Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3

Thirumala-Devi Kanneganti, Nesrin Özören, Mathilde Body-Malapel, Amal Amer, Jong-Hwan Park, Luigi Franchi, Joel Whitfield, Winfried Barchet, Marco Colonna, Peter Vandenabeele, John Bertin, Anthony Coyle, Ethan P. Grant, Shizuo Akira and Gabriel Núñez ()
Additional contact information
Thirumala-Devi Kanneganti: University of Michigan Medical School
Nesrin Özören: University of Michigan Medical School
Mathilde Body-Malapel: University of Michigan Medical School
Amal Amer: University of Michigan Medical School
Jong-Hwan Park: University of Michigan Medical School
Luigi Franchi: University of Michigan Medical School
Joel Whitfield: University of Michigan Medical School
Winfried Barchet: Washington University School of Medicine
Marco Colonna: Washington University School of Medicine
Peter Vandenabeele: Ghent University
John Bertin: Millennium Pharmaceuticals Inc.
Anthony Coyle: Millennium Pharmaceuticals Inc.
Ethan P. Grant: Millennium Pharmaceuticals Inc.
Shizuo Akira: Osaka University
Gabriel Núñez: University of Michigan Medical School

Nature, 2006, vol. 440, issue 7081, 233-236

Abstract: The first line of defence The inflammasome is a complex of proteins involved in the activation of the innate immune system, an evolutionarily ancient antimicrobial defence found in most multicelled animals. When activated the inflammasome sets in motion a cascade of events that leads to the production of active molecules including interleukins. Three papers in this issue report the identification of endogenous danger signals and bacterial components that activate inflammasomes containing cryopyrin (also known as NALP3). Mariathasan et al. show that cryopyrin activates the inflammasome in response to bacterial toxins and to ATP. Kanneganti et al. show that cryopyrin is activated by bacterial RNA and by the immune response modifiers R837 and R848. And Martinon et al. show that gout-associated uric acid crystals have a similar effect. In sum these results show that cryopyrin has a vital role in host antibacterial defences and may act as a sensor of cellular stress. In addition, this work provides insight into the mechanisms of autoinflammatory disorders in which abnormalities in the innate immune system have been implicated.

Date: 2006
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/nature04517 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:440:y:2006:i:7081:d:10.1038_nature04517

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature04517

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().