Pyroptosis: Host cell death and inflammation

Nature Reviews Microbiology

Volumn 7, Issue 2, 2009, Pages 99-109

  Bergsbaken, Tessa ^a   Fink, Susan L ^a   Cookson, Brad T ^a  

^a UNIVERSITY OF WASHINGTON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOKINE; INTERLEUKIN 18; INTERLEUKIN 1BETA; INTERLEUKIN 1BETA CONVERTING ENZYME; TOLL LIKE RECEPTOR;

BACTERIAL GROWTH; CELL ACTIVATION; CELL DEATH; CELL DESTRUCTION; CELL REGENERATION; CELL SURVIVAL; CEREBROVASCULAR ACCIDENT; CYTOKINE RELEASE; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME REGULATION; EUKARYOTIC CELL; GROWTH INHIBITION; HEART INFARCTION; HOST CELL; HOST PATHOGEN INTERACTION; HUMAN; IMMUNE RESPONSE; INFECTION; INFLAMMATION; MOLECULAR MECHANICS; NEOPLASM; NONHUMAN; PERSISTENT INFECTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN PROCESSING; PYROPTOSIS; REVIEW;

ANIMALS; APOPTOSIS; CASPASE 1; FEVER; HUMANS; INFLAMMATION; MICE;

EUKARYOTA;

EID: 58449083290     PISSN: 17401526     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrmicro2070     Document Type: Review

References (124)

