Insights in the Antimicrobial Potential of the Natural Nisin Variant Nisin H

Abstract

Lantibiotics are a growing class of antimicrobial peptides, which possess antimicrobial activity against mainly Gram-positive bacteria including the highly resistant strains such as methicillin-resistant Staphylococcus aureus or vancomycin-resistant enterococci. In the last decades numerous lantibiotics were discovered in natural habitats or designed with bioengineering tools. In this study, we present an insight in the antimicrobial potential of the natural occurring lantibiotic nisin H from Streptococcus hyointestinalis as well as the variant nisin H F 1 I. We determined the yield of the heterologously expressed peptide and quantified the cleavage efficiency employing the nisin protease NisP. Furthermore, we analyzed the effect on the modification via mass spectrometry analysis. With standardized growth inhibition assays we benchmarked the activity of pure nisin H and the variant nisin H F 1 I, and their influence on the activity of the nisin immunity proteins NisI and NisFEG from Lactococcus lactis and the nisin resistance proteins SaNSR and SaNsrFP from Streptococcus agalactiae COH1. We further checked the antibacterial activity against clinical isolates of Staphylococcus aureus, Enterococcus faecium and Enterococcus faecalis via microdilution method. In summary, nisin H and the nisin H F 1 I variant possessed better antimicrobial potency than the natural nisin A.

Anti-inflammatory and wound healing properties of lactic acid bacteria and its peptides

“…It is an antibacterial peptide that consists of 34 amino acid residues and has a wide range of applications (Kitagawa et al 2019 ). The class I lantibiotic consists of five methyl lanthionine rings that require various post-translational modifications that are then introduced in the precursor peptide (Reiners et al 2020 ). Different variants of Nisin have been identified.…”

“…Reduced inflammation in IL-10 deficient mice (Carroll et al 2007) lanthionine rings that require various post-translational modifications that are then introduced in the precursor peptide (Reiners et al 2020). Different variants of Nisin have been identified.…”

Nisin Variants Generated by Protein Engineering and Their Properties

“…Cleavage by NisP depends on the modification of precursor peptides; hence, factors affecting NisB and NisC will also affect NisP cleavage efficiency [ 85 ]. Low cleavage rates of the natural variant, nisin H, by NisP were restored by replacing phenylalanine with isoleucine [ 86 ], and integrity of the (methyl-)lanthionine rings is a prerequisite for recognition by the cleavage enzyme [ 85 ]. Therefore, the yield of nisin variants requires that the impact on residue changes be considered.…”

The inhibitory action of lactocin 63 on deterioration of seabass (Lateolabrax japonicus) during chilled storage

“…19,20 The antibacterial activity of nisin is limited to Gram-positive (G + ) bacteria, which restricts its application in foods primarily contaminated with G − spoilage bacteria, such as aquatic products. 21,22 In our previous study, Lactobacillus coryniformis FZU63 was isolated from traditional Chinese sauerkraut and has been found to produce a potent and broad-spectrum antimicrobial bacteriocin named lactocin 63. 23 This current study aims to elucidate the inhibitory mechanism of lactocin 63 against quality deterioration and spoilage in chilled seabass by investigating changes in microbial community and quality attributes.…”