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Antimicrob Agents Chemother. 2012 Apr;56(4):1854-61. doi: 10.1128/AAC.05131-11. Epub 2012 Jan 17.

Pharmacological inhibition of the ClpXP protease increases bacterial susceptibility to host cathelicidin antimicrobial peptides and cell envelope-active antibiotics.

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  • 1Department of Biology, Texas Christian University, Fort Worth, Texas, USA. s.mcgillivray@tcu.edu

Abstract

The ClpXP protease is a critical bacterial intracellular protease that regulates protein turnover in many bacterial species. Here we identified a pharmacological inhibitor of the ClpXP protease, F2, and evaluated its action in Bacillus anthracis and Staphylococcus aureus. We found that F2 exhibited synergistic antimicrobial activity with cathelicidin antimicrobial peptides and antibiotics that target the cell well and/or cell membrane, such as penicillin and daptomycin, in B. anthracis and drug-resistant strains of S. aureus. ClpXP inhibition represents a novel therapeutic strategy to simultaneously sensitize pathogenic bacteria to host defenses and pharmaceutical antibiotics.

PMID:
22252821
PMCID:
PMC3318395
DOI:
10.1128/AAC.05131-11
[PubMed - indexed for MEDLINE]
Free PMC Article
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