1. Samali, A., Zhivotovsky, B., Jones, D., Nagata, S. & Orrenius, S. Apoptosis: Cell death defined by caspase activation. Cell Death Differ. 6, 495-496 (1999).
2. Albert, M. L. Death-defying immunity: Do apoptotic cells influence antigen processing and presentation? Nature Rev. Immunol. 4b 223-231 (2004).
3. Fink, S. L. & Cookson, B. T. Apoptosis, pyroptosis, and necrosis: mechanistic description of dead and dying eukaryotic cells. Infect. Immun. 73, 1907-1916 (2005).
4. 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).
5. 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).
6. Brennan, M. A. & Cookson, B. T. Salmonella induces macrophage death by caspase-1-dependent necrosis. Mol. Microbiol. 38, 31-40 (2000).
7. 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).
8. Hersh, D. et al. The Salmonella invasin SipB induces macrophage apoptosis by binding to caspase-1. Proc. Natl Acad. Sci. USA 96, 2396-2401 (1999).
9. 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).
10. Hilbi, H. et al. Shigella-induced apoptosis is dependent on caspase-1 which binds to IpaB. J. Biol. Chem. 273, 32895-32900 (1998).
11. Zhou, X. et al. Nitric oxide induces thymocyte apoptosis via a caspase-1-dependent mechanism. J. Immunol. 165, 1252-1258 (2000).
12. 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).
13. Cookson, B. T. & Brennan, M. A. Pro-inflammatory programmed cell death. Trends Microbiol. 9, 113-114 (2001).
14. Li, P. et al. Mice deficient in IL-1β-converting enzyme are defective in production of mature IL-1β and resistant to endotoxic shock. Cell 80, 401-411 (1995).
15. Kuida, K. et al. Altered cytokine export and apoptosis in mice deficient in interleukin-1 beta converting enzyme. Science 267 2000-2003 (1995).
16. 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).
17. 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).
18. 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).
19. 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).
20. 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. USA 105, 4312-4317 (2008).
21. 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).
22. 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).
23. Molofsky, A. B. et al. Cytosolic recognition of flagellin by mouse macrophages restricts Legionella pneumophila infection. J. Exp. Med. 203, 1093-1104 (2006).
24. 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).
25. 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).
26. 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).
27. Monack, D. M., Raupach, B., Hromockyj, A. E. & Falkow, S. Salmonella typhimurium invasion induces apoptosis in infected macrophages. Proc. Natl Acad. Sci. USA 93, 9833-9838 (1996).
28. 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).
29. 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).
30. 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).
31. 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).
32. Matzinger, P. The danger model: A renewed sense of self. Science 296, 301-305 (2002).
33. Kawai, T. & Akira, S. TLR signaling. Semin. Immunol. 19, 24-32 (2007).
34. Kufer, T. A. & Sansonetti, P. J. Sensing of bacteria: NOD a lonely job. Curr. Opin. Microbiol. 10, 62-69 (2007).
35. Martinon, F. & Tschopp, J. Inflammatory caspases and inflammasomes: master switches of inflammation. Cell Death Differ. 14, 10-22 (2007).
36. 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).
37. 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).
38. Mariathasan, S. et al. Cryopyrin activates the inflammasome in response to toxins and ATP. Nature 440, 228-232 (2006).
39. 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. Cell 126 1135-1145 (2006).
40. Koo, I. C. et al. ESX-1-dependent cytolysis in lysosome secretion and inflammasome activation during mycobacterial infection. Cell. Microbiol. 10, 1866-1878 (2008).
41. Kanneganti, T. D. et al. Pannexin-1-mediated recognition of bacterial molecules activates the cryopyrin inflammasome independent of Toll-like receptor signaling. Immunity 26, 433-443 (2007).
42. 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).
43. Martinon, F., Petrilli, V., Mayor, A., Tardivel, A. & Tschopp, J. Gout-associated uric acid crystals activate the NALP3 inflammasome. Nature 440, 237-241 (2006).
44. Muruve, D. A. et al. The inflammasome recognizes cytosolic microbial and host DNA and triggers an innate immune response. Nature 452, 103-107 (2008).
45. Kanneganti, T. D. et al. Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3. Nature 440, 233-236 (2006).
46. Dostert, C. et al. Innate immune activation through Nalp3 inflammasome sensing of asbestos and silica. Science 320, 674-677 (2008).
47. Feldmeyer, L. et al. The inflammasome mediates UVB-induced activation and secretion of interleukin-1β by keratinocytes. Curr. Biol. 17, 1140-1145 (2007).
48. Perregaux, D. et al. IL-1β maturation: Evidence that mature cytokine formation can be induced specifically by nigericin. J. Immunol. 149, 1294-1303 (1992).
49. 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).
50. + for caspase-1 activation induced by intracellular and extracellular bacteria. J. Biol. Chem. 282, 18810-18818 (2007).
51. 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).
52. Petrilli, V. et al. Activation of the NALP3 inflammasome is triggered by low intracellular potassium concentration. Cell Death Differ. 14, 1583-1589 (2007).
53. 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).
54. 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).
55. Miao, E. A. et al. Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1β via Ipaf. Nature Immunol. 7, 569-575 (2006).
56. 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).
57. 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).
58. Miao, E. A., Ernst, R. K., Dors, M., Mao, D. P. & Aderem, A. Pseudomonas aeruginosa activates caspase 1 through Ipaf. Proc. Natl Acad. Sci. USA 105, 2562-2567 (2008).
59. Franchi, L. et al. Critical role for Ipaf in Pseudomonas aeruginosa-induced caspase-1 activation. Eur. J. Immunol. 37 3030-3039 (2007).
60. 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).
61. Lightfield, K. L. et al. Critical function for Naip5 in inflammasome activation by a conserved carboxyterminal domain of flagellin. Nature Immunol. 9, 1171-1178 (2008).
62. Sutterwala, F. S. et al. Immune recognition of Pseudomonas aeruginosa mediated by the IPAF/NLRC4 inflammasome. J. Exp. Med. 204, 3235-3245 (2007).
63. 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).
64. Boyden, E. D. & Dietrich, W. F. Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin. Nature Genet. 38, 240-244 (2006).
65. Martinon, F., Burns, K. & Tschopp, J. The inflammasome: A molecular platform triggering activation of inflammatory caspases and processing of proIL-β. Mol. Cell 10, 417-426 (2002).
