG. Mutations associated with target mutations contribute to, but still cannot completely explain, resistance to INH. Despite the wealth of genetic information currently available, the molecular mechanism of cell death induced by INH remains elusive.

Publication types

  • Review

MeSH terms

  • Antitubercular Agents / chemistry
  • Antitubercular Agents / pharmacology*
  • Bacterial Proteins*
  • Drug Resistance, Microbial / genetics
  • Humans
  • Isoniazid / chemistry
  • Isoniazid / pharmacology*
  • Mutation
  • Mycobacterium tuberculosis / drug effects*
  • Mycobacterium tuberculosis / enzymology
  • Mycobacterium tuberculosis / genetics*
  • Peroxidases / genetics
  • Peroxidases / metabolism
  • Tuberculosis, Pulmonary / microbiology

Substances

  • Antitubercular Agents
  • Bacterial Proteins
  • Peroxidases
  • catalase HPI
  • Isoniazid