Evidence map›Paper›PMID 26418177›Full record

ArticleMolecular microbiology2016

PepO, a CovRS-controlled endopeptidase, disrupts Streptococcus pyogenes quorum sensing.

Reid V Wilkening, Jennifer C Chang, Michael J Federle

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
5.3field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

34 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. PepO and CppA modulateVirulence · 2023
    Article
  4. Article
  5. Article
  6. Streptococcal peptides and their roles in host-microbe interactions.Frontiers in cellular and infection microbiology · 2023
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. AmBio · 2021
    Article
  15. Article
  16. Virulence · 2020
    Article
  17. Structure-function studies of Rgg binding to pheromones and target promoters reveal a model of transcription factor interplay.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  18. Article
  19. Article
  20. Novel Probiotic Mechanisms of the Oral BacteriumApplied and environmental microbiology · 2019
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Reid V WilkeningDepartment of Microbiology and Immunology, College of Medicine, University of Illinois at Chicago, Chicago, IL, 60607, USA.
Jennifer C ChangDepartment of Medicinal Chemistry and Pharmacognosy, Center for Biomolecular Sciences, College of Pharmacy, University of Illinois at Chicago, Chicago, IL, 60607, USA.
Michael J FederleDepartment of Medicinal Chemistry and Pharmacognosy, Center for Biomolecular Sciences, College of Pharmacy, University of Illinois at Chicago, Chicago, IL, 60607, USA.
University of Illinois Chicago · US

Funding

Mechanistic Dissection of Pheromone-Dependent Regulation of Group A StreptococcalR01AI091779 · NIAID · UNIVERSITY OF ILLINOIS AT CHICAGO · PI FEDERLE, MICHAEL J · 2011 to 2021
$3.9M
NIAID NIH HHS R01 AI091779NIAID NIH HHS R01-AI091779
6 · The paper itself

Abstract

Group A Streptococcus (GAS, Streptococcus pyogenes) is a human-restricted pathogen with a capacity to both colonize asymptomatically and cause illnesses ranging from pharyngitis to necrotizing fasciitis. An understanding of how and when GAS switches between genetic programs governing these different lifestyles has remained an enduring mystery and likely requires carefully tuned environmental sensors to activate and silence genetic schemes when appropriate. Herein, we describe the relationship between the Control of Virulence (CovRS, CsrRS) two-component system and the Rgg2/3 quorum-sensing pathway. We demonstrate that responses of CovRS to the stress signals Mg(2+) and a fragment of the antimicrobial peptide LL-37 result in modulated activity of pheromone signaling of the Rgg2/3 pathway through a means of proteolysis of SHP peptide pheromones. This degradation is mediated by the cytoplasmic endopeptidase PepO, which is the first identified enzymatic silencer of an RRNPP-type quorum-sensing pathway. These results suggest that under conditions in which the virulence potential of GAS is elevated (i.e. enhanced virulence gene expression), cellular responses mediated by the Rgg2/3 pathway are abrogated and allow individuals to escape from group behavior. These results also indicate that Rgg2/3 signaling is instead functional during non-virulent GAS lifestyles.

Indexed as

Quorum SensingSignal TransductionAntimicrobial Cationic PeptidesBacterial ProteinsCathelicidinsEndopeptidasesGene Regulatory NetworksHistidine KinaseIntracellular Signaling Peptides and ProteinsMagnesiumPheromonesRepressor ProteinsStreptococcus pyogenesVirulenceAntimicrobial Cationic PeptidesBacterial ProteinsCathelicidinsCovS protein, Streptococcus pyogenesCsrR protein, Streptococcus pyogenesEndopeptidasesHistidine KinaseIntracellular Signaling Peptides and ProteinsMagnesiumPheromonesRepressor Proteins

Identifiers

PMID26418177
PMCPMC4987125
OpenAlexW2161245713

What OpenQuestion holds

Textmetadata
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Read underepoch 390

Registered trials

None linked

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.