ArticleAntimicrobial agents and chemotherapy2007
Expression and purification of an active form of the Mycobacterium leprae DNA gyrase and its inhibition by quinolones.
Article in Antimicrobial agents and chemotherapy, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 26 citations in OpenAlex.
- Treatment and Evaluation Advances in Leprosy Neuropathy.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2021Review
- DC-159a Shows Inhibitory Activity against DNA Gyrases of Mycobacterium leprae.PLoS neglected tropical diseases · 2016Article
- DNA topoisomerase VIII: a novel subfamily of type IIB topoisomerases encoded by free or integrated plasmids in Archaea and Bacteria.Nucleic acids research · 2014Article
- Resistance of M. leprae to quinolones: a question of relativity?PLoS neglected tropical diseases · 2013Article
- Amino acid substitutions at position 95 in GyrA can add fluoroquinolone resistance to Mycobacterium leprae.Antimicrobial agents and chemotherapy · 2012Article
- Impact of amino acid substitutions in B subunit of DNA gyrase in Mycobacterium leprae on fluoroquinolone resistance.PLoS neglected tropical diseases · 2012Article
- Are all the DNA gyrase mutations found in Mycobacterium leprae clinical strains involved in resistance to fluoroquinolones?Antimicrobial agents and chemotherapy · 2008Article
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Authors and funding
6 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycobacterium leprae, the causative agent of leprosy, is noncultivable in vitro; therefore, evaluation of antibiotic activity against M. leprae relies mainly upon the mouse footpad system, which requires at least 12 months before the results become available. We have developed an in vitro assay for studying the activities of quinolones against the DNA gyrase of M. leprae. We overexpressed in Escherichia coli the M. leprae GyrA and GyrB subunits separately as His-tagged proteins by using a pET plasmid carrying the gyrA and gyrB genes. The soluble 97.5-kDa GyrA and 74.5-kDa GyrB subunits were purified by nickel chelate chromatography and were reconstituted as an enzyme with DNA supercoiling activity. Based on the drug concentrations that inhibited DNA supercoiling by 50% or that induced DNA cleavage by 25%, the 13 quinolones tested clustered into three groups. Analysis of the quinolone structure-activity relationship demonstrates that the most active quinolones against M. leprae DNA gyrase share the following structural features: a substituted carbon at position 8, a cyclopropyl substituent at N-1, a fluorine at C-6, and a substituent ring at C-7. We conclude that the assays based on DNA supercoiling inhibition and drug-induced DNA cleavage on purified M. leprae DNA gyrase are rapid, efficient, and safe methods for the screening of quinolone derivatives with potential in vivo activities against M. leprae.
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