Interaction of the pore forming‐peptide antibiotics Pep 5, nisin and subtilin with non‐energized liposomes

Kordel, Marianne; Schüller, Friederike; Sahl, Hans-G.

doi:10.1016/0014-5793(89)81171-8

Cited by 96 publications

(88 citation statements)

References 20 publications

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“…The concentration of nisin was quantified after incubating it in cell-free supernatant fluids of the nisin-resistant isolates. No differences in the size Since the biological target of nisin action is the cytoplasmic membrane (Ruhr and Sahl 1985;Kordel and Sahl 1986;Kordel et al 1989) and changes in the membrane composition have been reported for nisin-resistant isolates (Ming and Daeschel 1993), we hypothesized that nisin resistance at low temperatures would also involve changes in the membrane composition. Alternatively, the passage of nisin through the cell wall could be affected in the nisin-resistant isolates so that nisin could not reach the cytoplasm membrane.…”

Section: Resultsmentioning

confidence: 97%

Nisin induces changes in membrane fatty acid composition of Listeria monocytogenes nisin-resistant strains at 10°C and 30°C

1997

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A. s. MAZZOTTA AND T . J. MONTVILLE. 1997. Listel-ia nzonocj~togenes isolates resistant to i05 IU ml-' nisin were obtained a t 30°C (NR30) and at 10°C (NR10). Nisin prolonged the lag phase of isolate NR30 at 10°C. Isolates NR30 and NRlO did not produce a nisinase. Protoplasts of isolate NR30 were unaffected by exposure to nisin. The fatty acid composition from the nild-type strain and NR isolates was determined. As expected, temperature-induced differences in the C l YC17 fatty acid ratios were found.Growth of the Z R strains in the presence of nisin resulted in significantly different C15/Cl'i ratios and a significant increase in the percentage of C16 : 0, C16 : 1, C18 : 0 and C18 : 1 fatty acids at 10°C and 30°C. Both the NRlO and NR30 isolates had similar growth rates at low temperatures, but these were slower than the wild-type strain, These results indicate that 'nisin resistance' is an environmentally defined phenotype and that nisin induces changes in the fattp acid composition of the membrane in L. rnonocytogenes nisin-resistant isolates regardless of the growth temperature.

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Section: Resultsmentioning

confidence: 97%

Nisin induces changes in membrane fatty acid composition of Listeria monocytogenes nisin-resistant strains at 10°C and 30°C

1997

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“…Thus, the composition of phospholipid head groups is important, and in particular the presence of negative charge appears to enhance insertion into the hydrophobic phase of the membrane. The tryptophan at position one in subtilin, which has a structure very similar to that of nisin, is blueshifted by 8 nm in the presence of zwitterionic Ole,GroPCho liposomes (Kordel et al, 1989).…”

Section: Discussionmentioning

confidence: 99%

“…6 , for 30% spin label as described in Results. caused quenching, it appeared that the N-terminal tryptophan of subtilin may lie close to the water-lipid interface, slightly entering the hydrophobic core with its indole ring (Kordel et al, 1989). Fluorescence quenching of the centrally located tyrosine of epilancin K7 has also been studied with doxy1 moieties present at positions 5, 10 or 16 on the acyl chains of PtdCho and PtdGro.…”

Section: Discussionmentioning

confidence: 99%

“…Nisin interacts electrostatically with the negatively charged phosphate groups of phospholipid at the surface of the membrane (Henning et al, 1986). The presence of anionic phospholipid head groups enhance this association and encourage a concurrent reduction in phospholipid tluidity (Kordel et al, 1989;Giffard et al, 1996). This initial interaction can locally perturb the dynamics of the phospholipid of the bilayer (Driessen et al,199.5).…”

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confidence: 99%

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Interaction of the Lantibiotic Nisin with Membranes Revealed by Fluorescence Quenching of an Introduced Tryptophan

