ArticleAntimicrobial agents and chemotherapy2012
Amino acid substitutions at position 95 in GyrA can add fluoroquinolone resistance to Mycobacterium leprae.
Article in Antimicrobial agents and chemotherapy, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 28 citations in OpenAlex.
- Characterization of DNA Gyrase Activity and Elucidation of the Impact of Amino Acid Substitution in GyrA on Fluoroquinolone Resistance in Mycobacterium avium.Microbiology spectrum · 2023Article
- Molecular Characterization of Mycobacterium ulcerans DNA Gyrase and Identification of Mutations Reducing Susceptibility to QuinolonesAntimicrobial agents and chemotherapy · 2022Article
- DNA gyrase could be a crucial regulatory factor for growth and survival of Mycobacterium leprae.Scientific reports · 2019Article
- DC-159a Shows Inhibitory Activity against DNA Gyrases of Mycobacterium leprae.PLoS neglected tropical diseases · 2016Article
- Resistance of M. leprae to quinolones: a question of relativity?PLoS neglected tropical diseases · 2013Article
- Impact of amino acid substitutions in B subunit of DNA gyrase in Mycobacterium leprae on fluoroquinolone resistance.PLoS neglected tropical diseases · 2012Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
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Abstract
Amino acid substitutions at position 89 or 91 in GyrA of fluoroquinolone-resistant Mycobacterium leprae clinical isolates have been reported. In contrast, those at position 94 in M. tuberculosis, equivalent to position 95 in M. leprae, have been identified most frequently. To verify the possible contribution of amino acid substitutions at position 95 in M. leprae to fluoroquinolone resistance, we conducted an in vitro assay using wild-type and mutant recombinant DNA gyrases. Fluoroquinolone-mediated supercoiling activity inhibition assay and DNA cleavage assay revealed the potent contribution of an amino acid substitution of Asp to Gly or Asn at position 95 to fluoroquinolone resistance. These results suggested the possible future emergence of quinolone-resistant M. leprae isolates with these amino acid substitutions and the usefulness of detecting these mutations for the rapid identification of fluoroquinolone resistance in leprosy.
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