ClpP-independent function of ClpX interferes with telithromycin resistance conferred by Msr(A) in Staphylococcus aureus

Antimicrob Agents Chemother. 2015;59(6):3611-4. doi: 10.1128/AAC.04367-14. Epub 2015 Mar 23.

Abstract

The ABCF family protein Msr(A) confers high resistance to macrolides but only low resistance to ketolides in staphylococci. Mutations in conserved functional regions of ClpX as well as deletion of clpX significantly increased Msr(A)-mediated resistance to the ketolide antibiotic telithromycin. ClpX is the chaperone component of the ClpXP two-component proteolytic system. Nevertheless, no changes in resistance were observed in a clpP knockout strain expressing msr(A), demonstrating that ClpX affects Msr(A) independently of ClpP.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / pharmacology*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Ketolides / pharmacology*
  • Macrolides / pharmacology
  • Mutation
  • Staphylococcus aureus / drug effects*
  • Staphylococcus aureus / metabolism*

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Ketolides
  • Macrolides
  • telithromycin