Antimicrobial activity and bacterial-membrane interaction of ovine-derived cathelicidins.
Three ovine-derived cathelicidins, SMAP29, OaBac5mini, and OaBac7.5mini, were compared with respect to their antibacterial activities and interactions with membranes. SMAP29 was confirmed to be alpha-helical, broad spectrum, and able to disrupt both the outer and the cytoplasmic membranes at relatively low concentrations. In contrast, the two proline- and arginine-rich OaBac peptides had more-modest antibacterial activities, reduced levels of lipopolysaccharide binding, and a lesser ability to depolarize the cytoplasmic membrane, consistent with a cytoplasmic target.
Anderson
Rachel C
RC
Biotechnology Group, Institute of Technology and Engineering, College of Sciences, Massey University, Palmerston North, New Zealand.
Hancock
Robert E W
RE
Yu
Pak-Lam
PL
D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D001419:Bacteria / Q000187:drug effects*; D001798:Blood Proteins / Q000737:chemistry / Q000494:pharmacology*; D054804:Cathelicidins; D002462:Cell Membrane / Q000187:drug effects; D002942:Circular Dichroism; D004926:Escherichia coli / Q000187:drug effects / Q000378:metabolism; D008070:Lipopolysaccharides / Q000378:metabolism; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D012756:Sheep / Q000378:metabolism*
D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D001798:Blood Proteins; D054804:Cathelicidins; D008070:Lipopolysaccharides; C403305:SMAP29 protein, Ovis aries