Journal
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY
Volume 47, Issue 1, Pages 1-6Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/AAC.47.1.1-6.2003
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Funding
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI043412, R21AI044231, R01AI044231] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM054617] Funding Source: NIH RePORTER
- NIAID NIH HHS [AI38436, AI44231, R01 AI043412, R01 AI044231, R21 AI044231, AI43412] Funding Source: Medline
- NIGMS NIH HHS [GM54617] Funding Source: Medline
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Cationic antimicrobial peptides are believed to exert their primary activities on anionic bacterial cell membranes; however, this model does not adequately account for several important structure-activity relationships. These relationships are likely to be influenced by the bacterial response to peptide challenge. In order to characterize the genomic aspect of this response, transcription profiles were examined for Escherichia coli isolates treated with sublethal and lethal concentrations of the cationic antimicrobial peptide cecropin A. Transcript levels for 26 genes changed significantly following treatment with sublethal peptide concentrations, and half of the transcripts corresponded to protein products with unknown function. The pattern of response is distinct from that following treatment with lethal concentrations and is also distinct from the bacterial response to nutritional, thermal, osmotic, or oxidative stress. These results demonstrate that cecropin A induces a genomic response in E. coli apart from any lethal effects on the membrane and suggest that a complete understanding of its mechanism of action may require a detailed examination of this response.
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