Die Wirkung von Nisin auf Clostridium butyricum Prazm.

Hr, Ramseier

doi:10.1007/bf00414627

Cited by 64 publications

(16 citation statements)

References 99 publications

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“…The primary target of nisin in vegetative cells is the cytoplasmic membrane. Ramseier (1960) reported a strong adsorption of nisin to Clostridium butyricum vegetative cells. Nisin-treated cells leaked ultraviolet-absorbing material and subsequently lysed.…”

Section: Discussionmentioning

confidence: 99%

Production and utilization of polyclonal antibodies against nisin in an ELISA and for immuno-location of nisin in producing and sensitive bacterial strains

Bouksaim

Lacroix

Bazin

et al. 1999

Journal of Applied Microbiology

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M . B OU K SA IM , C. LA C RO IX , R. BA Z IN AN D R. E. S IM AR D . 1999. Specific nisin polyclonal antibodies (PAb) were produced in rabbits using nisin Z produced by Lactococcus lactis subsp. lactis biovar diacetylactis UL 719. Antisera were obtained from white female New Zealand rabbits that were first immunized with a nisin Z-keyhole limpet haemocyanin conjugate and boosted with free nisin Z. Nisin-specific PAb were purified by affinity chromatography with a yield of 15 mg specific antinisin 100 ml −1 serum. The detection limit of the ELISA test for nisin Z was 0·75 ng ml −1 in buffer but was 1·7 and 3·5 ng ml −1 in milk and complex media broth spiked (5, 10, 20 mg ml) with nisin Z, respectively. In nisin Z-spiked samples, the average concentration was between 90 and 107% of actual added amount. In contrast, when the bioassay (microtitration method) was used, only 50-63% of nisin Z biological activity could be detected. In addition, the affinity-purified nisin PAb, antirabbit IgG gold conjugate and transmission electron microscopy were successfully used to locate nisin Z on producing cells and to observe its bactericidal effects against sensitive cells.

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Section: Discussionmentioning

confidence: 99%

Production and utilization of polyclonal antibodies against nisin in an ELISA and for immuno-location of nisin in producing and sensitive bacterial strains

Bouksaim

Lacroix

Bazin

et al. 1999

Journal of Applied Microbiology

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“…Nisin is the most prominent member of the type A lantibiotics, which are elongated, amphiphilic, screw-shaped peptides with a net positive charge (11). The first report on the mode of action of nisin dates back to 1960, when Ramseier observed leakage of UV-absorbing intracellular compounds from treated cells, suggesting a detergent effect (16). Subsequent experiments showed that lantibiotics induce the rapid efflux of ions or cytoplasmic solutes such as amino acids and nucleotides.…”

mentioning

confidence: 99%

Lipid II-Mediated Pore Formation by the Peptide Antibiotic Nisin: a Black Lipid Membrane Study

Wiedemann

Benz²,

Sahl³

2004

J Bacteriol

164

131

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The antibiotic peptide nisin is the first known lantibiotic that uses a docking molecule within the bacterial cytoplasmic membrane for pore formation. Through specific interaction with the cell wall precursor lipid II, nisin forms defined pores which are stable for seconds and have pore diameters of 2 to 2.5 nm.Nisin, an amphiphilic antibiotic peptide, is produced by a number of strains of Lactococcus lactis subsp. lactis. It has antibacterial activity against various gram-positive bacteria and is widely used as a food preservative (10,15). Nisin belongs to the lantibiotics, which are ribosome synthesized, posttranslationally modified peptides characterized by intramolecular rings formed by the rare thioether amino acids lanthionine and 3-methyllanthionine (9, 12). Nisin is the most prominent member of the type A lantibiotics, which are elongated, amphiphilic, screw-shaped peptides with a net positive charge (11). The first report on the mode of action of nisin dates back to 1960, when Ramseier observed leakage of UV-absorbing intracellular compounds from treated cells, suggesting a detergent effect (16). Subsequent experiments showed that lantibiotics induce the rapid efflux of ions or cytoplasmic solutes such as amino acids and nucleotides. The concomitant depolarization of the cytoplasmic membrane resulted in a rapid termination of all biosynthetic processes (18,20). These results led to the conclusion that the primary mode of action of nisin is the formation of channels in the cytoplasmic membrane. Although the pore formation process of nisin in artificial membranes was intensively studied and several models, such as the wedge model, were established (8), it was not possible to explain some special features of nisin activity in vivo. For example, nisin is active against some bacteria even in the nanomolar range, whereas in artificial membranes, pore formation required micromolar concentrations (4).The first hints for the identification of a target molecule for nisin activity arose from observations by Linnett and Strominger (14); in an in vitro system with isolated membranes, nisin was shown to interfere with cell wall biosynthesis, which was later found to be based on interaction with the membrane-bound cell wall precursor lipid II [undecaprenylpyrophosphoryl-MurNAc-(pentapeptide)-GlcNAc] (17).The cell wall precursor lipid II was purified, and it was demonstrated with intact cells and lipid II-doped multilamellar liposomes (7) that nisin uses lipid II as a docking molecule for pore formation. The specificity of the nisin-lipid II interaction resulting in high-level activity of nisin was further demonstrated in a comparative study with the pore-forming amphiphilic defense peptide magainin 2. In contrast to magainin, the activity of nisin was enhanced by a factor of 10 3 when lipid II was available for targeted pore formation (5).To obtain information on the electrochemistry of the pore formation process in the presence of lipid II, we performed black lipid membrane bilayer experiments. The basic procedure f...

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“…'This effect is brought about by complex formation of nisin with the undecaprenyl pyrophosphate-activated intermediates of murein synthesis, resulting in the inhibition of the synthesis of this polymer. In an early paper, Ramseier (13) observed membrane leakiness of nisin-treated clostridia and discussed an effect similar to that of cationic detergents. The structure of nisin was elucidated by Gross and Morell (5), who showed that it contains inner-molecular-ring structures built by the thioether amino acid lanthionine.…”

mentioning

confidence: 99%

Mode of action of the peptide antibiotic nisin and influence on the membrane potential of whole cells and on cytoplasmic and artificial membrane vesicles

Ruhr¹,

Sahl²

1985

Antimicrob Agents Chemother

364

255

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The peptide antibiotic nisin was shown to cause a rapid efflux of amino acids and Rb+ from the cytoplasm of gram-positive bacteria (Staphylococcus cohnii 22, Bacillus subtilis W 23, Micrococcus luteus ATCC 4698, and Streptococcus zymogenes 24). It strongly decreased the membrane potential of cells as judged by the distribution of the lipophilic tetraphenylphosphonium cation. Ascorbate-phenazine methosulfate-driven transport of L-proline by cytoplasmic membrane vesicles was blocked after addition of nisin, and accumulated amino acids were released from the vesicles, Soybean phospholipid (asolectin) vesicles were not affected by nisin. The data suggest that the cytoplasmic membrane is the primary target and that membrane disruption accounts for the bactericidal action of nisin.

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Die Wirkung von Nisin auf Clostridium butyricum Prazm.

Cited by 64 publications

References 99 publications

Production and utilization of polyclonal antibodies against nisin in an ELISA and for immuno-location of nisin in producing and sensitive bacterial strains

Production and utilization of polyclonal antibodies against nisin in an ELISA and for immuno-location of nisin in producing and sensitive bacterial strains

Lipid II-Mediated Pore Formation by the Peptide Antibiotic Nisin: a Black Lipid Membrane Study

Mode of action of the peptide antibiotic nisin and influence on the membrane potential of whole cells and on cytoplasmic and artificial membrane vesicles

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