Evidence map›Paper›PMID 28221753›Full record

ArticleACS chemical biology2017

Structure-Activity Relationships of the Competence Stimulating Peptides (CSPs) in Streptococcus pneumoniae Reveal Motifs Critical for Intra-group and Cross-group ComD Receptor Activation.

Yifang Yang, Bimal Koirala, Lucia A Sanchez, Naiya R Phillips, Sally R Hamry, Yftah Tal-Gan

Open access · greenAbstract read
In one paragraph

Article in ACS chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

40 citing papers in PubMed, 52 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Competence Regulation inCurrent medicinal chemistry · 2025
    Review
  6. Article
  7. The quorum-sensing peptidic inhibitor rescues host immune system eradication: A novel infectivity mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Investigating theMicrobiology (Reading, England) · 2022
    Article
  14. Review
  15. Article
  16. Attenuating theJournal of medicinal chemistry · 2022
    Article
  17. Article
  18. Article
  19. Review
  20. Pharmacology of T2R Mediated Host-Microbe Interactions.Handbook of experimental pharmacology · 2022
    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

6 authors at 1 institution in 1 country.

Yifang YangDepartment of Chemistry, University of Nevada, Reno , 1664 North Virginia Street, Reno, Nevada 89557, United States.
Bimal KoiralaDepartment of Chemistry, University of Nevada, Reno , 1664 North Virginia Street, Reno, Nevada 89557, United States.
Lucia A SanchezDepartment of Chemistry, University of Nevada, Reno , 1664 North Virginia Street, Reno, Nevada 89557, United States.
Naiya R PhillipsDepartment of Chemistry, University of Nevada, Reno , 1664 North Virginia Street, Reno, Nevada 89557, United States.
Sally R HamryDepartment of Chemistry, University of Nevada, Reno , 1664 North Virginia Street, Reno, Nevada 89557, United States.
Yftah Tal-GanDepartment of Chemistry, University of Nevada, Reno , 1664 North Virginia Street, Reno, Nevada 89557, United States.ORCID 0000-0003-2052-6782
University of Nevada, Reno · US

Funding

Outreach/Diversity/Pipeline ProjectP20GM103440 · NIGMS · UNIVERSITY OF NEVADA RENO · PI Eduardo A Robleto · 2012 to 2026
$58.0M
NIGMS NIH HHS P20 GM103440
6 · The paper itself

Abstract

Streptococcus pneumoniae is a highly recombinogenic human pathogen that utilizes the competence stimulating peptide (CSP)-based quorum sensing (QS) circuitry to acquire antibiotic resistance genes from the environment and initiate its attack on the human host. Modulation of QS in this bacterium, either inhibition or activation, can therefore be used to attenuate S. pneumoniae infectivity and slow down pneumococcal resistance development. In this study, we set to determine the molecular mechanism that drives CSP:receptor binding and identify CSP-based QS modulators with distinct activity profiles. To this end, we conducted systematic replacement of the amino acid residues in the two major CSP signals (CSP1 and CSP2) and assessed the ability of the mutated analogs to modulate QS against both cognate and noncognate ComD receptors. We then evaluated the overall 3D structures of these analogs using circular dichroism (CD) to correlate between the structure and function of these peptides. Our CD analysis revealed a strong correlation between α-helicity and bioactivity for both specificity groups (CSP1 and CSP2). Furthermore, we identified the first pan-group QS activator and the most potent group-II QS inhibitor to date. These chemical probes can be used to study the role of QS in S. pneumoniae and as scaffolds for the design of QS-based anti-infective therapeutics against S. pneumoniae infections.

Indexed as

Bacterial ProteinsBinding SitesCircular DichroismGenes, BacterialProtein ConformationQuorum SensingStreptococcus pneumoniaeStructure-Activity RelationshipBacterial Proteins

Identifiers

PMID28221753
PMCPMC5400695
OpenAlexW2590191504

What OpenQuestion holds

Textmetadata
LicenceTDM
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.