Pyroptosis: host cell death and inflammation (original) (raw)
Samali, A., Zhivotovsky, B., Jones, D., Nagata, S. & Orrenius, S. Apoptosis: cell death defined by caspase activation. Cell Death Differ.6, 495–496 (1999). ArticleCASPubMed Google Scholar
Albert, M. L. Death-defying immunity: do apoptotic cells influence antigen processing and presentation? Nature Rev. Immunol.4, 223–231 (2004). ArticleCAS Google Scholar
Fink, S. L. & Cookson, B. T. Apoptosis, pyroptosis, and necrosis: mechanistic description of dead and dying eukaryotic cells. Infect. Immun.73, 1907–1916 (2005). ArticleCASPubMedPubMed Central Google Scholar
Frantz, S. et al. Targeted deletion of caspase-1 reduces early mortality and left ventricular dilatation following myocardial infarction. J. Mol. Cell. Cardiol.35, 685–694 (2003). ArticleCASPubMed Google Scholar
Fantuzzi, G. & Dinarello, C. A. Interleukin-18 and interleukin-1 beta: two cytokine substrates for ICE (caspase-1). J. Clin. Immunol.19, 1–11 (1999). ArticleCASPubMed Google Scholar
Brennan, M. A. & Cookson, B. T. Salmonella induces macrophage death by caspase-1-dependent necrosis. Mol. Microbiol.38, 31–40 (2000). ArticleCASPubMed Google Scholar
Fink, S. L. & Cookson, B. T. Caspase-1-dependent pore formation during pyroptosis leads to osmotic lysis of infected host macrophages. Cell. Microbiol.8, 1812–1825 (2006). Mechanistic description of the features of pyroptosis, including the identification of caspase 1-dependent membrane pore formation, which leads to cell lysis. ArticleCASPubMed Google Scholar
Hersh, D. et al. The Salmonella invasin SipB induces macrophage apoptosis by binding to caspase-1. Proc. Natl Acad. Sci. USA96, 2396–2401 (1999). ArticleCASPubMedPubMed Central Google Scholar
Chen, Y., Smith, M. R., Thirumalai, K. & Zychlinsky, A. A bacterial invasin induces macrophage apoptosis by binding directly to ICE. EMBO J.15, 3853–3860 (1996). First description of caspase 1 activity that led to pathogen-induced cell death. ArticleCASPubMedPubMed Central Google Scholar
Hilbi, H. et al. _Shigella_-induced apoptosis is dependent on caspase-1 which binds to IpaB. J. Biol. Chem.273, 32895–32900 (1998). ArticleCASPubMed Google Scholar
Zhou, X. et al. Nitric oxide induces thymocyte apoptosis via a caspase-1-dependent mechanism. J. Immunol.165, 1252–1258 (2000). ArticleCASPubMed Google Scholar
Bergsbaken, T. & Cookson, B. T. Macrophage activation redirects _Yersinia_-infected host cell death from apoptosis to caspase-1-dependent pyroptosis. PLoS Pathog.3, e161 (2007). This study demonstrated host redirection of cell death from apoptosis to pyroptosis in activated macrophages in response toYersiniainfection. ArticlePubMedPubMed CentralCAS Google Scholar
Cookson, B. T. & Brennan, M. A. Pro-inflammatory programmed cell death. Trends Microbiol.9, 113–114 (2001). ArticleCASPubMed Google Scholar
Li, P. et al. Mice deficient in IL-1β-converting enzyme are defective in production of mature IL-1β and resistant to endotoxic shock. Cell80, 401–411 (1995). ArticleCASPubMed Google Scholar
Kuida, K. et al. Altered cytokine export and apoptosis in mice deficient in interleukin-1 beta converting enzyme. Science267, 2000–2003 (1995). ArticleCASPubMed Google Scholar
Jesenberger, V., Procyk, K. J., Yuan, J., Reipert, S. & Baccarini, M. _Salmonella_-induced caspase-2 activation in macrophages: a novel mechanism in pathogen-mediated apoptosis. J. Exp. Med.192, 1035–1046 (2000). ArticleCASPubMedPubMed Central Google Scholar
Kelk, P., Johansson, A., Claesson, R., Hanstrom, L. & Kalfas, S. Caspase 1 involvement in human monocyte lysis induced by Actinobacillus actinomycetemcomitans leukotoxin. Infect. Immun.71, 4448–4455 (2003). ArticleCASPubMedPubMed Central Google Scholar
