Abstract

The lantibiotic nisin is a small 3.4 kDa antimicrobial peptide, which acts against Gram-positive bacteria in the nmol/L range. Nisin is produced and secreted by several Lactococcus lactis strains to ensure advantages against other bacteria in their habitat. Nisin contains five specific lanthionine rings of which the first two are important for Lipid II binding and the last two are crucial for the pore formation in the membrane. To gain immunity against nisin, the producing strain is expressing an ABC transporter called NisFEG, which expels nisin from the membrane. As a result six to eightfold more nisin is needed to affect the cells. The hydrolysis of ATP by NisFEG is required for this immunity as shown by a mutant, where the ATP hydrolysis is disrupted (NisFH181AEG). Furthermore, NisFEG recognizes the C-terminus of nisin, since deletion of the last six amino acids as well as of the last ring lowered the fold of immunity displayed by NisFEG.

Highlights

  • Lantibiotics are small ribosomally synthesized peptides produced by numerous of gram-negative bacteria

  • The plasmid pILNisFEG or pILNisFH181AEG was transformed into L. lactis NZ9000

  • To address the activity of nisin against the NZ9000Erm, NZ9000NisFEG and NZ9000NisFH181AEG strains, the IC50 value of nisin was determined for the different strains, which reflects the growth inhibition of the corresponding strain by 50%

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Summary

Introduction

Lantibiotics are small ribosomally synthesized peptides produced by numerous of gram-negative bacteria. Lantibiotics are activated, upon the cleavage of the lantibiotic-specific presequence (or leader peptide), which is important for the modification machinery and subsequent secretion (Kuipers et al 2004; Rink et al 2005). These active lantibiotics are able to lyse mainly gram-positive bacteria as well as a limited number of gram-negative bacteria and act via different but distinct mechanisms (Wiedemann et al 2001; Chatterjee et al 2005b) targeting the membrane of the bacteria. In most lantibiotic gene clusters both proteins are present some exceptions are known (Chatterjee et al 2005b; Alkhatib et al 2012)

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