ArticleACS infectious diseases2018
Structure-Activity Relationships of the Competence Stimulating Peptide in Streptococcus mutans Reveal Motifs Critical for Membrane Protease SepM Recognition and ComD Receptor Activation.
Article in ACS infectious diseases, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 1 of them a synthesis that pooled it.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
27 citing papers in PubMed, 1 synthesis or guideline pooled it, 43 citations in OpenAlex.
- Key virulence genes associated withFrontiers in oral health · 2025Pooled it
- Quorum sensing in streptococci and its peptide-mediated modulation.Bioscience reports · 2026Review
- Quorum Sensing and Quorum Quenching in Periodontal Disease: Mechanisms and Therapeutic Potential.Current issues in molecular biology · 2026Review
- The Quorum Sensing-Controlled Competence Regulon Drives HACS infectious diseases · 2025Article
- Elucidating the Role of the Competence Regulon Quorum Sensing Circuitry inACS chemical biology · 2025Article
- SepM mutation in Streptococcus mutans clinical isolates and related function analysis.BMC oral health · 2024Article
- Anti-quorum Sensing of Terminalia catappa and Murraya koenigii Against Streptococcus mutans.Cureus · 2023Article
- Association of polymicrobial interactions with dental caries development and prevention.Frontiers in microbiology · 2023Review
- Exploiting Conserved Quorum Sensing Signals in Streptococcus mutans and Streptococcus pneumoniaeMicroorganisms · 2022Article
- The Outer Surface Protease, SepM, Is Required forJournal of bacteriology · 2022Article
- Quorum quenching of Streptococcus mutans via the nano-quercetin-based antimicrobial photodynamic therapy as a potential target for cariogenic biofilm.BMC microbiology · 2022Article
- Peptidomimetics as Potential Anti-Virulence Drugs Against Resistant Bacterial Pathogens.Frontiers in microbiology · 2022Review
- Genomic and phenotypic characterization ofFrontiers in microbiology · 2022Article
- Elucidating the Role and Structure-Activity Relationships of theACS chemical biology · 2021Article
- [Association of sepM gene mutation with mutacin Ⅳ production byNan fang yi ke da xue xue bao = Journal of Southern Medical University · 2021Article
- Cariogenic Biofilm: Pathology-Related Phenotypes and Targeted Therapy.Microorganisms · 2021Review
- Article
- Structure Activity Relationship Study of the XIP Quorum Sensing Pheromone inACS chemical biology · 2020Article
- Development and utilization of peptide-based quorum sensing modulators in Gram-positive bacteria.Organic & biomolecular chemistry · 2020Review
- Biological Evaluation of Native Streptococcal Competence Stimulating Peptides Reveal Potential Crosstalk BetweenRSC chemical biology · 2020Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Streptococcus mutans ( S. mutans) is a Gram-positive human pathogen that is one of the major contributors to dental caries, a condition with an economic cost of over $100 billion per year in the United States. S. mutans secretes a 21-amino-acid peptide termed the competence stimulating peptide (21-CSP) to assess its population density in a process termed quorum sensing (QS) and to initiate a variety of phenotypes such as biofilm formation and bacteriocin production. 21-CSP is processed by a membrane bound protease SepM into active 18-CSP, which then binds to the ComD receptor. This study seeks to determine the molecular mechanism that ties 21-CSP:SepM recognition and 18-CSP:ComD receptor binding and to identify QS modulators with distinct activity profiles. To this end, we conducted systematic replacement of the amino acid residues in both 21-CSP and 18-CSP and assessed the ability of the mutated analogs to modulate QS. We identified residues that are important to SepM recognition and ComD receptor binding. Our results shed light on the S. mutans competence QS pathway at the molecular level. Moreover, our structural insights of the CSP signal can be used to design QS-based anti-infective therapeutics against S. mutans.
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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.