Lactococcal bacteriocins - mode of action and immunity
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.read more
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
H. Chen And and,Dallas G. Hoover +1 more
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.
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Production of class II bacteriocins by lactic acid bacteria; an example of biological warfare and communication
Vincent G. H. Eijsink,Lars Axelsson,Dzung B. Diep,Leiv Sigve Håvarstein,Helge Holo,Ingolf F. Nes +5 more
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
The leader peptide of colicin V shares consensus sequences with leader peptides that are common among peptide bacteriocins produced by gram-positive bacteria.
TL;DR: The findings strongly indicate that colicin V belongs to a family of small peptide bacteriocins that have been found previously only among the Gram-positive lactic acid bacteria.
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Genes involved in immunity to the lantibiotic nisin produced by Lactococcus lactis 6F3.
K Siegers,Karl-Dieter Entian +1 more
TL;DR: The NisF-NisE ABC transporter is homologous to an ABC transporter of Bacillus subtilis and the MbcF-MbcE transporter of Escherichia coli, which are involved in immunity to subtilin and microcin B17, respectively.
Journal ArticleDOI
Cytolytic pore-forming proteins and peptides: is there a common structural motif?
TL;DR: An evaluation of the secondary structures suggest that common secondary structures may be employed by most of the toxic PFPs isolated from a wide array of species ranging from humans to bacteria.
Journal ArticleDOI
Mechanistic studies of lantibiotic-induced permeabilization of phospholipid vesicles.
Arnold J. M. Driessen,H.W. van den Hooven,W. Kuiper,M. van de Kamp,Hans-Georg Sahl,Ruud N.H. Konings,W.N Konings +6 more
TL;DR: It is concluded that nisin acts as an anion-selective carrier in the absence of anionic phospholipids, and pore formation by cationic (type A) lantibiotics involves the local perturbation of the bilayer structure and a delta psi-dependent reorientation of these molecules from a surface-bound into a membrane-inserted configuration.
Book
Food Biopreservatives of Microbial Origin
TL;DR: Food Biopreservatives of Microbial Origin provides basic and applied information regarding how antimicrobial metabolites of safe, food-grade bacteria can be utilized as food preservatives.