Evidence map›Paper›PMID 20955240›Full record

ArticleCellular microbiology2011

Pseudomonas aeruginosa pilin activates the inflammasome.

Cecilia S Lindestam Arlehamn, Tom J Evans

Open access · greenAbstract read
In one paragraph

Article in Cellular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

37 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Multidrug-resistantVirulence · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Flagella, Chemotaxis and Surface Sensing.Advances in experimental medicine and biology · 2022
    Article
  9. Article
  10. International journal of molecular sciences · 2021
    Review
  11. Review
  12. Article
  13. Frontiers in immunology · 2020
    Article
  14. NOD-like receptor(s) and host immune responses with Pseudomonas aeruginosa infection.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2018
    Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Review
  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

2 authors at 2 institutions in 2 countries.

Cecilia S Lindestam ArlehamnInstitute of Infection, Immunity and Inflammation, College of Medicine, Veterinary and Life Sciences, University of Glasgow, UK.
Tom J Evans
Institute of Infection and Immunity · CAUniversity of Glasgow · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

IL-1β is produced from inactive pro-IL-1β by activation of caspase-1 brought about by a multi-subunit protein platform called the inflammasome. Many bacteria can trigger inflammasome activity through flagellin activation of the host protein NLRC4. However, strains of the common human pathogen Pseudomonas aeruginosa lacking flagellin can still activate the inflammasome. We set out to identify what non-flagellin components could produce this activation. Using mass spectroscopy, we identified an inflammasome-activating factor from P. aeruginosa as pilin, the major component of the type IV bacterial pilus. Purified pilin introduced into mouse macrophages by liposomal delivery activated caspase-1 and led to secretion of mature IL-1β, as did recombinant pilin purified from Escherichia coli. This was dependent on caspase-1 but not on the host inflammasome proteins NLRC4, NLRP3 or ASC. Mutants of P. aeruginosa strain PA103 lacking pilin did not activate the inflammasome following infection of macrophages with live bacteria. Type III secretion remained intact in the absence of pili, showing this was not due to a lack of effector delivery. Our observations show pilin is a novel activator of the inflammasome in addition to flagellin and the recently described PrgJ protein family, the basal body rod component of the type III apparatus.

Indexed as

AnimalsApoptosis Regulatory ProteinsBlotting, WesternCalcium-Binding ProteinsCARD Signaling Adaptor ProteinsCarrier ProteinsCaspase 1Cytoskeletal ProteinsEnzyme-Linked Immunosorbent AssayEscherichia coliFimbriae ProteinsFlagellinInflammasomesInterleukin-1betaMacrophagesMass SpectrometryApoptosis Regulatory ProteinsCalcium-Binding ProteinsCARD Signaling Adaptor ProteinsCarrier ProteinsCaspase 1Cytoskeletal ProteinsFimbriae ProteinsFlagellinInflammasomesInterleukin-1betaIpaf protein, mouseNLR Family, Pyrin Domain-Containing 3 ProteinNlrp3 protein, mousePycard protein, mouse

Identifiers

PMID20955240
PMCPMC3429865
OpenAlexW2121596705

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.