Evidence map›Paper›PMID 23504942›Full record

ArticleMicrobiologyOpen2013

Expression of Fap amyloids in Pseudomonas aeruginosa, P. fluorescens, and P. putida results in aggregation and increased biofilm formation.

Morten S Dueholm, Mads T Søndergaard, Martin Nilsson, Gunna Christiansen, Allan Stensballe, Michael T Overgaard, Michael Givskov, Tim Tolker-Nielsen, Daniel E Otzen, Per H Nielsen

Open access · goldAbstract read
In one paragraph

Article in MicrobiologyOpen, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

87 citing papers in PubMed, 165 citations in OpenAlex.

  1. Review
  2. Article
  3. The Importance of Being Imperfect: Structure and Function of Bacterial Amyloid.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  4. Review
  5. Review
  6. Article
  7. Structural basis ofScience advances · 2025
    Article
  8. Article
  9. Insights on pathoadaptation of sequentialMicrobiology spectrum · 2025
    Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Antibiotics (Basel, Switzerland) · 2024
    Review
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article

27 more citing papers are in PubMed but not listed here.

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

10 authors at 3 institutions in 2 countries.

Morten S DueholmDepartment of Biotechnology, Chemistry and Environmental Engineering, Aalborg University, Aalborg, Denmark.
Mads T Søndergaard
Martin Nilsson
Gunna Christiansen
Allan Stensballe
Michael T Overgaard
Michael Givskov
Tim Tolker-Nielsen
Daniel E Otzen
Per H Nielsen
Aalborg University · DKUniversity of Copenhagen · DKAarhus University · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The fap operon, encoding functional amyloids in Pseudomonas (Fap), is present in most pseudomonads, but so far the expression and importance for biofilm formation has only been investigated for P. fluorescens strain UK4. In this study, we demonstrate the capacity of P. aeruginosa PAO1, P. fluorescens Pf-5, and P. putida F1 to express Fap fibrils, and investigated the effect of Fap expression on aggregation and biofilm formation. The fap operon in all three Pseudomonas species conferred the ability to express Fap fibrils as shown using a recombinant approach. This Fap overexpression consistently resulted in highly aggregative phenotypes and in increased biofilm formation. Detailed biophysical investigations of purified fibrils confirmed FapC as the main fibril monomer and supported the role of FapB as a minor, nucleating constituent as also indicated by bioinformatic analysis. Bioinformatics analysis suggested FapF and FapD as a potential β-barrel membrane pore and protease, respectively. Manipulation of the fap operon showed that FapA affects monomer composition of the final amyloid fibril, and that FapB is an amyloid protein, probably a nucleator for FapC polymerization. Our study highlights the fap operon as a molecular machine for functional amyloid formation.

Indexed as

AmyloidBacterial AdhesionBacterial ProteinsBiofilmsComputational BiologyOperonProtein MultimerizationPseudomonas aeruginosaPseudomonas fluorescensPseudomonas putidaAmyloidBacterial Proteins

Identifiers

PMID23504942
PMCPMC3684753
OpenAlexW2094135937

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.