Martin

Ruysschaert

Sanders

et al. 1996

European Journal of Biochemistry

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Nisin is a lantibiotic produced by strains of Lactococcus lactis subsp. lactis. The target for nisin action is the cytoplasmic membrane of gram-positive bacteria. To aid understanding of its mode of action, the interaction of nisin with vesicles of differing phospholipid composition were investigated by fluorescence techniques, using a variant of nisin in which the isoleucine at position 30 was replaced by a tryptophan residue. Activity of the site-directed variant containing tryptophan was established to be similar to that of the wild-type peptide. Fluorescence experiments showed a blue shift of the emission wavelength maximum in the presence of lipid vesicles, indicating that the tryptophan residue enters a more liydrophobic environment. Quenching experiments with aqueous and membrane-restricted quenchers (iodide and spin-labelled lipids, respectively) both confirmed a non-aqueous environment for the Trp30 residue, and implied that the residue resides between 0.36 nm and 0.52 nm from the centre of the membrane, depending on the lipid identity. The results clearly demonstrate that nisin interacts strongly with the hydrophobic phase of lipid vesicles. This interaction is stronger in the presence of negatively charged lipids suggesting their importance i n the functional interaction of nisin with membranes.

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“…The theory asserts that nisin forms pores that could disrupt the proton motive force and the pH equilibrium, causing the leakage of ions and hydrolysis of ATP and leading to cell death (De Arauz et al, 2009). The outer membrane of Gram-negative bacteria effectively excludes nisin from making contact and interacting with the cytoplasmic membrane (Kordel et al, 1989). Any treatment, such as chelating agent, sublethal heat, hydrostatic pressure, or freezing, or organic acids, which disrupts the outer membrane, may render Gram-negative cells sensitive to nisin (De Arauz et al, 2009).…”

Section: Discussionmentioning

confidence: 99%

Inactivation of Escherichia coli and Staphyloccocus aureus in Litchi Juice by Dimethyl Dicarbonate (DMDC) Combined With Nisin

Yu¹,

Xu²,

Wu³

et al. 2014

JFR

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Inactivation of Gram-negative Escherichia coli and Gram-positive Staphyloccocus aureus in litchi juice by DMDC combined with nisin was individually investigated. A 1.66 log cycles reduction of E. coli and 2.03 log cycles reduction of S. aureus in litchi juice (pH 4.5) added without nisin was achieved as exposed to 150 mg/l DMDC at 30 °C for 1 h, and the inactivation rate of E. coli and S. aureus during initial 1 h was far greater than during the remaining 5 h. As exposed to 150 mg/l DMDC at 30 °C for 1 h, the inactivation of E. coli and S. aureus in the litchi juice showed a trend toward increase with increasing of nisin addition level in the range from 0 to 200 IU/ml. Moreover, DMDC and nisin exhibited a synergistic effect on the inactivation of E. coli and S. aureus in litchi juice, and the inactivation of E. coli and S. aureus in the litchi juice also depends on the temperature of litchi juice, pH value of litchi juice and DMDC concentration when treated with DMDC and nisin. In addition, E. coli showed higher resistance to nisin as comparing with S. aureus. After E. coli and S. aureus in the litchi juice of pH 4.0 were individually treated with 150 mg/l DMDC combined with 200 IU/ml nisin at 30 °C for 1 h, a complete inactivation of S. aureus (6.59 log cycles) was achieved, but only 3.52 log cycles reduction of E. coli was observed.

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Interaction of the pore forming‐peptide antibiotics Pep 5, nisin and subtilin with non‐energized liposomes

Cited by 96 publications

References 20 publications

Nisin induces changes in membrane fatty acid composition of Listeria monocytogenes nisin-resistant strains at 10°C and 30°C

Nisin induces changes in membrane fatty acid composition of Listeria monocytogenes nisin-resistant strains at 10°C and 30°C

Interaction of the Lantibiotic Nisin with Membranes Revealed by Fluorescence Quenching of an Introduced Tryptophan

Inactivation of Escherichia coli and Staphyloccocus aureus in Litchi Juice by Dimethyl Dicarbonate (DMDC) Combined With Nisin

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