The interaction of a recombinant cecropin/melittin hybrid peptide with the outer membrane of Pseudomonas aeruginosa

Mol Microbiol. 1994 Jun;12(6):951-8. doi: 10.1111/j.1365-2958.1994.tb01083.x.

Abstract

A cecropin/melittin hybrid peptide (CEME) produced by recombinant DNA procedures was tested for its ability to interact with the outer membrane of Pseudomonas aeruginosa and found to have identical biological properties to that of chemically synthesized CEME. CEME was shown to kill P. aeruginosa and permeabilize its outer membrane to lysozyme and 1-N-phenylnaphthlyamine, in some cases better than other antimicrobial agents and permeabilizers. CEME demonstrated a high-binding affinity to purified P. aeruginosa lipopolysaccharide (LPS) and LPS in whole-cell environments. These data provide information on the molecular mechanism of CEME antimicrobial activity and strongly suggest that it is taken up across the outer membrane by the self-promoted uptake pathway.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 1-Naphthylamine / analogs & derivatives
  • 1-Naphthylamine / metabolism
  • Anti-Bacterial Agents / metabolism*
  • Anti-Bacterial Agents / pharmacology
  • Antimicrobial Cationic Peptides
  • Cell Membrane / metabolism
  • Cell Membrane Permeability
  • Drug Synergism
  • Fluorescent Dyes
  • Lipopolysaccharides / metabolism
  • Melitten / metabolism*
  • Melitten / pharmacology
  • Microbial Sensitivity Tests
  • Muramidase / metabolism
  • Proteins / metabolism
  • Proteins / pharmacology
  • Pseudomonas aeruginosa / drug effects
  • Pseudomonas aeruginosa / metabolism*
  • Recombinant Fusion Proteins / metabolism*
  • Recombinant Fusion Proteins / pharmacology

Substances

  • Anti-Bacterial Agents
  • Antimicrobial Cationic Peptides
  • Fluorescent Dyes
  • Lipopolysaccharides
  • Proteins
  • Recombinant Fusion Proteins
  • Melitten
  • cecropin A
  • N-phenyl-1-naphthylamine
  • 1-Naphthylamine
  • Muramidase