The antimicrobial peptide polyphemusin localizes to the cytoplasm of Escherichia coli following treatment.
The horseshoe crab peptide polyphemusin I possesses high antimicrobial activity, but its mechanism of action is as yet not well defined. Using a biotin-labeled polyphemusin I analogue and confocal fluorescence microscopy, we showed that the peptide accumulates in the cytoplasm of wild-type Escherichia coli within 30 min after addition without causing substantial membrane damage.
Department of Microbiology and Immunology, University of British Columbia, Vancouver, British Columbia V6T 1Z4, Canada.
Jon-Paul S
JP
Powers
Morgan M
MM
Martin
Danika L
DL
Goosney
Robert E W
RE
Hancock
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000378:metabolism / Q000494:pharmacology*; D003593:Cytoplasm / Q000378:metabolism*; D004926:Escherichia coli / Q000187:drug effects* / Q000378:metabolism; D008969:Molecular Sequence Data; D017830:Octoxynol / Q000494:pharmacology
D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; C062385:polyphemusin I; D017830:Octoxynol