ArticleFrontiers in microbiology2018
Specificity and Application of the Lantibiotic Protease NisP.
Article in Frontiers in microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 61 citations in OpenAlex.
- Biosynthesis of the Biphenomycin Family of Potent Antibiotics.Angewandte Chemie (International ed. in English) · 2025Article
- Expression of Caseicin from Lacticaseibacillus casei and Lacticaseibacillus zeae Provides Insight into Antilisterial Class IIa Bacteriocins.Probiotics and antimicrobial proteins · 2025Article
- Synthesis and Antimicrobial Specificities of Halogenated Tryptophan-Containing Nisin Variants.ACS chemical biology · 2025Article
- Functionalizing Nisin with a Sugar Moiety Improves Its Solubility and Results in an Altered Antibacterial Spectrum and Mode of Action.ACS synthetic biology · 2025Article
- The nisin O cluster: species dissemination, candidate leader peptide proteases and the role of regulatory systems.Microbiology (Reading, England) · 2025Article
- Facile Halogenation of Antimicrobial Peptides As Demonstrated by Producing Bromotryptophan-Labeled Nisin Variants with Enhanced Antimicrobial Activity.Journal of natural products · 2024Article
- Rombocin, a Short Stable Natural Nisin Variant, Displays Selective Antimicrobial Activity againstACS synthetic biology · 2024Article
- Cesin, a short natural variant of nisin, displays potent antimicrobial activity against major pathogens despite lacking two C-terminal macrocycles.Microbiology spectrum · 2023Article
- Lipidated variants of the antimicrobial peptide nisin produced via incorporation of methionine analogs for click chemistry show improved bioactivity.The Journal of biological chemistry · 2023Article
- After a century of nisin research - where are we now?FEMS microbiology reviews · 2023Review
- Nisin S, a Novel Nisin Variant Produced byInternational journal of molecular sciences · 2023Article
- Investigating the Specificity of the Dehydration and Cyclization Reactions in Engineered Lanthipeptides by Synechococcal SyncM.ACS synthetic biology · 2023Article
- Unusual Class I Lanthipeptides from the Marine BacteriaACS synthetic biology · 2022Article
- Correlational networking guides the discovery of unclustered lanthipeptide protease-encoding genes.Nature communications · 2022Article
- Analysis of Cross-Functionality within LanBTC Synthetase Complexes from Different Bacterial Sources with Respect to Production of Fully Modified Lanthipeptides.Applied and environmental microbiology · 2022Article
- Recombinant production of the lantibiotic nisin using Corynebacterium glutamicum in a two-step process.Microbial cell factories · 2022Article
- Novel pathways in bacteriocin synthesis by lactic acid bacteria with special reference to ethnic fermented foods.Food science and biotechnology · 2022Review
- Article
- Functional Expression and Characterization of the Highly Promiscuous Lanthipeptide Synthetase SyncM, Enabling the Production of Lanthipeptides with a Broad Range of Ring Topologies.ACS synthetic biology · 2021Article
- Therapeutic Application of Lantibiotics and Other Lanthipeptides: Old and New Findings.Applied and environmental microbiology · 2021Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lantibiotics are ribosomally produced and posttranslationally modified peptides containing several lanthionine residues. They exhibit substantial antimicrobial activity against Gram-positive bacteria, including relevant pathogens. The production of the model lantibiotic nisin minimally requires the expression of the modification and export machinery. The last step during nisin maturation is the cleavage of the leader peptide. This liberates the active compound and is catalyzed by the cell wall-anchored protease NisP. Here, we report the production and purification of a soluble variant of NisP. This has enabled us to study its specificity and test its suitability for biotechnological applications. The ability of soluble NisP to cleave leaders from various substrates was tested with two sets of nisin variants. The first set was designed to investigate the influence of amino acid variations in the leader peptide or variations around the cleavage site. The second set was designed to study the influence of the lanthionine ring topology on the proteolytic efficiency. We show that the substrate promiscuity is higher than has previously been suggested. Our results demonstrate the importance of the arginine residue at the end of the leader peptide and the importance of lanthionine rings in the substrate for specific cleavage. Collectively, these data indicate that NisP is a suitable protease for the activation of diverse heterologously expressed lantibiotics, which is required to release active antimicrobial compounds.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.