Lactococcal bacteriocins - mode of action and immunity
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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.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.
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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.
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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.
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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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Voltage-dependent depolarization of bacterial membranes and artificial lipid bilayers by the peptide antibiotic nisin.
TL;DR: The peptide antibiotic nisin is shown to disrupt valinomycin-induced potassium diffusion potentials imposed on intact cells of Staphylococcus cohnii 22 suggesting that nisin has to be regarded as a membrane-depolarizing agent which acts in a voltage-dependent fashion.
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In vitro pore-forming activity of the lantibiotic nisin. Role of protonmotive force and lipid composition
TL;DR: The in vitro action of nisin was studied on liposomes loaded with the fluorophore carboxyfluorescein and it was concluded that a delta psi is not essential, but that the total protonmotive force stimulates the action ofnisin.
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Cloning, expression, and nucleotide sequence of the Lactobacillus helveticus 481 gene encoding the bacteriocin helveticin J.
M C Joerger,Todd R. Klaenhammer +1 more
TL;DR: The 3' end of another open reading frame, ORF1, was located upstream of ORF2 and ORF3, and a non-coding region and a putative promoter were located between ORFs1 and ORFs2 as mentioned in this paper.
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Identification and characterization of some bacterial membrane sulfhydryl groups which are targets of bacteriostatic and antibiotic action.
TL;DR: Nisin, a 34-residue peptide antibiotic, inhibited spore outgrowth and sulfhydryl modification at a concentration of about 0.1 microM, suggesting substances directed toward them may be a useful new class of bacteriostatic agents and antibiotics.
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Production and Mode of Action of Lactocin 27: Bacteriocin from a Homofermentative Lactobacillus
G. C. Upreti,R. D. Hinsdill +1 more
TL;DR: Lactobacillus helveticus strain LP27 produced a bacteriocin, lactocin 27, in dialyzable and nondialyzable forms, which inhibited primarily protein synthesis without affecting deoxyribonucleic acid and ribon nucleic acid synthesis or adenosine 5′-triphosphate levels.