Ability of cecropin B to penetrate the enterobacterial outer membrane.
The cationic amphipathic insect peptide cecropin B was almost as active on wild-type enteric bacteria as it was on their lipopolysaccharide and lipid A mutants that have very defective outer membrane. The polymyxin-resistant strains, which elaborate altered, less anionic lipopolysaccharide, were completely susceptible to cecropin B. No synergism was found between cecropin B and hydrophobic antibiotics. Throughout the study, the activity of cecropin B resembled that of quaternary detergents.
Department of Bacteriology and Immunology, University of Helsinki, Finland.
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D002463:Cell Membrane Permeability; D004926:Escherichia coli / Q000187:drug effects / Q000378:metabolism*; D007301:Insect Hormones / Q000493:pharmacokinetics* / Q000494:pharmacology; D019476:Insect Proteins; D008050:Lipid A / Q000235:genetics; D008070:Lipopolysaccharides / Q000096:biosynthesis; D008826:Microbial Sensitivity Tests; D009154:Mutation; D011112:Polymyxin B / Q000494:pharmacology; D012486:Salmonella typhimurium / Q000187:drug effects / Q000378:metabolism*
D007301:Insect Hormones; D019476:Insect Proteins; D008050:Lipid A; D008070:Lipopolysaccharides; C031162:cecropin B protein, Insecta; D011112:Polymyxin B