On the catalase-peroxidase gene, katG, of Mycobacterium leprae and the implications for treatment of leprosy with isoniazid
Autor: | Beate Heym, Stewart T. Cole, Karin Eiglmeier, Hafida Fsihi |
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Rok vydání: | 2006 |
Předmět: |
Pseudogene
Molecular Sequence Data Antitubercular Agents Microbiology law.invention Bacterial Proteins law Leprosy Isoniazid Genetics medicine Cloning Molecular Molecular Biology Mycobacterium leprae Gene Catalase-peroxidase Polymerase chain reaction Sequence Homology Amino Acid biology Mycobacterium smegmatis biochemical phenomena metabolism and nutrition Cosmids bacterial infections and mycoses biology.organism_classification medicine.disease Peroxidases Genes Bacterial Pseudogenes medicine.drug |
Zdroj: | FEMS Microbiology Letters. 149:273-278 |
ISSN: | 0378-1097 |
Popis: | The toxicity of the potent tuberculocidal agent, isoniazid, is mediated by the heme-containing enzyme, catalase-peroxidase, encoded by the katG gene. Although isoniazid has been used for the treatment of leprosy, it is shown here that the katG gene of Mycobacterium leprae is a pseudogene, which has probably been inactivated by multiple mutations. Inactive genes were detected by the polymerase chain reaction in several isolates of M. leprae, of different geographical origins, and attempts to complement an isoniazid-resistant strain of Mycobacterium smegmatis with the katG pseudogene were unsuccessful. Isoniazid is thus likely to be of no therapeutic benefit to leprosy patients. |
Databáze: | OpenAIRE |
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