Bacteriocin inhibition of two glucose transport systems in Listeria monocytogenes

B. L. Waite, G. R. Siragusa, R. W. Hutkins

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Listeria monocytogenes transports glucose by proton motive force- mediated and phosphoenolpyruvate-dependent phosphotransferase systems (PEP- dependent PTS). Inhibition of both systems by nisin, pediocin JD and leuconosin S is reported here for four strains of L. monocytogenes. Intracellular and extracellular adenosine triphosphate (ATP) and extracellular inorganic phosphate were measured in energized L. monocytogenes Scott A cells to determine whether inhibition of the PEP-dependent PTS might occur as a result of bacteriocin-induced leakage of intracellular components. Addition of nisin resulted in a decrease in intracellular ATP with an increase in extracellular ATP. Leuconosin S and pediocin JD induced a depletion of intracellular ATP. ATP efflux was low for the leuconosin S- treated cells and barely detectable for pediocin JD-treated cells. Addition of nisin, leuconosin S and pediocin JD induced efflux of inorganic phosphate. It appears that bacteriocin-mediated inhibition of the glucose PEP-dependent PTS occurs as a result of hydrolysis or efflux of ATP, PEP and other essential molecules from L. monocytogenes cells.

Original languageEnglish (US)
Pages (from-to)715-721
Number of pages7
JournalJournal of Applied Microbiology
Volume84
Issue number5
DOIs
StatePublished - Jan 1 1998

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Bacteriocins
adenosine triphosphate
bacteriocins
Listeria monocytogenes
pediocins
Adenosine Triphosphate
Nisin
Glucose
glucose
nisin
Phosphates
cells
phosphates
Phosphoenolpyruvate
Proton-Motive Force
phosphotransferases (kinases)
Hydrolysis
Phosphotransferases
hydrolysis
Peptamen

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology

Cite this

Bacteriocin inhibition of two glucose transport systems in Listeria monocytogenes. / Waite, B. L.; Siragusa, G. R.; Hutkins, R. W.

In: Journal of Applied Microbiology, Vol. 84, No. 5, 01.01.1998, p. 715-721.

Research output: Contribution to journalArticle

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