title: Susceptibilities of Bordetella pertussis strains to antimicrobial peptides.
abstract: We examined the susceptibilities of Bordetella pertussis strains to several antimicrobial peptides by determining the concentration required to inhibit or kill 50% of the bacterial population. The peptides are ranked in decreasing potency as follows: cecropin B > cecropin A >> melittin > cecropin P1 > (ala8,13,18)-magainin II amide > mastoparan = defensin HNP1 > protamine > or = magainin II = magainin I. By using a radial diffusion assay to compare susceptibilities between strains, wild-type B. pertussis BP338 was more resistant than the avirulent bvg mutant strain BP347 and the brk mutant strain BPM2041 to killing by cecropin P1. In contrast, compared with the wild type, the avirulent BP347 strain was highly resistant to killing by protamine and defensin HNP1.
authors.affiliation: Department of Molecular Genetics, Biochemistry and Microbiology, University of Cincinnati, Ohio 45267, USA.
authors.forename: R C
authors.initials: RC
authors.lastname: Fernandez
authors.forename: A A
authors.initials: AA
authors.lastname: Weiss
mesh_terms: D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides; D001886:Bordetella pertussis / Q000187:drug effects*; D036341:Intercellular Signaling Peptides and Proteins; D008555:Melitten / Q000494:pharmacology; D008826:Microbial Sensitivity Tests; D010455:Peptides / Q000494:pharmacology; D014862:Wasp Venoms / Q000494:pharmacology
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D036341:Intercellular Signaling Peptides and Proteins; D010455:Peptides; D014862:Wasp Venoms; D008555:Melitten; C037500:mastoparan; C031161:cecropin A