Membrane permeabilization of Listeria monocytogenes and mitochondria by the bacteriocin mesentericin Y105

J Bacteriol. 1993 May;175(10):3232-5. doi: 10.1128/jb.175.10.3232-3235.1993.

Abstract

Mesentericin Y105, a bacteriocin produced by a Leuconostoc mesenteroides strain, dissipates the plasma membrane potential of Listeria monocytogenes and inhibits the transport of leucine and glutamic acid. It also induces an efflux of preaccumulated amino acids from cells. In addition, the bacteriocin uncouples mitochondria by increasing state 4 respiration and decreasing state 3 respiration. The bacteriocin inhibits ATP synthase and adenine nucleotide translocase of the organelle while the affinity of ADP for its carrier is not modified. The results suggest that mesentericin Y105 acts by inducing, directly or indirectly, pore formation in the energy-transducing membranes, especially those of its natural target.

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Amino Acids / metabolism
  • Animals
  • Bacteriocins / pharmacology*
  • Biological Transport / drug effects
  • Cell Membrane Permeability / drug effects*
  • Dose-Response Relationship, Drug
  • Intracellular Membranes / drug effects*
  • Listeria monocytogenes / drug effects*
  • Membrane Potentials / drug effects
  • Mitochondria, Liver / drug effects*
  • Mitochondria, Liver / enzymology
  • Mitochondrial ADP, ATP Translocases / drug effects
  • Oxygen Consumption / drug effects
  • Permeability / drug effects
  • Rats

Substances

  • Amino Acids
  • Bacteriocins
  • mesentericin Y105 protein, Leuconostoc mesenteroides
  • Adenosine Triphosphate
  • Mitochondrial ADP, ATP Translocases