ReviewFrontiers in microbiology2016
Protein Defense Systems against the Lantibiotic Nisin: Function of the Immunity Protein NisI and the Resistance Protein NSR.
Review in Frontiers in microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers, 1 of them a synthesis that pooled it.
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Who cites it
29 citing papers in PubMed, 1 synthesis or guideline pooled it, 48 citations in OpenAlex.
- Identification ofVirulence · 2021Pooled it
- The DdD protein confers intracellular and extracellular immunity to the leaderless bacteriocin enterocin DD14.PNAS nexus · 2026Article
- Recent Advances in Antimicrobial Proteins and Peptides: A Promising Clinical Breakthrough and Patent Landscape.Current protein & peptide science · 2026Review
- Bactofencin A Displays a Delayed Killing Effect on a Clinical Strain ofAntibiotics (Basel, Switzerland) · 2025Article
- PanBGC: a pangenome-inspired framework for comparative analysis of biosynthetic gene clusters.ISME communications · 2025Article
- TheCurrent research in microbial sciences · 2025Article
- Discovery and Heterologous Expression of Trilenodin, an Antimicrobial Lasso Peptide with a Unique Tri-Isoleucine Motif.Chembiochem : a European journal of chemical biology · 2024Article
- Bacteriocin diversity, function, discovery and application as antimicrobials.Nature reviews. Microbiology · 2024Review
- Guarding the walls: the multifaceted roles of Bce modules in cell envelope stress sensing and antimicrobial resistance.Journal of bacteriology · 2024Review
- After a century of nisin research - where are we now?FEMS microbiology reviews · 2023Review
- Structure-activity relationships of antibacterial peptides.Microbial biotechnology · 2023Review
- A Function of Amyloid-β in Mediating Activity-Dependent Axon/Synapse Competition May Unify Its Roles in Brain Physiology and Pathology.Journal of Alzheimer's disease : JAD · 2023Review
- Bioengineered Nisin A Derivatives Display Enhanced Activity against Clinical Neonatal Pathogens.Antibiotics (Basel, Switzerland) · 2022Article
- New insights into the resistance mechanism for the BceAB-type transporter SaNsrFP.Scientific reports · 2022Article
- The effect of ultrasound treatment in combination with nisin on the inactivation of Listeria innocua and Escherichia coli.Ultrasonics sonochemistry · 2021Article
- Current Knowledge of the Mode of Action and Immunity Mechanisms of LAB-Bacteriocins.Microorganisms · 2021Review
- A Bioengineered Nisin Derivative To Control Streptococcus uberis Biofilms.Applied and environmental microbiology · 2021Article
- In Silico Prediction and Analysis of Unusual Lantibiotic Resistance Operons in the GenusMicroorganisms · 2021Article
- Cell wall homeostasis in lactic acid bacteria: threats and defences.FEMS microbiology reviews · 2020Review
- Insights in the Antimicrobial Potential of the Natural Nisin Variant Nisin H.Frontiers in microbiology · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lantibiotics are potential alternatives to antibiotics because of their broad-range killing spectrum. The producer strain is immune against its own synthesized lantibiotic via the expression of two proteins LanI and LanFEG. Recently, gene operons are found in mainly human pathogenic strains, which confer resistance against lantibiotics. Of all the lantibiotics discovered till date, nisin produced by some Lactococcus lactis strains is the most prominent member. Nisin has multiple mode of actions of which binding to the cell wall precursor lipid II and subsequent insertion into the bacterial membrane to form pores are the most effective. The nisin producing strains express the lipoprotein NisI to prevent a suicidal effect. NisI binds nisin, inducing a reversible cell clustering to prevent nisin from reaching the membrane. Importantly NisI does not modify nisin and releases it as soon as the concentration in the media drops below a certain level. The human pathogen Streptococcus agalactiae is naturally resistant against nisin by expressing a resistance protein called SaNSR, which is a nisin degrading enzyme. By cleaving off the last six amino acids of nisin, its effectiveness is 100-fold reduced. This cleavage reaction appears to be specific for nisin since SaNSR recognizes the C-terminal located lanthionine rings. Recently, the structures of both NisI and SaNSR were determined by NMR and X-ray crystallography, respectively. Furthermore, for both proteins the binding site for nisin was determined. Within this review, the structures of both proteins and their different defense mechanisms are described.
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