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Lactococcal bacteriocins - mode of action and immunity

Koen Venema, +2 more
- 01 Aug 1995 - 
- Vol. 3, Iss: 8, pp 299-304
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TLDR
The lactococcal bacteriocins are hydrophobic cationic peptides, which form pores in the cytoplasmic membrane of sensitive cells.
About
This article is published in Trends in Microbiology.The article was published on 1995-08-01 and is currently open access. It has received 78 citations till now. The article focuses on the topics: Bacteriocin & Antimicrobial peptides.

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Citations
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Journal ArticleDOI

Bacteriocins: Safe, natural antimicrobials for food preservation

TL;DR: Toxicity data exist for only a few bacteriocins, but research and their long-time intentional use strongly suggest that bacteriOCins can be safely used.
Journal ArticleDOI

Food fermentations: role of microorganisms in food production and preservation.

TL;DR: The role of lactic acid bacteria in many such fermentations and the mechanisms of antibiosis with particular reference to bacteriocins are outlined and a brief description of some important fermented foods from various countries are given.
Journal ArticleDOI

Class IIa bacteriocins: biosynthesis, structure and activity

TL;DR: The present review attempts to provide an insight into general knowledge available for class IIa bacteriocins and discusses common features and recent findings concerning these substances.
Journal ArticleDOI

Bacteriocins and their Food Applications

TL;DR: This review article focuses primarily on class I and class IIa bacteriocins produced by lactic acid bacteria (LAB) given their development as food preservatives.
Journal ArticleDOI

Production of class II bacteriocins by lactic acid bacteria; an example of biological warfare and communication

TL;DR: Although today a lot is known about LAB bacteriocins and the regulation of their production, several fundamental questions remain to be solved, including questions regarding mechanisms of immunity and resistance, as well as the molecular basis of target-cell specificity.
References
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Journal ArticleDOI

Genetics of ribosomally synthesized peptide antibiotics.

TL;DR: The results supporting these conclusions and the genes involved in modification and export of the peptide antibiotics are generally found adjacent to the structural gene and are under the same regulation.
Journal ArticleDOI

Structure, organization, and expression of the lct gene for lacticin 481, a novel lantibiotic produced by Lactococcus lactis

TL;DR: The structural gene for the lactococcal lantibiotic lacticin 481 (lct) has been identified and cloned using a degenerated 20-mer DNA oligonucleotide based on the amino-terminal 7 amino acid residues of the purified protein this paper.
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Purification, partial characterization and plasmid‐linkage of pediocin SJ‐1, a bacteriocin produced by Pediococcus acidilactici

TL;DR: Pediococcus acidilactici SJ-1, isolated from a naturally-fermented meat product, produced an antibacterial agent active against selected strains of Lactobacillus spp.
Journal ArticleDOI

Effect of Treatment Conditions on Nisin Inactivation of Gram-negative Bacteria

TL;DR: The addition of bovine serum albumin to the treatments containing nisin and EDTA did not result in a significant decrease in inhibitory action, and all of the chelators examined exhibited some inhibitory activity.
Journal ArticleDOI

Permeation of bacterial cells, permeation of cytoplasmic and artificial membrane vesicles, and channel formation on lipid bilayers by peptide antibiotic AS-48.

TL;DR: Electrical measurements suggest that AS-48 can form channels in lipid bilayers, and at low concentrations, this peptide causes permeability of liposomes to low-molecular-weight compounds without a requirement for a membrane potential.
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