Article
Ability of cecropin B to penetrate the enterobacterial outer membrane.
Antimicrobial agents and chemotherapy - 1 Oct 1994
Vaara M, Vaara T
Abstract excerpt
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...
Topics
- Cell Membrane Permeability
- Escherichia coli
- Insect Hormones
- Insect Proteins
- Lipid A
- Lipopolysaccharides
- Microbial Sensitivity Tests
- Mutation
- Polymyxin B
- Salmonella typhimurium