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Bacteriocins inhibit glucose PEP:PTS activity in Listeria monocytogenes by induced efflux of intracellular metabolites
Author(s) -
B. L. Waite,
Robert W. Hutkins
Publication year - 1998
Publication title -
journal of applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 1364-5072
DOI - 10.1046/j.1365-2672.1998.00502.x
Subject(s) - bacteriocin , efflux , listeria monocytogenes , nisin , intracellular , microbiology and biotechnology , extracellular , biology , biochemistry , phosphoenolpyruvate carboxykinase , pep group translocation , enzyme , chemistry , bacteria , antimicrobial , genetics
Glucose transport by the phosphoenolpyruvate (PEP)‐dependent phosphotransferase system (PTS) of Listeria monocytogenes is inhibited by the bacteriocins nisin, pediocin JD and leuconocin S. To investigate the mechanism of inhibition, PTS activity assays were performed with permeabilized, bacteriocin‐treated L. monocytogenes Scott A cells. In the presence of exogenous PEP, nisin stimulated the PTS while both pediocin JD and leuconocin S partially inhibited its activity. These results suggested that PTS enzymes were still active in bacteriocin‐treated cells and that bacteriocin‐induced PEP efflux may be a mechanism for inhibition of the PTS. To verify that PEP did efflux from bacteriocin‐treated L. monocytogenes Scott A cells, intracellular and extracellular PEP were measured by HPLC. All three bacteriocins induced efflux of PEP. Nisin, pediocin JD and leuconocin S also induced efflux of AMP, ADP and ATP. These studies indicate that bacteriocin inhibition of the glucose PEP:PTS in L. monocytogenes is due to efflux of intracellular metabolites, particularly PEP.