Literature DB >> 9464377

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

O McAuliffe1, M P Ryan, R P Ross, C Hill, P Breeuwer, T Abee.   

Abstract

Lacticin 3147 is a broad-spectrum bacteriocin produced by Lactococcus lactis subsp. lactis DPC3147 (M. P. Ryan, M. C. Rea, C. Hill, and R. P. Ross, 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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Year:  1998        PMID: 9464377      PMCID: PMC106063     

Source DB:  PubMed          Journal:  Appl Environ Microbiol        ISSN: 0099-2240            Impact factor:   4.792


  26 in total

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Authors:  P Breeuwer; T Abee
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3.  Bactericidal mode of action of plantaricin C.

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5.  Interaction of the pore forming-peptide antibiotics Pep 5, nisin and subtilin with non-energized liposomes.

Authors:  M Kordel; F Schüller; H G Sahl
Journal:  FEBS Lett       Date:  1989-02-13       Impact factor: 4.124

6.  Lactococcin G is a potassium ion-conducting, two-component bacteriocin.

Authors:  G Moll; T Ubbink-Kok; H Hildeng-Hauge; J Nissen-Meyer; I F Nes; W N Konings; A J Driessen
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7.  Dependence of Streptococcus lactis phosphate transport on internal phosphate concentration and internal pH.

Authors:  B Poolman; R M Nijssen; W N Konings
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9.  Lactococcin A, a new bacteriocin from Lactococcus lactis subsp. cremoris: isolation and characterization of the protein and its gene.

Authors:  H Holo; O Nilssen; I F Nes
Journal:  J Bacteriol       Date:  1991-06       Impact factor: 3.490

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  42 in total

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Journal:  Appl Environ Microbiol       Date:  2001-06       Impact factor: 4.792

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4.  Lantibiotics biosynthesis genes and bacteriocinogenic activity of Lactobacillus spp. isolated from raw milk and cheese.

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5.  Lactocin 160, a Bacteriocin Produced by Vaginal Lactobacillus rhamnosus, Targets Cytoplasmic Membranes of the Vaginal Pathogen, Gardnerella vaginalis.

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6.  Cell Wall-active Bacteriocins and Their Applications Beyond Antibiotic Activity.

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7.  Sequential actions of the two component peptides of the lantibiotic lacticin 3147 explain its antimicrobial activity at nanomolar concentrations.

Authors:  Sheila M Morgan; Paula M O'connor; Paul D Cotter; R Paul Ross; Colin Hill
Journal:  Antimicrob Agents Chemother       Date:  2005-07       Impact factor: 5.191

8.  Insertional mutagenesis to generate lantibiotic resistance in Lactococcus lactis.

Authors:  Caitriona M Guinane; Paul D Cotter; Elaine M Lawton; Colin Hill; R Paul Ross
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9.  Influence of Ca(2+) ions on the activity of lantibiotics containing a mersacidin-like lipid II binding motif.

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10.  Bactericidal activity of glycinecin A, a bacteriocin derived from Xanthomonas campestris pv. glycines, on phytopathogenic Xanthomonas campestris pv. vesicatoria cells.

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Journal:  Appl Environ Microbiol       Date:  2004-08       Impact factor: 4.792

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