Mode of Action of Nisin Z against
            <i>Listeria monocytogenes</i>
            Scott A Grown at High and Low Temperatures

Abee, Tjakko; Rombouts, F.M.; Hugenholtz, Jeroen; Guihard, Gilles; Letellìer, Lucienne

doi:10.1128/aem.60.6.1962-1968.1994

Cited by 163 publications

(118 citation statements)

References 31 publications

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“…By comparing the rates of pediocin-PA-1-induced ATP depletion and inorganic phosphate e¥ux, Chen and Montville [89] have suggested that the observed depletion of ATP is most likely due to attempts of the cell to regenerate the decreased PMF, rather than a shift in the ATP hydrolysis equilibrium due to the loss of inorganic phosphate. Again, contrasting results have been reported for the lantibiotic nisin Z [91].…”

Section: Bactericidal E¡ectsmentioning

confidence: 71%

Class IIa bacteriocins: biosynthesis, structure and activity

Ennahar¹

2000

FEMS Microbiology Reviews

141

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In the last decade, a variety of ribosomally synthesized antimicrobial peptides or bacteriocins produced by lactic acid bacteria have been identified and characterized. As a result of these studies, insight has been gained into fundamental aspects of biology and biochemistry such as producer self protection, membrane-protein interactions, and protein modification and secretion. Moreover, it has become evident that these peptides may be developed into useful antimicrobial additives. Class IIa bacteriocins can be considered as the major subgroup of bacteriocins from lactic acid bacteria, not only because of their large number, but also because of their activities and potential applications. They have first attracted particular attention as listericidal compounds and are now believed to be the next in line if more bacteriocins are to be approved in the future. 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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Section: Bactericidal E¡ectsmentioning

confidence: 71%

Class IIa bacteriocins: biosynthesis, structure and activity

Ennahar¹

2000

FEMS Microbiology Reviews

141

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“…Subsequently, it has been shown that nisin kills bacterial cells by interfering with basic energy transduction occurring at the cytoplasmic membrane [166,173,181]. It was found that pores formed in the membrane by the nisin molecules allowed the di¡usion of small compounds, since no transport system for ATP has been reported [173,186]. The increase in membrane permeability results in the collapse of the PMF; in the case of nisin, both the vpH and the vi are completely dissipated leading to a rapid cessation of all biosynthetic processes [173,175,187,188].…”

Section: Biological Activity Of Nisinmentioning

confidence: 99%

Lantibiotics: structure, biosynthesis and mode of action

McAuliffe¹,

Ross²,

Hill³

2001

FEMS Microbiol Rev

547

312

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The lantibiotics are a group of ribosomally synthesised, post-translationally modified peptides containing unusual amino acids, such as dehydrated and lanthionine residues. This group of bacteriocins has attracted much attention in recent years due to the success of the well characterised lantibiotic, nisin, as a food preservative. Numerous other lantibiotics have since been identified and can be divided into two groups on the basis of their structures, designated type-A and type-B. To date, many of these lantibiotics have undergone extensive characterisation resulting in an advanced understanding of them at both the structural and mechanistic level. This review outlines some of the more recent developments in the biochemistry, genetics and mechanism of action of these peptides.

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“…Nisin interferes with the cytoplasmic membrane of sensitive species, leading to pore formation, and dissipates the proton motive force. This allows e¥ux of low-molecularmass solutes such as amino acids and K [8]. The e¤cacy of nisin as an antibacterial agent would be compromised by the emergence of nisin-resistant bacteria in a food-processing situation.…”

Section: Introductionmentioning

confidence: 99%

Involvement of cell envelope in nisin resistance of Pectinatus frisingensis, a Gram-negative, strictly anaerobic beer-spoilage bacterium naturally sensitive to nisin

Chihib¹

1999

FEMS Microbiology Letters

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A nisin-resistant strain of Pectinatus frisingensis (Nis-5000) to high nisin concentration (5000 IU ml 3:1 ) was isolated. The nisin resistance phenotype of strain Nis-5000 was stable after five passages through nisin-free medium. The involvement of the cell envelope in nisin resistance was investigated. EDTA treatment of Nis-5000 strain cells did not render them sensitive to the bacteriocin, suggesting that the lipopolysaccharide layer was not involved in nisin resistance. The Nis-5000 strain shows a significantly different fatty acid composition compared with that of the wild-type strain. The modifications occurred mainly in C17 :1 (P 6 0.05) and C18 :cyclo (P 6 0.05), suggesting the involvement of membrane fluidity in preventing nisin's effect. ß

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Mode of Action of Nisin Z against Listeria monocytogenes Scott A Grown at High and Low Temperatures

Cited by 163 publications

References 31 publications

Class IIa bacteriocins: biosynthesis, structure and activity

Class IIa bacteriocins: biosynthesis, structure and activity

Lantibiotics: structure, biosynthesis and mode of action

Involvement of cell envelope in nisin resistance of Pectinatus frisingensis, a Gram-negative, strictly anaerobic beer-spoilage bacterium naturally sensitive to nisin

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