ArticleScientific reports2016
Structural basis of lantibiotic recognition by the nisin resistance protein from Streptococcus agalactiae.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 49 citations in OpenAlex.
- Identification of glyoxalase A in group BInfection and immunity · 2025Article
- Identification of Glyoxalase A in Group BbioRxiv : the preprint server for biology · 2024Article
- Constitutive activation of two-component systems reveals regulatory network interactions in Streptococcus agalactiae.Nature communications · 2024Article
- 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
- Bromelain: A Potent Phytomedicine.Cureus · 2022Review
- Article
- Nisin Variants Generated by Protein Engineering and Their Properties.Bioengineering (Basel, Switzerland) · 2022Review
- Role of Antimicrobial Drug in the Development of Potential Therapeutics.Evidence-based complementary and alternative medicine : eCAM · 2022Review
- Bromelain and Nisin: The Natural Antimicrobials with High Potential in Biomedicine.Pharmaceutics · 2021Review
- Nisin- and Ripcin-Derived Hybrid Lanthipeptides Display Selective Antimicrobial Activity againstACS synthetic biology · 2021Article
- Gene-Trait Matching and Prevalence of Nisin Tolerance Systems inFrontiers in bioengineering and biotechnology · 2021Article
- Characterization of the nucleotide-binding domain NsrF from the BceAB-type ABC-transporter NsrFP from the human pathogen Streptococcus agalactiae.Scientific reports · 2020Article
- Two-Component Signal Transduction Systems in the Human Pathogen Streptococcus agalactiae.Infection and immunity · 2020Review
- Combating Antimicrobial Resistance With New-To-Nature Lanthipeptides Created by Genetic Code Expansion.Frontiers in microbiology · 2020Review
- Insights in the Antimicrobial Potential of the Natural Nisin Variant Nisin H.Frontiers in microbiology · 2020Article
- Conjugation of Synthetic Polyproline Moietes to Lipid II Binding Fragments of Nisin Yields Active and Stable Antimicrobials.Frontiers in microbiology · 2020Article
- Comparison of Antibiotic Resistance Mechanisms in Antibiotic-Producing and Pathogenic Bacteria.Molecules (Basel, Switzerland) · 2019Review
- Analysis of modular bioengineered antimicrobial lanthipeptides at nanoliter scale.Nature chemical biology · 2019Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lantibiotics are potent antimicrobial peptides. Nisin is the most prominent member and contains five crucial lanthionine rings. Some clinically relevant bacteria express membrane-associated resistance proteins that proteolytically inactivate nisin. However, substrate recognition and specificity of these proteins is unknown. Here, we report the first three-dimensional structure of a nisin resistance protein from Streptococcus agalactiae (SaNSR) at 2.2 Å resolution. It contains an N-terminal helical bundle, and protease cap and core domains. The latter harbors the highly conserved TASSAEM region, which lies in a hydrophobic tunnel formed by all domains. By integrative modeling, mutagenesis studies, and genetic engineering of nisin variants, a model of the SaNSR/nisin complex is generated, revealing that SaNSR recognizes the last C-terminally located lanthionine ring of nisin. This determines the substrate specificity of SaNSR and ensures the exact coordination of the nisin cleavage site at the TASSAEM region.
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