Sun, G. W., Lu, J., Pervaiz, S., Cao, W. P. & Gan, Y. H. Caspase-1 dependent macrophage death induced by Burkholderia pseudomallei. Cell. Microbiol.7, 1447–1458 (2005). ArticleCASPubMed Google Scholar
Cervantes, J., Nagata, T., Uchijima, M., Shibata, K. & Koide, Y. Intracytosolic Listeria monocytogenes induces cell death through caspase-1 activation in murine macrophages. Cell. Microbiol.10, 41–52 (2008). CASPubMed Google Scholar
Fink, S. L., Bergsbaken, T. & Cookson, B. T. Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms. Proc. Natl Acad. Sci. USA105, 4312–4317 (2008). This study showed that distinct events which lead to caspase 1 activation, and ultimately cell death, occur through a common pathway of caspase 1-mediated pyroptosis. ArticleCASPubMedPubMed Central Google Scholar
Thumbikat, P., Dileepan, T., Kannan, M. S. & Maheswaran, S. K. Mechanisms underlying Mannheimia haemolytica leukotoxin-induced oncosis and apoptosis of bovine alveolar macrophages. Microb. Pathog.38, 161–172 (2005). ArticleCASPubMed Google Scholar
Ren, T., Zamboni, D. S., Roy, C. R., Dietrich, W. F. & Vance, R. E. Flagellin-deficient Legionella mutants evade caspase-1- and Naip5-mediated macrophage immunity. PLoS Pathog.2, e18 (2006). ArticlePubMedPubMed CentralCAS Google Scholar
Molofsky, A. B. et al. Cytosolic recognition of flagellin by mouse macrophages restricts Legionella pneumophila infection. J. Exp. Med.203, 1093–1104 (2006). ArticleCASPubMedPubMed Central Google Scholar
Mariathasan, S., Weiss, D. S., Dixit, V. M. & Monack, D. M. Innate immunity against Francisella tularensis is dependent on the ASC/caspase-1 axis. J. Exp. Med.202, 1043–1049 (2005). ArticleCASPubMedPubMed Central Google Scholar
van der Velden, A. W., Velasquez, M. & Starnbach, M. N. Salmonella rapidly kill dendritic cells via a caspase-1-dependent mechanism. J. Immunol.171, 6742–6749 (2003). ArticleCASPubMed Google Scholar
Edgeworth, J. D., Spencer, J., Phalipon, A., Griffin, G. E. & Sansonetti, P. J. Cytotoxicity and interleukin-1β processing following Shigella flexneri infection of human monocyte-derived dendritic cells. Eur. J. Immunol.32, 1464–1471 (2002). ArticleCASPubMed Google Scholar
Monack, D. M., Raupach, B., Hromockyj, A. E. & Falkow, S. Salmonella typhimurium invasion induces apoptosis in infected macrophages. Proc. Natl Acad. Sci. USA93, 9833–9838 (1996). ArticleCASPubMedPubMed Central Google Scholar
Hilbi, H., Chen, Y., Thirumalai, K. & Zychlinsky, A. The interleukin 1β-converting enzyme, caspase 1, is activated during _Shigella flexneri_-induced apoptosis in human monocyte-derived macrophages. Infect. Immun.65, 5165–5170 (1997). ArticleCASPubMedPubMed Central Google Scholar
Watson, P. R. et al. Salmonella enterica serovars Typhimurium and Dublin can lyse macrophages by a mechanism distinct from apoptosis. Infect. Immun.68, 3744–3747 (2000). ArticleCASPubMedPubMed Central Google Scholar
Wickliffe, K. E., Leppla, S. H. & Moayeri, M. Killing of macrophages by anthrax lethal toxin: involvement of the N-end rule pathway. Cell. Microbiol.10, 1352–1362 (2008). ArticleCASPubMedPubMed Central Google Scholar
Shao, W., Yeretssian, G., Doiron, K., Hussain, S. N. & Saleh, M. The caspase-1 digestome identifies the glycolysis pathway as a target during infection and septic shock. J. Biol. Chem.282, 36321–36329 (2007). ArticleCASPubMed Google Scholar
Kufer, T. A. & Sansonetti, P. J. Sensing of bacteria: NOD a lonely job. Curr. Opin. Microbiol.10, 62–69 (2007). ArticleCASPubMed Google Scholar
