Lacticin 3147, a broad-spectrum bacteriocin which selectively dissipates the membrane potential

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TY  - JOUR
  - McAuliffe, O,Ryan, MP,Ross, RP,Hill, C,Breeuwer, P,Abee, T
  - 1998
  - February
  - Applied and Environmental Microbiology
  - Lacticin 3147, a broad-spectrum bacteriocin which selectively dissipates the membrane potential
  - Validated
  - ()
  - GRAM-POSITIVE BACTERIA LACTOCOCCUS-LACTIS PEDIOCOCCUS-ACIDILACTICI CYTOPLASMIC MEMBRANE COMPLEMENTARY ACTION ACID BACTERIA LACTACIN-F 2 PEPTIDES NISIN PH
  - 64
  - 439
  - 445
  - Lacticin 3147 is a broad-spectrum bacteriocin produced by Lactococcus lactis subsp. lactis DPC3147 (M. P. Ryan, M. C. Pea, C. Hill, and R. P. Boss, Appl. Environ. Microbiol. 62:612-619, 1996). Partial purification of the bacteriocin by hydrophobic interaction chromatography and reverse-phase fast protein liquid chromatography revealed that two components are required for full activity. Lacticin 3147 is bactericidal against L. lactis, Listeria monocytogenes, and Bacillus subtilis; at low concentrations of the bacteriocin, bactericidal activity is enhanced when target cells are energized. This finding suggests that the presence of a proton motive force promotes the interaction of the bacteriocin with the cytoplasmic membrane, leading to the formation of pores at these low lacticin 3147 concentrations. These pores were shown to be selective for K+ ions and inorganic phosphate. The loss of these ions resulted in immediate dissipation of the membrane potential and hydrolysis of internal ATP, leading to an eventual collapse of the pH gradient at the membrane and ultimately to cell death. Our results suggest that lacticin 3147 is a pore-forming bacteriocin which acts on a broad range of gram-positive bacteria.
DA  - 1998/02
ER  - 
@article{V160744456,
   = {McAuliffe,  O and Ryan,  MP and Ross,  RP and Hill,  C and Breeuwer,  P and Abee,  T },
   = {1998},
   = {February},
   = {Applied and Environmental Microbiology},
   = {Lacticin 3147, a broad-spectrum bacteriocin which selectively dissipates the membrane potential},
   = {Validated},
   = {()},
   = {GRAM-POSITIVE BACTERIA LACTOCOCCUS-LACTIS PEDIOCOCCUS-ACIDILACTICI CYTOPLASMIC MEMBRANE COMPLEMENTARY ACTION ACID BACTERIA LACTACIN-F 2 PEPTIDES NISIN PH},
   = {64},
  pages = {439--445},
   = {{Lacticin 3147 is a broad-spectrum bacteriocin produced by Lactococcus lactis subsp. lactis DPC3147 (M. P. Ryan, M. C. Pea, C. Hill, and R. P. Boss, Appl. Environ. Microbiol. 62:612-619, 1996). Partial purification of the bacteriocin by hydrophobic interaction chromatography and reverse-phase fast protein liquid chromatography revealed that two components are required for full activity. Lacticin 3147 is bactericidal against L. lactis, Listeria monocytogenes, and Bacillus subtilis; at low concentrations of the bacteriocin, bactericidal activity is enhanced when target cells are energized. This finding suggests that the presence of a proton motive force promotes the interaction of the bacteriocin with the cytoplasmic membrane, leading to the formation of pores at these low lacticin 3147 concentrations. These pores were shown to be selective for K+ ions and inorganic phosphate. The loss of these ions resulted in immediate dissipation of the membrane potential and hydrolysis of internal ATP, leading to an eventual collapse of the pH gradient at the membrane and ultimately to cell death. Our results suggest that lacticin 3147 is a pore-forming bacteriocin which acts on a broad range of gram-positive bacteria.}},
  source = {IRIS}
}
AUTHORSMcAuliffe, O,Ryan, MP,Ross, RP,Hill, C,Breeuwer, P,Abee, T
YEAR1998
MONTHFebruary
JOURNAL_CODEApplied and Environmental Microbiology
TITLELacticin 3147, a broad-spectrum bacteriocin which selectively dissipates the membrane potential
STATUSValidated
TIMES_CITED()
SEARCH_KEYWORDGRAM-POSITIVE BACTERIA LACTOCOCCUS-LACTIS PEDIOCOCCUS-ACIDILACTICI CYTOPLASMIC MEMBRANE COMPLEMENTARY ACTION ACID BACTERIA LACTACIN-F 2 PEPTIDES NISIN PH
VOLUME64
ISSUE
START_PAGE439
END_PAGE445
ABSTRACTLacticin 3147 is a broad-spectrum bacteriocin produced by Lactococcus lactis subsp. lactis DPC3147 (M. P. Ryan, M. C. Pea, C. Hill, and R. P. Boss, Appl. Environ. Microbiol. 62:612-619, 1996). Partial purification of the bacteriocin by hydrophobic interaction chromatography and reverse-phase fast protein liquid chromatography revealed that two components are required for full activity. Lacticin 3147 is bactericidal against L. lactis, Listeria monocytogenes, and Bacillus subtilis; at low concentrations of the bacteriocin, bactericidal activity is enhanced when target cells are energized. This finding suggests that the presence of a proton motive force promotes the interaction of the bacteriocin with the cytoplasmic membrane, leading to the formation of pores at these low lacticin 3147 concentrations. These pores were shown to be selective for K+ ions and inorganic phosphate. The loss of these ions resulted in immediate dissipation of the membrane potential and hydrolysis of internal ATP, leading to an eventual collapse of the pH gradient at the membrane and ultimately to cell death. Our results suggest that lacticin 3147 is a pore-forming bacteriocin which acts on a broad range of gram-positive bacteria.
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