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Quinolone mode of action

D C Hooper1

  • 1Infectious Disease Unit, Massachusetts General Hospital, Harvard Medical School, Boston, USA.

Drugs
|January 1, 1995
PubMed
Summary

Quinolone antibiotics bind to DNA gyrase and topoisomerase IV, with mutations affecting drug binding and bacterial susceptibility. Efflux transporters also influence quinolone effectiveness in various bacteria.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Pharmacology

Background:

  • Quinolones are crucial antibiotics targeting bacterial DNA gyrase and topoisomerase IV.
  • Understanding drug-target interactions is key to combating antibiotic resistance.
  • Bacterial resistance mechanisms, including target mutations and efflux pumps, are critical areas of study.

Purpose of the Study:

  • To elucidate the binding interactions of quinolones with DNA gyrase and topoisomerase IV.
  • To investigate the impact of mutations in gyrA, gyrB, parC, and parE genes on quinolone binding and susceptibility.
  • To explore the role of efflux transporters in modulating bacterial susceptibility to quinolones.

Main Methods:

  • Physical studies of quinolone-DNA gyrase-DNA complex binding.
  • Analysis of resistance and hypersusceptibility mutations in gyrase and topoisomerase genes.
  • Examination of quinolone activity against topoisomerase IV in different bacterial species.
  • Investigation of efflux transporter systems (NorA, Emr, MexAB-OprK) and their effect on quinolone susceptibility.

Main Results:

  • Quinolones exhibit distinct binding sites on the DNA gyrase-DNA complex, with affinities influenced by gyrase mutations.
  • Mutations conferring resistance decrease quinolone binding, while hypersusceptibility mutations increase it.
  • Topoisomerase IV is a secondary target in E. coli and N. gonorrhoeae, but a primary target in S. aureus.
  • Efflux transporters like NorA, Emr, and MexAB-OprK significantly affect bacterial susceptibility to various quinolones.

Conclusions:

  • Quinolone binding to DNA gyrase involves complex interactions with both GyrA and GyrB subunits.
  • Bacterial topoisomerase IV plays a variable role as a primary or secondary quinolone target depending on the species.
  • Membrane efflux transporters are significant contributors to quinolone resistance and susceptibility across different bacterial types.

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