The antimicrobial peptides lactoferricin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm

FEBS Lett. 2001 Nov 23;508(3):389-93. doi: 10.1016/s0014-5793(01)03100-3.

Abstract

The localization of immunolabelled antimicrobial peptides was studied using transmission electron microscopy. Staphylococcus aureus and Escherichia coli were exposed to lactoferricin B (17-41), lactoferricin B (17-31) and D-lactoferricin B (17-31). E. coli was also exposed to cecropin P1 and magainin 2. The lactoferricins were found in the cytoplasm of both bacteria. In S. aureus the amount of cytoplasmic lactoferricin B (17-41) was time- and concentration-dependent, reaching a maximum within 30 min. Cecropin P1 was confined to the cell wall, while magainin 2 was found in the cytoplasm of E. coli. The finding of intracellularly localized magainin is not reported previously.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antimicrobial Cationic Peptides / metabolism*
  • Antimicrobial Cationic Peptides / pharmacology
  • Cell Membrane / metabolism*
  • Cytoplasm / metabolism
  • Escherichia coli / drug effects
  • Escherichia coli / metabolism*
  • Immunohistochemistry
  • Lactoferrin / analogs & derivatives*
  • Lactoferrin / metabolism*
  • Lactoferrin / pharmacology
  • Magainins
  • Microbial Sensitivity Tests
  • Staphylococcus aureus / drug effects
  • Staphylococcus aureus / metabolism*
  • Xenopus Proteins*

Substances

  • Antimicrobial Cationic Peptides
  • Magainins
  • Xenopus Proteins
  • magainin 2 peptide, Xenopus
  • lactoferricin B
  • Lactoferrin