Journal
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY
Volume 56, Issue 4, Pages 1854-1861Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/AAC.05131-11
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Funding
- Hartwell Foundation
- Texas Christian University [60595]
- Junior Faculty Summer Research Program
- National Institutes of Health [GM68720, AI052453, AR052728, HD071600, GM06852]
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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.
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