Martinon, F. & Tschopp, J. Inflammatory caspases and inflammasomes: master switches of inflammation. Cell Death Differ.14, 10–22 (2007). ArticleCASPubMed Google Scholar
Kahlenberg, J. M., Lundberg, K. C., Kertesy, S. B., Qu, Y. & Dubyak, G. R. Potentiation of caspase-1 activation by the P2X7 receptor is dependent on TLR signals and requires NF-κB-driven protein synthesis. J. Immunol.175, 7611–7622 (2005). ArticleCASPubMed Google Scholar
Le Feuvre, R. A., Brough, D., Iwakura, Y., Takeda, K. & Rothwell, N. J. Priming of macrophages with lipopolysaccharide potentiates P2X7-mediated cell death via a caspase-1-dependent mechanism, independently of cytokine production. J. Biol. Chem.277, 3210–3218 (2002). ArticleCASPubMed Google Scholar
Mariathasan, S. et al. Cryopyrin activates the inflammasome in response to toxins and ATP. Nature440, 228–232 (2006). ArticleCASPubMed Google Scholar
Gurcel, L., Abrami, L., Girardin, S., Tschopp, J. & van der Goot, F. G. Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival. Cell126, 1135–1145 (2006). ArticleCASPubMed Google Scholar
Koo, I. C. et al. ESX-1-dependent cytolysis in lysosome secretion and inflammasome activation during mycobacterial infection. Cell. Microbiol.10, 1866–1878 (2008). ArticleCASPubMedPubMed Central Google Scholar
Kanneganti, T. D. et al. Pannexin-1-mediated recognition of bacterial molecules activates the cryopyrin inflammasome independent of Toll-like receptor signaling. Immunity26, 433–443 (2007). ArticleCASPubMed Google Scholar
Kanneganti, T. D. et al. Critical role for cryopyrin/Nalp3 in activation of caspase-1 in response to viral infection and double-stranded RNA. J. Biol. Chem.281, 36560–36568 (2006). ArticleCASPubMed Google Scholar
Martinon, F., Petrilli, V., Mayor, A., Tardivel, A. & Tschopp, J. Gout-associated uric acid crystals activate the NALP3 inflammasome. Nature440, 237–241 (2006). ArticleCASPubMed Google Scholar
Muruve, D. A. et al. The inflammasome recognizes cytosolic microbial and host DNA and triggers an innate immune response. Nature452, 103–107 (2008). ArticleCASPubMed Google Scholar
Kanneganti, T. D. et al. Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3. Nature440, 233–236 (2006). ArticleCASPubMed Google Scholar
Feldmeyer, L. et al. The inflammasome mediates UVB-induced activation and secretion of interleukin-1β by keratinocytes. Curr. Biol.17, 1140–1145 (2007). ArticleCASPubMed Google Scholar
Perregaux, D. et al. IL-1β maturation: evidence that mature cytokine formation can be induced specifically by nigericin. J. Immunol.149, 1294–1303 (1992). CASPubMed Google Scholar
Kahlenberg, J. M. & Dubyak, G. R. Mechanisms of caspase-1 activation by P2X7 receptor-mediated K+ release. Am. J. Physiol. Cell Physiol.286, C1100–C1108 (2004). ArticleCASPubMed Google Scholar
Franchi, L., Kanneganti, T. D., Dubyak, G. R. & Nunez, G. Differential requirement of P2X7 receptor and intracellular K+ for caspase-1 activation induced by intracellular and extracellular bacteria. J. Biol. Chem.282, 18810–18818 (2007). ArticleCASPubMed Google Scholar
Pelegrin, P. & Surprenant, A. Pannexin-1 couples to maitotoxin- and nigericin-induced interleukin-1β release through a dye uptake-independent pathway. J. Biol. Chem.282, 2386–2394 (2007). ArticleCASPubMed Google Scholar
Petrilli, V. et al. Activation of the NALP3 inflammasome is triggered by low intracellular potassium concentration. Cell Death Differ.14, 1583–1589 (2007). ArticleCASPubMed Google Scholar
Wickliffe, K. E., Leppla, S. H. & Moayeri, M. Anthrax lethal toxin-induced inflammasome formation and caspase-1 activation are late events dependent on ion fluxes and the proteasome. Cell. Microbiol.10, 332–343 (2008). ArticleCASPubMed Google Scholar
