ArticleJournal of bacteriology2014
A conserved streptococcal membrane protein, LsrS, exhibits a receptor-like function for lantibiotics.
Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
- SpbR controls lipoteichoic acid length by directly inhibiting signal peptidase SpsB inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- The Role of SilX in Bacteriocin Production ofFrontiers in microbiology · 2022Article
- Synergistic Inhibition of Plantaricin E/F and Lactic Acid AgainstFrontiers in microbiology · 2022Article
- Regulated cleavage of glycan strands by the murein hydrolase SagB inJournal of bacteriology · 2021Article
- Complete Genome Sequence of Streptococcus mutans Strain MD, Which Produces Highly Potent Mutacins.Microbiology resource announcements · 2020Article
- Complete Genome Sequences of Two Mutacin-Producing Streptococcus mutans Strains, T8 and UA140.Microbiology resource announcements · 2020Article
- Characterization of a stress tolerance-defective mutant of Lactobacillus rhamnosus LRB.Molecular oral microbiology · 2019Article
- Control ofInfection and immunity · 2019Article
- Molecular Basis for Immunity Protein Recognition of a Type VII Secretion System Exported Antibacterial Toxin.Journal of molecular biology · 2018Article
- The Leaderless Bacteriocin Enterocin K1 Is Highly Potent againstFrontiers in microbiology · 2017Article
- Article
- Lantibiotic resistance.Microbiology and molecular biology reviews : MMBR · 2015Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Streptococcus mutans strain GS-5 produces a two-peptide lantibiotic, Smb, which displays inhibitory activity against a broad spectrum of bacteria, including other streptococci. For inhibition, lantibiotics must recognize specific receptor molecules present on the sensitive bacterial cells. However, so far no such receptor proteins have been identified for any lantibiotics. In this study, using a powerful transposon mutagenesis approach, we have identified in Streptococcus pyogenes a gene that exhibits a receptor-like function for Smb. The protein encoded by that gene, which we named LsrS, is a membrane protein belonging to the CAAX protease family. We also found that nisin, a monopeptide lantibiotic, requires LsrS for its optimum inhibitory activity. However, we found that LsrS is not required for inhibition by haloduracin and galolacticin, both of which are two-peptide lantibiotics closely related to Smb. LsrS appears to be a well-conserved protein that is present in many streptococci, including S. mutans. Inactivation of SMU.662, an LsrS homolog, in S. mutans strains UA159 and V403 rendered the cells refractory to Smb-mediated killing. Furthermore, overexpression of LsrS in S. mutans created cells more susceptible to Smb. Although LsrS and its homolog contain the CAAX protease domain, we demonstrate that inactivation of the putative active sites on the LsrS protein has no effect on its receptor-like function. This is the first report describing a highly conserved membrane protein that displays a receptor-like function for 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.