Evidence map›Paper›PMID 19717510›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2009

A critical role for hemolysins and bacterial lipoproteins in Staphylococcus aureus-induced activation of the Nlrp3 inflammasome.

Raúl Muñoz-Planillo, Luigi Franchi, Lloyd S Miller, Gabriel Núñez

Open access · bronzeAbstract read
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 202 papers.

0numbers the graph read from it
0cells of the map it votes in
202citing papers in PubMed
10.9field-weighted citation impact, top 1% 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

202 citing papers in PubMed, 325 citations in OpenAlex.

  1. Trial
  2. An underlying mechanism of bovine mastitis: PGEThe veterinary quarterly · 2026
    Article
  3. Article
  4. Article
  5. Infection and immunity · 2026
    Article
  6. Infection and immunity · 2026
    Article
  7. Review
  8. [Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2026
    Article
  9. α-hemolysin polymorphisms in methicillin-resistantbioRxiv : the preprint server for biology · 2025
    Article
  10. bioRxiv : the preprint server for biology · 2025
    Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Investigation ofMicroorganisms · 2024
    Article
  18. Review
  19. Article
  20. Article

142 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

4 authors at 3 institutions in 1 country.

Raúl Muñoz-PlanilloDepartment of Pathology and Comprehensive Cancer Center, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
Luigi Franchi
Lloyd S Miller
Gabriel Núñez
University of Michigan–Ann Arbor · USMichigan Center for Translational Pathology · USUniversity of California, Los Angeles · US

Funding

Cryopyrin/NLRP3 Signaling in Inflammation and Innate ImmunityR37AI063331 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI NUNEZ, GABRIEL · 2016 to 2025
$3.9M
Cryopyrin Signaling in Inflammation and Innate ImmunityR01AI063331 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI NUNEZ, GABRIEL · 2005 to 2015
$3.3M
Role of Ipaf in Inflammation and Host DefenseR01AI064748 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI NUNEZ, GABRIEL · 2005 to 2009
$1.6M
Role of ASC signaling Pathway in Inflammatory DiseaseR01AR052756 · NIAMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI NUNEZ, GABRIEL · 2006 to 2010
$1.4M
Cryopyrin/NLRP3 Signaling in Inflammation and Innate ImmunityR56AI063331 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI NUNEZ, GABRIEL · 2010 to 2010
$386k
NIAID NIH HHS AI063331NIAID NIH HHS AI064748NIAID NIH HHS R01 AI063331NIAID NIH HHS R01 AI064748NIAID NIH HHS R37 AI063331NIAID NIH HHS R56 AI063331NIAMS NIH HHS R01 AR052756
6 · The paper itself

Abstract

The mechanism by which bacterial pathogens activate caspase-1 via Nlrp3 remains poorly understood. In this study, we show that the ability of Staphylococcus aureus, a leading cause of infection in humans, to activate caspase-1 and induce IL-1beta secretion resides in culture supernatants of growing bacteria. Caspase-1 activation induced by S. aureus required alpha-, beta-, and gamma-hemolysins and the host Nlrp3 inflammasome. Mechanistically, alpha- and beta-hemolysins alone did not trigger caspase-1 activation, but they did so in the presence of bacterial lipoproteins released by S. aureus. Notably, caspase-1 activation induced by S. aureus supernatant was independent of the P2X7 receptor and the essential TLR adaptors MyD88 and TIR domain-containing adapter-inducing IFN-beta, but was inhibited by extracellular K(+). These results indicate that S. aureus hemolysins circumvent the requirement of ATP and the P2X7 receptor to induce caspase-1 activation via Nlrp3. Furthermore, these studies revealed that hemolysins promote in the presence of lipoproteins the activation of the Nlrp3 inflammasome.

Indexed as

Adenosine TriphosphateAnimalsBacterial ProteinsCarrier ProteinsCaspase 1Hemolysin ProteinsInflammationInterleukin-1betaLipoproteinsMiceMice, KnockoutMultiprotein ComplexesNLR Family, Pyrin Domain-Containing 3 ProteinPotassiumReceptors, Purinergic P2Receptors, Purinergic P2X7Adenosine TriphosphateBacterial ProteinsCarrier ProteinsCaspase 1Hemolysin ProteinsInterleukin-1betaLipoproteinsMultiprotein ComplexesNLR Family, Pyrin Domain-Containing 3 ProteinNlrp3 protein, mouseP2RX7 protein, humanP2rx7 protein, mousePotassiumReceptors, Purinergic P2Receptors, Purinergic P2X7

Identifiers

PMID19717510
PMCPMC2762867
OpenAlexW2127453904

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.