ArticleAntimicrobial agents and chemotherapy2010
Production of a class II two-component lantibiotic of Streptococcus pneumoniae using the class I nisin synthetic machinery and leader sequence.
Article in Antimicrobial agents and chemotherapy, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 73 citations in OpenAlex.
- Promiscuity of lanthipeptide enzymes: new challenges and applications.World journal of microbiology & biotechnology · 2025Review
- Insights into the production and evolution of lantibiotics from a computational analysis of peptides associated with the lanthipeptide cyclase domain.Royal Society open science · 2024Article
- Engineering lanthipeptides by introducing a large variety of RiPP modifications to obtain new-to-nature bioactive peptides.FEMS microbiology reviews · 2023Review
- Synthesis of a Novel Lantibiotic Using Mutacin II Biosynthesis Apparatus.Microbiology spectrum · 2023Article
- Targeted Large-Scale Genome Mining and Candidate Prioritization for Natural Product Discovery.Marine drugs · 2022Review
- Complex peptide natural products: Biosynthetic principles, challenges and opportunities for pathway engineering.Synthetic and systems biotechnology · 2022Article
- The structure of MadC fromFrontiers in microbiology · 2022Article
- Bacteriocin: A natural approach for food safety and food security.Frontiers in bioengineering and biotechnology · 2022Review
- Biogeography of Bacterial Communities and Specialized Metabolism in Human Aerodigestive Tract Microbiomes.Microbiology spectrum · 2021Article
- Engineering of new-to-nature ribosomally synthesized and post-translationally modified peptide natural products.Current opinion in biotechnology · 2021Review
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
- High-Throughput Screening for Substrate Specificity-Adapted Mutants of the Nisin Dehydratase NisB.ACS synthetic biology · 2020Article
- An Engineered Double Lipid II Binding Motifs-Containing Lantibiotic Displays Potent and Selective Antimicrobial Activity against Enterococcus faecium.Antimicrobial agents and chemotherapy · 2020Article
- Probiotics at War Against Viruses: What Is Missing From the Picture?Frontiers in microbiology · 2020Review
- Analysis of modular bioengineered antimicrobial lanthipeptides at nanoliter scale.Nature chemical biology · 2019Article
- Characterization of a Signaling System in Streptococcus mitis That Mediates Interspecies Communication with Streptococcus pneumoniae.Applied and environmental microbiology · 2019Article
- Modifying the Lantibiotic Mutacin 1140 for Increased Yield, Activity, and Stability.Applied and environmental microbiology · 2018Article
- Processing and Structure of the Lantibiotic Peptide Nso From the Human Gut Bacterium Blautia obeum A2-162 analysed by Mass Spectrometry.Scientific reports · 2018Article
- Increasing the Antimicrobial Activity of Nisin-Based Lantibiotics against Gram-Negative Pathogens.Applied and environmental microbiology · 2018Article
- Characterization of Leader Peptide Binding During Catalysis by the Nisin Dehydratase NisB.Journal of the American Chemical Society · 2018Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recent studies showed that the nisin modification machinery can successfully dehydrate serines and threonines and introduce lanthionine rings in small peptides that are fused to the nisin leader sequence. This opens up exciting possibilities to produce and engineer larger antimicrobial peptides in vivo. Here we demonstrate the exploitation of the class I nisin production machinery to generate, modify, and secrete biologically active, previously not-yet-isolated and -characterized class II two-component lantibiotics that have no sequence homology to nisin. The nisin synthesis machinery, composed of the modification enzymes NisB and NisC and the transporter NisT, was used to modify and secrete a putative two-component lantibiotic of Streptococcus pneumoniae. This was achieved by genetically fusing the propeptide-encoding sequences of the spr1765 (pneA1) and spr1766 (pneA2) genes to the nisin leader-encoding sequence. The chimeric prepeptides were secreted out of Lactococcus lactis, purified by cation exchange fast protein liquid chromatography, and further characterized. Mass spectrometry analyses demonstrated the presence and partial localization of multiple dehydrated serines and/or threonines and (methyl)lanthionines in both peptides. Moreover, after cleavage of the leader peptide from the prepeptides, both modified propeptides displayed antimicrobial activity against Micrococcus flavus. These results demonstrate that the nisin synthetase machinery can be successfully used to modify and produce otherwise difficult to obtain antimicrobially active lantibiotics.
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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.