Fernandes-Alnemri, T. et al. The pyroptosome: a supramolecular assembly of ASC dimers mediating inflammatory cell death via caspase 1 activation. Cell Death Differ.14, 1590–1604 (2007). This study found that a macromolecular structure which contained ASC and caspase-1 was formed during pyroptosis. ArticleCASPubMed Google Scholar
Miao, E. A. et al. Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1β via Ipaf. Nature Immunol.7, 569–575 (2006). ArticleCAS Google Scholar
Franchi, L. et al. Cytosolic flagellin requires Ipaf for activation of caspase-1 and interleukin 1β in _Salmonella_-infected macrophages. Nature Immunol.7, 576–582 (2006). Together with References 23 and 55, this study found that bacterial flagellin and the host protein NLRC4 are required for the activation of caspase 1 during infection withLegionellaandSalmonella. ArticleCAS Google Scholar
Zamboni, D. S. et al. The Birc1e cytosolic pattern-recognition receptor contributes to the detection and control of Legionella pneumophila infection. Nature Immunol.7, 318–325 (2006). ArticleCAS Google Scholar
Miao, E. A., Ernst, R. K., Dors, M., Mao, D. P. & Aderem, A. Pseudomonas aeruginosa activates caspase 1 through Ipaf. Proc. Natl Acad. Sci. USA105, 2562–2567 (2008). ArticleCASPubMedPubMed Central Google Scholar
Franchi, L. et al. Critical role for Ipaf in _Pseudomonas aeruginosa_-induced caspase-1 activation. Eur. J. Immunol.37, 3030–3039 (2007). ArticleCASPubMed Google Scholar
Warren, S. E., Mao, D. P., Rodriguez, A. E., Miao, E. A. & Aderem, A. Multiple Nod-like receptors activate caspase 1 during Listeria monocytogenes infection. J. Immunol.180, 7558–7564 (2008). ArticleCASPubMed Google Scholar
Lightfield, K. L. et al. Critical function for Naip5 in inflammasome activation by a conserved carboxy-terminal domain of flagellin. Nature Immunol.9, 1171–1178 (2008). ArticleCAS Google Scholar
Sutterwala, F. S. et al. Immune recognition of Pseudomonas aeruginosa mediated by the IPAF/NLRC4 inflammasome. J. Exp. Med.204, 3235–3245 (2007). ArticleCASPubMedPubMed Central Google Scholar
Suzuki, T. et al. Differential regulation of caspase-1 activation, pyroptosis, and autophagy via Ipaf and ASC in _Shigella_-infected macrophages. PLoS Pathog.3, e111 (2007). ArticlePubMedPubMed CentralCAS Google Scholar
Boyden, E. D. & Dietrich, W. F. Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin. Nature Genet.38, 240–244 (2006). ArticleCASPubMed Google Scholar
Martinon, F., Burns, K. & Tschopp, J. The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-β. Mol. Cell10, 417–426 (2002). First description of the inflammasome as a caspase 1-activating platform. ArticleCASPubMed Google Scholar
Faustin, B. et al. Reconstituted NALP1 inflammasome reveals two-step mechanism of caspase-1 activation. Mol. Cell25, 713–724 (2007). ArticleCASPubMed Google Scholar
Poyet, J. L. et al. Identification of Ipaf, a human caspase-1-activating protein related to Apaf-1. J. Biol. Chem.276, 28309–28313 (2001). ArticleCASPubMed Google Scholar
Mariathasan, S. et al. Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf. Nature430, 213–218 (2004). ArticleCASPubMed Google Scholar
Schmidt, M., Hanna, J., Elsasser, S. & Finley, D. Proteasome-associated proteins: regulation of a proteolytic machine. Biol. Chem.386, 725–737 (2005). ArticleCASPubMed Google Scholar
Bao, Q. & Shi, Y. Apoptosome: a platform for the activation of initiator caspases. Cell Death Differ.14, 56–65 (2007). ArticleCASPubMed Google Scholar
Amer, A. O. & Swanson, M. S. Autophagy is an immediate macrophage response to Legionella pneumophila. Cell. Microbiol.7, 765–778 (2005). ArticleCASPubMedPubMed Central Google Scholar
