ArticleJournal of bacteriology2013
SmbFT, a putative ABC transporter complex, confers protection against the lantibiotic Smb in Streptococci.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Unveiling the biosynthesis mechanism of novel lantibiotic homicorcin: an in silico analysis.Scientific reports · 2024Article
- Synthesis of a Novel Lantibiotic Using Mutacin II Biosynthesis Apparatus.Microbiology spectrum · 2023Article
- Clp ATPases differentially affect natural competence development in Streptococcus mutans.MicrobiologyOpen · 2022Article
- A single system detects and protects the beneficial oral bacterium Streptococcus sp. A12 from a spectrum of antimicrobial peptides.Molecular microbiology · 2021Article
- Complete Genome Sequence of Streptococcus mutans Strain MD, Which Produces Highly Potent Mutacins.Microbiology resource announcements · 2020Article
- Novel Probiotic Mechanisms of the Oral BacteriumApplied and environmental microbiology · 2019Article
- Characterization of Brucella abortus mutant strain Δ22915, a potential vaccine candidate.Veterinary research · 2017Article
- Article
- Biosynthesis and transport of the lantibiotic mutacin 1140 produced by Streptococcus mutans.Journal of bacteriology · 2015Article
- Antimicrobial Peptide Resistance Mechanisms of Gram-Positive Bacteria.Antibiotics (Basel, Switzerland) · 2014Article
- A conserved streptococcal membrane protein, LsrS, exhibits a receptor-like function for lantibiotics.Journal of bacteriology · 2014Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Streptococcus mutans, a dental pathogen, secretes different kinds of lantibiotic and nonlantibiotic bacteriocins. For self-protection, a bacteriocin producer strain must possess one or more cognate immunity mechanisms. We report here the identification of one such immunity complex in S. mutans strain GS-5 that confers protection against Smb, a two-component lantibiotic. The immunity complex that we identified is an ABC transporter composed of two proteins: SmbF (the ATPase component) and SmbT (the permease component). Both of the protein-encoding genes are located within the smb locus. We show that GS-5 becomes sensitized to Smb upon deletion of smbT, which makes the ABC transporter nonfunctional. To establish the role SmbFT in providing immunity, we heterologously expressed this ABC transporter complex in four different sensitive streptococcal species and demonstrated that it can confer resistance against Smb. To explore the specificity of SmbFT in conferring resistance, we tested mutacin IV (a nonlantibiotic), nisin (a single peptide lantibiotics), and three peptide antibiotics (bacitracin, polymyxin B, and vancomycin). We found that SmbFT does not recognize these structurally different peptides. We then tested whether SmbFT can confer protection against haloduracin, another two-component lantibiotic that is structurally similar to Smb; SmbFT indeed conferred protection against haloduracin. SmbFT can also confer protection against an uncharacterized but structurally similar lantibiotic produced by Streptococcus gallolyticus. Our data suggest that SmbFT truly displays immunity function and confer protection against Smb and structurally similar lantibiotics.
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Registered trials
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.