ArticleThe Journal of biological chemistry2012
The First structure of a lantibiotic immunity protein, SpaI from Bacillus subtilis, reveals a novel fold.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Exploring the lipoproteome of Parageobacillus thermoglucosidasius.Access microbiology · 2026Article
- Current Knowledge of the Mode of Action and Immunity Mechanisms of LAB-Bacteriocins.Microorganisms · 2021Review
- Solution structure and RNA-binding of a minimal ProQ-homolog fromRNA (New York, N.Y.) · 2020Article
- LanI-Mediated Lantibiotic Immunity in Bacillus subtilis: Functional Analysis.Applied and environmental microbiology · 2019Article
- Crystal Structure of NisI in a Lipid-Free Form, the Nisin Immunity Protein, from Lactococcus lactis.Antimicrobial agents and chemotherapy · 2018Article
- Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes.Chemical reviews · 2017Review
- Structural basis of lantibiotic recognition by the nisin resistance protein from Streptococcus agalactiae.Scientific reports · 2016Article
- Protein Defense Systems against the Lantibiotic Nisin: Function of the Immunity Protein NisI and the Resistance Protein NSR.Frontiers in microbiology · 2016Review
- Structure of the Response Regulator NsrR from Streptococcus agalactiae, Which Is Involved in Lantibiotic Resistance.PloS one · 2016Article
- The Solution Structure of the Lantibiotic Immunity Protein NisI and Its Interactions with Nisin.The Journal of biological chemistry · 2015Article
- Structure and mechanism of lanthipeptide biosynthetic enzymes.Current opinion in structural biology · 2014Review
- Antimicrobial Peptide Resistance Mechanisms of Gram-Positive Bacteria.Antibiotics (Basel, Switzerland) · 2014Article
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lantibiotics are peptide-derived antibiotics that inhibit the growth of Gram-positive bacteria via interactions with lipid II and lipid II-dependent pore formation in the bacterial membrane. Due to their general mode of action the Gram-positive producer strains need to express immunity proteins (LanI proteins) for protection against their own lantibiotics. Little is known about the immunity mechanism protecting the producer strain against its own lantibiotic on the molecular level. So far, no structures have been reported for any LanI protein. We solved the structure of SpaI, a LanI protein from the subtilin producing strain Bacillus subtilis ATCC 6633. SpaI is a 16.8-kDa lipoprotein that is attached to the outside of the cytoplasmic membrane via a covalent diacylglycerol anchor. SpaI together with the ABC transporter SpaFEG protects the B. subtilis membrane from subtilin insertion. The solution-NMR structure of a 15-kDa biologically active C-terminal fragment reveals a novel fold. We also demonstrate that the first 20 N-terminal amino acids not present in this C-terminal fragment are unstructured in solution and are required for interactions with lipid membranes. Additionally, growth tests reveal that these 20 N-terminal residues are important for the immunity mediated by SpaI but most likely are not part of a possible subtilin binding site. Our findings are the first step on the way of understanding the immunity mechanism of B. subtilis in particular and of other lantibiotic producing strains in general.
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