Swanson, M. S. & Molofsky, A. B. Autophagy and inflammatory cell death, partners of innate immunity. Autophagy1, 174–176 (2005). ArticleCASPubMed Google Scholar
Checroun, C., Wehrly, T. D., Fischer, E. R., Hayes, S. F. & Celli, J. Autophagy-mediated reentry of Francisella tularensis into the endocytic compartment after cytoplasmic replication. Proc. Natl Acad. Sci. USA103, 14578–14583 (2006). ArticleCASPubMedPubMed Central Google Scholar
Willingham, S. B. et al. Microbial pathogen-induced necrotic cell death mediated by the inflammasome components CIAS1/cryopyrin/NLRP3 and ASC. Cell Host Microbe2, 147–159 (2007). ArticleCASPubMedPubMed Central Google Scholar
Hernandez, L. D., Pypaert, M., Flavell, R. A. & Galan, J. E. A Salmonella protein causes macrophage cell death by inducing autophagy. J. Cell Biol.163, 1123–1131 (2003). ArticleCASPubMedPubMed Central Google Scholar
Delaleu, N. & Bickel, M. Interleukin-1β and interleukin-18: regulation and activity in local inflammation. Periodontol. 200035, 42–52 (2004). ArticlePubMed Google Scholar
Nakanishi, K., Yoshimoto, T., Tsutsui, H. & Okamura, H. Interleukin-18 regulates both Th1 and Th2 responses. Annu. Rev. Immunol.19, 423–474 (2001). ArticleCASPubMed Google Scholar
Monack, D. M., Detweiler, C. S. & Falkow, S. Salmonella pathogenicity island 2-dependent macrophage death is mediated in part by the host cysteine protease caspase-1. Cell. Microbiol.3, 825–837 (2001). ArticleCASPubMed Google Scholar
Andrei, C. et al. The secretory route of the leaderless protein interleukin 1β involves exocytosis of endolysosome-related vesicles. Mol. Biol. Cell10, 1463–1475 (1999). ArticleCASPubMedPubMed Central Google Scholar
Andrei, C. et al. Phospholipases C and A2 control lysosome-mediated IL-1β secretion: implications for inflammatory processes. Proc. Natl Acad. Sci. USA101, 9745–9750 (2004). ArticleCASPubMedPubMed Central Google Scholar
Brough, D. & Rothwell, N. J. Caspase-1-dependent processing of pro-interleukin-1β is cytosolic and precedes cell death. J. Cell Sci.120, 772–781 (2007). ArticleCASPubMed Google Scholar
Qu, Y., Franchi, L., Nunez, G. & Dubyak, G. R. Nonclassical IL-1β secretion stimulated by P2X7 receptors is dependent on inflammasome activation and correlated with exosome release in murine macrophages. J. Immunol.179, 1913–1925 (2007). ArticleCASPubMed Google Scholar
Pizzirani, C. et al. Stimulation of P2 receptors causes release of IL-1β-loaded microvesicles from human dendritic cells. Blood109, 3856–3864 (2007). ArticleCASPubMed Google Scholar
Bianco, F. et al. Astrocyte-derived ATP induces vesicle shedding and IL-1β release from microglia. J. Immunol.174, 7268–7677 (2005). ArticleCASPubMed Google Scholar
MacKenzie, A. et al. Rapid secretion of interleukin-1β by microvesicle shedding. Immunity15, 825–835 (2001). ArticleCASPubMed Google Scholar
Keller, M., Ruegg, A., Werner, S. & Beer, H. D. Active caspase-1 is a regulator of unconventional protein secretion. Cell132, 818–831 (2008). ArticleCASPubMed Google Scholar
Miggin, S. M. et al. NF-κB activation by the Toll-IL-1 receptor domain protein MyD88 adapter-like is regulated by caspase-1. Proc. Natl Acad. Sci. USA104, 3372–3377 (2007). ArticleCASPubMedPubMed Central Google Scholar
Amer, A. et al. Regulation of Legionella phagosome maturation and infection through flagellin and host Ipaf. J. Biol. Chem.281, 35217–35223 (2006). ArticleCASPubMed Google Scholar
Siegel, R. M. Caspases at the crossroads of immune-cell life and death. Nature Rev. Immunol.6, 308–317 (2006). ArticleCAS Google Scholar
