Surface glycosaminoglycans protect eukaryotic cells against membrane-driven peptide bacteriocins

Antimicrob Agents Chemother. 2015 Jan;59(1):677-81. doi: 10.1128/AAC.04427-14. Epub 2014 Oct 20.

Abstract

Enzymatic elimination of surface glycosaminoglycans or inhibition of their sulfation provokes sensitizing of HT-29 and HeLa cells toward the peptide bacteriocins nisin A, plantaricin C, and pediocin PA-1/AcH. The effect can be partially reversed by heparin, which also lowers the susceptibility of Lactococcus lactis to nisin A. These data indicate that the negative charge of the glycosaminoglycan sulfate residues binds the positively charged bacteriocins, thus protecting eukaryotic cells from plasma membrane damage.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacteriocins / pharmacology*
  • Cell Membrane / drug effects
  • Cell Membrane / physiology
  • Glycosaminoglycans / physiology*
  • HT29 Cells / drug effects
  • HT29 Cells / physiology
  • HeLa Cells / drug effects
  • HeLa Cells / physiology
  • Heparin / pharmacology
  • Humans
  • Lactococcus lactis / metabolism
  • Nisin / pharmacology
  • Pediocins

Substances

  • Bacteriocins
  • Glycosaminoglycans
  • Pediocins
  • plantaricin C
  • pediocin PA-1
  • Nisin
  • Heparin
  • nisin A