MEMBRANE PERMEABILIZATION OF LISTERIA-MONOCYTOGENES AND MITOCHONDRIA BY THE BACTERIOCIN MESENTERICIN-Y105

Mesentericin Y105, a bacteriocin produced by a Leuconostoc mesenteroid es strain, dissipates the plasma membrane potential of Listeria monocy togenes and inhibits the transport of leucine and glutamic acid. It al so induces an efflux of preaccumulated amino acids from cells. In addi tion, the bacteriocin uncouples mitochondria by increasing state 4 res piration 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 sugg est that mesentericin Y105 acts by inducing, directly or indirectly, p ore formation in the energy-transducing membranes, especially those of its natural target.