Shin, H. & Cornelis, G. R. Type III secretion translocation pores of Yersinia enterocolitica trigger maturation and release of pro-inflammatory IL-1β. Cell. Microbiol.9, 2893–2902 (2007). ArticleCASPubMed Google Scholar
Simon, A. & van der Meer, J. W. Pathogenesis of familial periodic fever syndromes or hereditary autoinflammatory syndromes. Am. J. Physiol. Regul. Integr. Comp. Physiol.292, R86–R98 (2007). ArticleCASPubMed Google Scholar
Schielke, G. P., Yang, G. Y., Shivers, B. D. & Betz, A. L. Reduced ischemic brain injury in interleukin-1β converting enzyme-deficient mice. J. Cereb. Blood Flow Metab.18, 180–185 (1998). ArticleCASPubMed Google Scholar
Siegmund, B., Lehr, H. A., Fantuzzi, G. & Dinarello, C. A. IL-1β-converting enzyme (caspase-1) in intestinal inflammation. Proc. Natl Acad. Sci. USA98, 13249–13254 (2001). ArticleCASPubMedPubMed Central Google Scholar
Ona, V. O. et al. Inhibition of caspase-1 slows disease progression in a mouse model of Huntington's disease. Nature399, 263–267 (1999). ArticleCASPubMed Google Scholar
Wang, W. et al. Endotoxemic acute renal failure is attenuated in caspase-1-deficient mice. Am. J. Physiol. Renal Physiol.288, F997–F1004 (2005). ArticleCASPubMed Google Scholar
Faubel, S. et al. Cisplatin-induced acute renal failure is associated with an increase in the cytokines interleukin (IL)-1, IL-18, IL-6, and neutrophil infiltration in the kidney. J. Pharmacol. Exp. Ther.322, 8–15 (2007). ArticleCASPubMed Google Scholar
Sarkar, A. et al. Caspase-1 regulates Escherichia coli sepsis and splenic B cell apoptosis independently of interleukin-1β and interleukin-18. Am. J. Respir. Crit. Care Med.174, 1003–1010 (2006). ArticleCASPubMedPubMed Central Google Scholar
Raupach, B., Peuschel, S. K., Monack, D. M. & Zychlinsky, A. Caspase-1-mediated activation of interleukin-1β (IL-1β) and IL-18 contributes to innate immune defenses against Salmonella enterica serovar Typhimurium infection. Infect. Immun.74, 4922–4926 (2006). ArticleCASPubMedPubMed Central Google Scholar
Sansonetti, P. J. et al. Caspase-1 activation of IL-1β and IL-18 are essential for _Shigella flexneri_-induced inflammation. Immunity12, 581–590 (2000). ArticleCASPubMed Google Scholar
Pedra, J. H. et al. ASC/PYCARD and caspase-1 regulate the IL-18/IFN-γ axis during Anaplasma phagocytophilum infection. J. Immunol.179, 4783–4791 (2007). ArticleCASPubMed Google Scholar
Tsuji, N. M. et al. Roles of caspase-1 in Listeria infection in mice. Int. Immunol.16, 335–343 (2004). ArticleCASPubMed Google Scholar
Henry, T. & Monack, D. M. Activation of the inflammasome upon Francisella tularensis infection: interplay of innate immune pathways and virulence factors. Cell Microbiol.9, 2543–2551 (2007). Identified a role for type I IFN signalling in priming macrophages to undergo pyroptosis in response toFrancisellainfection. ArticleCASPubMed Google Scholar
Mencacci, A. et al. Interleukin 18 restores defective Th1 immunity to Candida albicans in caspase 1-deficient mice. Infect. Immun.68, 5126–5131 (2000). ArticleCASPubMedPubMed Central Google Scholar
Shi, Y., Evans, J. E. & Rock, K. L. Molecular identification of a danger signal that alerts the immune system to dying cells. Nature425, 516–521 (2003). ArticleCASPubMed Google Scholar
Mariathasan, S. & Monack, D. M. Inflammasome adaptors and sensors: intracellular regulators of infection and inflammation. Nature Rev. Immunol.7, 31–40 (2007). ArticleCAS Google Scholar
Kool, M. et al. Alum adjuvant boosts adaptive immunity by inducing uric acid and activating inflammatory dendritic cells. J. Exp. Med.205, 869–882 (2008). ArticleCASPubMedPubMed Central Google Scholar
