Evidence map›Paper›PMID 25586180›Full record

ArticleThe Journal of biological chemistry2015

Functional amyloids keep quorum-sensing molecules in check.

Thomas Seviour, Susan Hove Hansen, Liang Yang, Yin Hoe Yau, Victor Bochuan Wang, Marcel R Stenvang, Gunna Christiansen, Enrico Marsili, Michael Givskov, Yicai Chen and 5 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
4.5field-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

35 citing papers in PubMed, 89 citations in OpenAlex.

  1. The Evolution of Functional Amyloids and Their Impact on Host-Microbe Interactions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Nanosilver Mitigates Biofilm Formation via FapC Amyloidosis Inhibition.Small (Weinheim an der Bergstrasse, Germany) · 2020
    Article
  17. Article
  18. Functional Amyloids.Cold Spring Harbor perspectives in biology · 2019
    Review
  19. Article
  20. 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

15 authors at 4 institutions in 3 countries.

Thomas SeviourFrom the Singapore Centre on Environmental Life Sciences Engineering (SCELSE) and twseviour@ntu.edu.sg.
Susan Hove Hansenthe Center for Microbial Communities, Aalborg University, 9220 Aalborg East, Denmark.
Liang YangFrom the Singapore Centre on Environmental Life Sciences Engineering (SCELSE) and.
Yin Hoe Yauthe School of Biological Sciences (SBS), Nanyang Technological University, Singapore 637551, Singapore.
Victor Bochuan WangFrom the Singapore Centre on Environmental Life Sciences Engineering (SCELSE) and the School of Materials Science and Engineering (MSE), Nanyang Technological University, Singapore 639798.
Marcel R Stenvangthe Interdisciplinary Nanoscience Center (iNANO), Department of Molecular Biology and Genetics, Center for Insoluble Protein Structures (inSPIN), and.
Gunna Christiansenthe Department of Biomedicine, Aarhus University, 8000 Aarhus C, Denmark.
Enrico MarsiliFrom the Singapore Centre on Environmental Life Sciences Engineering (SCELSE) and.
Michael GivskovFrom the Singapore Centre on Environmental Life Sciences Engineering (SCELSE) and the Department of International Health, Immunology and Microbiology, University of Copenhagen, 1165 Copenhagen, Denmark, and.
Yicai ChenFrom the Singapore Centre on Environmental Life Sciences Engineering (SCELSE) and.
Daniel E Otzenthe Interdisciplinary Nanoscience Center (iNANO), Department of Molecular Biology and Genetics, Center for Insoluble Protein Structures (inSPIN), and.
Per Halkjær NielsenFrom the Singapore Centre on Environmental Life Sciences Engineering (SCELSE) and the Center for Microbial Communities, Aalborg University, 9220 Aalborg East, Denmark.
Susana Geifman-Shochatthe School of Biological Sciences (SBS), Nanyang Technological University, Singapore 637551, Singapore.
Staffan KjellebergFrom the Singapore Centre on Environmental Life Sciences Engineering (SCELSE) and the Centre for Marine Bio-innovation and School of Biotechnology and Biomolecular Science, University of New South Wales, Mosman, New South Wales 2088, Australia.
Morten S Dueholmthe Center for Microbial Communities, Aalborg University, 9220 Aalborg East, Denmark.
Nanyang Technological University · SGAarhus University · DKAalborg University · DKSingapore Centre for Environmental Life Sciences Engineering · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mechanism by which extracellular metabolites, including redox mediators and quorum-sensing signaling molecules, traffic through the extracellular matrix of biofilms is poorly explored. We hypothesize that functional amyloids, abundant in natural biofilms and possessing hydrophobic domains, retain these metabolites. Using surface plasmon resonance, we demonstrate that the quorum-sensing (QS) molecules, 2-heptyl-3-hydroxy-4(1H)-quinolone and N-(3-oxododecanoyl)-l-homoserine lactone, and the redox mediator pyocyanin bind with transient affinity to functional amyloids from Pseudomonas (Fap). Their high hydrophobicity predisposes them to signal-amyloid interactions, but specific interactions also play a role. Transient interactions allow for rapid association and dissociation kinetics, which make the QS molecules bioavailable and at the same time secure within the extracellular matrix as a consequence of serial bindings. Retention of the QS molecules was confirmed using Pseudomonas aeruginosa PAO1-based 2-heptyl-3-hydroxy-4(1H)-quinolone and N-(3-oxododecanoyl)-l-homoserine lactone reporter assays, showing that Fap fibrils pretreated with the QS molecules activate the reporters even after sequential washes. Pyocyanin retention was validated by electrochemical analysis of pyocyanin-pretreated Fap fibrils subjected to the same washing process. Results suggest that QS molecule-amyloid interactions are probably important in the turbulent environments commonly encountered in natural habitats.

Indexed as

Biofilms4-ButyrolactoneAmyloidGene Expression Regulation, BacterialHumansProtein FoldingPseudomonas aeruginosaQuorum Sensing4-ButyrolactoneAmyloidhomoserine lactoneAmyloidBiofilmFunctional AmyloidPseudomonasPseudomonas aeruginosa (P. aeruginosa)Quorum Sensing

Identifiers

PMID25586180
PMCPMC4358280
OpenAlexW2017044836

What OpenQuestion holds

Textmetadata
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.