66. Faustin, B. et al. Reconstituted NALP1 inflammasome reveals two-step mechanism of caspase-1 activation. Mol. Cell 25, 713-724 (2007).
67. 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).
68. Mariathasan, S. et al. Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf. Nature 430, 213-218 (2004).
69. Schmidt, M., Hanna, J., Elsasser, S. & Finley, D. Proteasome-associated proteins: Regulation of a proteolytic machine. Biol. Chem. 386 725-737 (2005).
70. Bao, Q. & Shi, Y. Apoptosome: A platform for the activation of initiator caspases. Cell Death Differ. 14, 56-65 (2007).
71. Amer, A. O. & Swanson, M. S. Autophagy is an immediate macrophage response to Legionella pneumophila. Cell. Microbiol. 7, 765-778 (2005).
72. Swanson, M. S. & Molofsky, A. B. Autophagy and inflammatory cell death, partners of innate immunity. Autophagy 1, 174-176 (2005).
73. 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. USA 103, 14578-14583 (2006).
74. Willingham, S. B. et al. Microbial pathogen-induced necrotic cell death mediated by the inflammasome components CIAS1/cryopyrin/NLRP3 and ASC. Cell Host Microbe 2, 147-159 (2007).
75. 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).
76. Delaleu, N. & Bickel, M. Interleukin-1β and interleukin-18: Regulation and activity in local inflammation. Periodontol. 2000 35, 42-52 (2004).
77. Nakanishi, K., Yoshimoto, T., Tsutsui, H. & Okamura, H. Interleukin-18 regulates both Th1 and Th2 responses. Annu. Rev. Immunol. 19 423-474 (2001).
78. 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).
79. Andrei, C. et al. The secretory route of the leaderless protein interleukin 1β involves exocytosis of endolysosome-related vesicles. Mol. Biol. Cell 10, 1463-1475 (1999).
80. 2 control lysosome-mediated IL-1β secretion: Implications for inflammatory processes. Proc. Natl Acad. Sci. USA 101, 9745-9750 (2004).
81. 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).
82. 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).
83. Pizzirani, C. et al. Stimulation of P2 receptors causes release of IL-1β-loaded microvesicles from human dendritic cells. Blood 109, 3856-3864 (2007).
84. Bianco, F. et al. Astrocyte-derived ATP induces vesicle shedding and IL-1β release from microglia. J. Immunol. 174, 7268-7677 (2005).
85. MacKenzie, A. et al. Rapid secretion of interleukin-1β by microvesicle shedding. Immunity 15, 825-835 (2001).
86. Keller, M., Ruegg, A., Werner, S. & Beer, H. D. Active caspase-1 is a regulator of unconventional protein secretion. Cell 132, 818-831 (2008).
87. 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. USA 104, 3372-3377 (2007).
88. Amer, A. et al. Regulation of Legionella phagosome maturation and infection through flagellin and host Ipaf. J. Biol. Chem. 281, 35217-35223 (2006).
89. Master, S. S. et al. Mycobacterium tuberculosis prevents inflammasome activation. Cell Host Microbe 3, 224-232 (2008).
90. Siegel, R. M. Caspases at the crossroads of immune-cell life and death. Nature Rev. Immunol. 6, 308-317 (2006).
91. 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).
92. 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).
93. 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).
94. Siegmund, B., Lehr, H. A., Fantuzzi, G. & Dinarello, C. A. IL-1β-converting enzyme (caspase-1) in intestinal inflammation. Proc. Natl Acad. Sci. USA 98, 13249-13254 (2001).
95. Ona, V. O. et al. Inhibition of caspase-1 slows disease progression in a mouse model of Huntington's disease. Nature 399, 263-267 (1999).
96. Wang, W. et al. Endotoxemic acute renal failure is attenuated in caspase-1-deficient mice. Am. J. Physiol. Renal Physiol. 288 F997-F1004 (2005).
97. 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).
98. 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).
99. Lara-Tejero, M. et al. Role of the caspase-1 inflammasome in Salmonella typhimurium pathogenesis. J. Exp. Med. 203, 1407-1412 (2006).
100. 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).
101. Sansonetti, P. J. et al. Caspase-1 activation of IL-1β and IL-18 are essential for Shigella flexneri-induced inflammation. Immunity 12, 581-590 (2000).
102. Pedra, J. H. et al. ASC/PYCARD and caspase-1 regulate the IL-18/ IFN-a axis during Anaplasma phagocytophilum infection. J. Immunol. 179, 4783-4791 (2007).
103. Tsuji, N. M. et al. Roles of caspase-1 in Listeria infection in mice. Int. Immunol. 16, 335-343 (2004).
104. 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 to Francisella infection.
105. Mencacci, A. et al. Interleukin 18 restores defective Th1 immunity to Candida albicans in caspase 1-deficient mice. Infect. Immun. 68, 5126-5131 (2000).
106. Shi, Y., Evans, J. E. & Rock, K. L. Molecular identification of a danger signal that alerts the immune system to dying cells. Nature 425 516-521 (2003).
107. Mariathasan, S. & Monack, D. M. Inflammasome adaptors and sensors: intracellular regulators of infection and inflammation. Nature Rev. Immunol. 7, 31-40 (2007).
108. 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).
109. Kool, M. et al. Cutting edge: Alum adjuvant stimulates inflammatory dendritic cells through activation of the NALP3 inflammasome. J. Immunol. 181, 3755-3759 (2008).
110. 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. Nature 453 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.
111. 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).
112. 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).
113. 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).
114. 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).
115. + T cell responses are restricted by bacterial regulation of antigen expression. J. Immunol. 174, 7929-7938 (2005).
116. Johnston, J. B. et al. A poxvirus-encoded pyrin domain protein interacts with ASC-1 to inhibit host inflammatory and apoptotic responses to infection. Immunity 23, 587-598 (2005). This study identified a microbial protein that is capable of inhibiting caspase 1 activation by disrupting inflammasome formation.
117. 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).
118. 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).
119. Weiss, D. S. et al. In vivo negative selection screen identifies genes required for Francisella virulence. Proc. Natl Acad. Sci. USA 104, 6037-6042 (2007).
120. 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).
121. Esposti, M. D. Apoptosis: Who was first? Cell Death Differ. 5 719 (1998).
122. Kerr, J. F., Wyllie, A. H. & Currie, A. R. Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 26, 239-257 (1972).
123. Majno, G. & Joris, I. Apoptosis, oncosis, and necrosis. An overview of cell death. Am. J. Pathol. 146, 3-15 (1995).
124. 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).