Kool, M. et al. Cutting edge: alum adjuvant stimulates inflammatory dendritic cells through activation of the NALP3 inflammasome. J. Immunol.181, 3755–3759 (2008). ArticleCASPubMed Google Scholar
Eisenbarth, S. C., Colegio, O. R., O'Connor, W., Sutterwala, F. S. & Flavell, R. A. Crucial role for the Nalp3 inflammasome in the immunostimulatory properties of aluminium adjuvants. Nature453, 1122–1126 (2008). Showed that the adjuvant activity of alum is due to its ability to stimulate caspase 1 activation, highlighting the role of caspase 1 in the enhancement of adaptive immunity. ArticleCASPubMedPubMed Central Google Scholar
Franchi, L. & Nunez, G. The Nlrp3 inflammasome is critical for aluminium hydroxide-mediated IL-1β secretion but dispensable for adjuvant activity. Eur. J. Immunol.38, 2085–2089 (2008). ArticleCASPubMedPubMed Central Google Scholar
Li, H., Willingham, S. B., Ting, J. P. & Re, F. Cutting edge: inflammasome activation by alum and alum's adjuvant effect are mediated by NLRP3. J. Immunol.181, 17–21 (2008). ArticleCASPubMed Google Scholar
Lockman, H. A. & Curtiss, R. 3rd. Salmonella typhimurium mutants lacking flagella or motility remain virulent in BALB/c mice. Infect. Immun.58, 137–143 (1990). ArticleCASPubMedPubMed Central Google Scholar
Hammer, B. K. & Swanson, M. S. Co-ordination of Legionella pneumophila virulence with entry into stationary phase by ppGpp. Mol. Microbiol.33, 721–731 (1999). ArticleCASPubMed Google Scholar
Cummings, L. A., Barrett, S. L., Wilkerson, W. D., Fellnerova, I. & Cookson, B. T. FliC-specific CD4+ T cell responses are restricted by bacterial regulation of antigen expression. J. Immunol.174, 7929–7938 (2005). ArticleCASPubMed Google Scholar
Johnston, J. B. et al. A poxvirus-encoded pyrin domain protein interacts with ASC-1 to inhibit host inflammatory and apoptotic responses to infection. Immunity23, 587–598 (2005). This study identified a microbial protein that is capable of inhibiting caspase 1 activation by disrupting inflammasome formation. ArticleCASPubMed Google Scholar
Stasakova, J. et al. Influenza A mutant viruses with altered NS1 protein function provoke caspase-1 activation in primary human macrophages, resulting in fast apoptosis and release of high levels of interleukins 1β and 18. J. Gen. Virol.86, 185–195 (2005). ArticleCASPubMed Google Scholar
Schotte, P. et al. Targeting Rac1 by the Yersinia effector protein YopE inhibits caspase-1-mediated maturation and release of interleukin-1β. J. Biol. Chem.279, 25134–25142 (2004). ArticleCASPubMed Google Scholar
Weiss, D. S. et al. In vivo negative selection screen identifies genes required for Francisella virulence. Proc. Natl Acad. Sci. USA104, 6037–6042 (2007). ArticleCASPubMedPubMed Central Google Scholar
Henry, T., Brotcke, A., Weiss, D. S., Thompson, L. J. & Monack, D. M. Type I interferon signaling is required for activation of the inflammasome during Francisella infection. J. Exp. Med.204, 987–994 (2007). ArticleCASPubMedPubMed Central Google Scholar
Kerr, J. F., Wyllie, A. H. & Currie, A. R. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer26, 239–257 (1972). ArticleCASPubMedPubMed Central Google Scholar
Majno, G. & Joris, I. Apoptosis, oncosis, and necrosis. An overview of cell death. Am. J. Pathol.146, 3–15 (1995). CASPubMedPubMed Central Google Scholar
Fernandez-Prada, C. M., Hoover, D. L., Tall, B. D. & Venkatesan, M. M. Human monocyte-derived macrophages infected with virulent Shigella flexneri in vitro undergo a rapid cytolytic event similar to oncosis but not apoptosis. Infect. Immun.65, 1486–1496 (1997). ArticleCASPubMedPubMed Central Google Scholar