Evidence map›Paper›PMID 32611811›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Intercepting second-messenger signaling by rationally designed peptides sequestering c-di-GMP.

Chee-Seng Hee, Judith Habazettl, Christoph Schmutz, Tilman Schirmer, Urs Jenal, Stephan Grzesiek

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

19 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Antimicrobial peptides: from discovery to developmental applications.Applied and environmental microbiology · 2025
    Review
  3. Article
  4. Article
  5. Review
  6. Proteomics and EPS Compositional Analysis RevealsMaterials (Basel, Switzerland) · 2024
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Controlling Biofilm Development Through Cyclic di-GMP Signaling.Advances in experimental medicine and biology · 2022
    Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Review
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.

Chee-Seng HeeBiozentrum, University of Basel, 4056 Basel, Switzerland.ORCID 0000-0002-7697-312X
Judith HabazettlBiozentrum, University of Basel, 4056 Basel, Switzerland j.habazettl@unibas.ch urs.jenal@unibas.ch stephan.grzesiek@unibas.ch.ORCID 0000-0002-7976-768X
Christoph SchmutzBiozentrum, University of Basel, 4056 Basel, Switzerland.
Tilman SchirmerBiozentrum, University of Basel, 4056 Basel, Switzerland.ORCID 0000-0001-9512-8346
Urs JenalBiozentrum, University of Basel, 4056 Basel, Switzerland j.habazettl@unibas.ch urs.jenal@unibas.ch stephan.grzesiek@unibas.ch.ORCID 0000-0002-1637-3376
Stephan GrzesiekBiozentrum, University of Basel, 4056 Basel, Switzerland j.habazettl@unibas.ch urs.jenal@unibas.ch stephan.grzesiek@unibas.ch.ORCID 0000-0003-1998-4225
University of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The bacterial second messenger cyclic diguanylate (c-di-GMP) regulates a wide range of cellular functions from biofilm formation to growth and survival. Targeting a second-messenger network is challenging because the system involves a multitude of components with often overlapping functions. Here, we present a strategy to intercept c-di-GMP signaling pathways by directly targeting the second messenger. For this, we developed a c-di-GMP-sequestering peptide (CSP) that was derived from a CheY-like c-di-GMP effector protein. CSP binds c-di-GMP with submicromolar affinity. The elucidation of the CSP⋅c-di-GMP complex structure by NMR identified a linear c-di-GMP-binding motif, in which a self-intercalated c-di-GMP dimer is tightly bound by a network of H bonds and π-stacking interactions involving arginine and aromatic residues. Structure-based mutagenesis yielded a variant with considerably higher, low-nanomolar affinity, which subsequently was shortened to 19 residues with almost uncompromised affinity. We demonstrate that endogenously expressed CSP intercepts c-di-GMP signaling and effectively inhibits biofilm formation in

Indexed as

Second Messenger SystemsSignal TransductionBacterial ProteinsBiofilmsCyclic GMPEscherichia coli ProteinsModels, MolecularMutagenesisPeptidesPoint MutationProtein ConformationProtein DomainsProtein Interaction Domains and MotifsPseudomonas aeruginosaBacterial Proteinsbis(3',5')-cyclic diguanylic acidCyclic GMPEscherichia coli ProteinsPeptidesbiofilmc-di-GMPNMR solution structurepeptide designprotein dynamics

Identifiers

PMID32611811
PMCPMC7382256
OpenAlexW3038760654

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.