Cryopyrin activates the inflammasome in response to toxins and ATP

Sanjeev Mariathasan, David S. Weiss, Kim Newton, Jacqueline McBride, Karen O'Rourke, Meron Roose-Girma, Wyne P. Lee, Yvette Weinrauch, Denise M. Monack and Vishva M. Dixit ()
Additional contact information
Sanjeev Mariathasan: Molecular Oncology Department
David S. Weiss: Stanford University School of Medicine
Kim Newton: Molecular Oncology Department
Jacqueline McBride: Genentech Inc
Karen O'Rourke: Molecular Oncology Department
Meron Roose-Girma: Physiology Department
Wyne P. Lee: Genentech Inc
Yvette Weinrauch: New York University School of Medicine
Denise M. Monack: Stanford University School of Medicine
Vishva M. Dixit: Molecular Oncology Department

Nature, 2006, vol. 440, issue 7081, 228-232

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
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DOI: 10.1038/nature04515

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