Inflammasome adaptors and sensors: intracellular regulators of infection and inflammation (original) (raw)

• Raskin, D. M., Seshadri, R., Pukatzki, S. U. & Mekalanos, J. J. Bacterial genomics and pathogen evolution. Cell 124, 703–714 (2006).
  Article CAS PubMed Google Scholar
• Pizarro-Cerda, J. & Cossart, P. Bacterial adhesion and entry into host cells. Cell 124, 715–727 (2006).
  Article CAS PubMed Google Scholar
• Akira, S. & Takeda, K. Toll-like receptor signalling. Nature Rev. Immunol. 4, 499–511 (2004).
  Article CAS Google Scholar
• Strober, W., Murray, P. J., Kitani, A. & Watanabe, T. Signalling pathways and molecular interactions of NOD1 and NOD2. Nature Rev. Immunol. 6, 9–20 (2006).
  Article CAS Google Scholar
• Ting, J. P., Kastner, D. L. & Hoffman, H. M. CATERPILLERs, pyrin and hereditary immunological disorders. Nature Rev. Immunol. 6, 183–195 (2006).
  Article CAS Google Scholar
• Inohara, N., Chamaillard, M., McDonald, C. & Nunez, G. NOD-LRR proteins: role in host-microbial interactions and inflammatory disease. Annu. Rev. Biochem. 74, 355–383 (2005).
  Article CAS PubMed Google Scholar
• Kufer, T. A., Fritz, J. H. & Philpott, D. J. NACHT-LRR proteins (NLRs) in bacterial infection and immunity. Trends Microbiol. 13, 381–388 (2005).
  Article CAS PubMed Google Scholar
• Viala, J. et al. Nod1 responds to peptidoglycan delivered by the Helicobacter pylori cag pathogenicity island. Nature Immunol. 5, 1166–1174 (2004).
  Article CAS 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).
  Article PubMed PubMed Central CAS 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).
  Article CAS 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). References 10 and 11 provide evidence that caspase-1 is activated in response to flagellin that is secreted by the intracellular pathogen S. typhimurium in an IPAF-dependent manner.
  Article CAS Google Scholar
• Philpott, D. J. & Girardin, S. E. The role of Toll-like receptors and Nod proteins in bacterial infection. Mol. Immunol. 41, 1099–1108 (2004).
  Article CAS PubMed Google Scholar
• Meylan, E., Tschopp, J. & Karin, M. Intracellular pattern recognition receptors in the host response. Nature 442, 39–44 (2006).
  Article CAS PubMed Google Scholar
• Martinon, F., Burns, K. & Tschopp, J. The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-1β. Mol. Cell 10, 417–426 (2002). The first description of the caspase-1 inflammasome.
  Article CAS PubMed Google Scholar
• Schmitz, J. et al. IL-33, an interleukin-1-like cytokine that signals via the IL-1 receptor-related protein ST2 and induces T helper type 2-associated cytokines. Immunity 23, 479–490 (2005).
  Article CAS PubMed 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. Cell 126, 1135–1145 (2006). Describes the role of caspase-1 in activating lipid metabolic pathways in fibroblasts.
  Article CAS PubMed Google Scholar
• Tschopp, J., Irmler, M. & Thome, M. Inhibition of Fas death signals by FLIPs. Curr. Opin. Immunol. 10, 552–558 (1998).
  Article CAS PubMed Google Scholar
• Chu, Z. L. et al. A novel enhancer of the Apaf1 apoptosome involved in cytochrome _c_-dependent caspase activation and apoptosis. J. Biol. Chem. 276, 9239–9245 (2001).
  Article CAS PubMed Google Scholar
• Martinon, F. & Tschopp, J. Inflammatory caspases and inflammasomes: master switches of inflammation. Cell Death Differ. 15 September 2006 (doi: 10.1038/sj.cdd.4402038).
• Sutterwala, F. S., Ogura, Y., Zamboni, D. S., Roy, C. R. & Flavell, R. A. NALP3: a key player in caspase-1 activation. J. Endotoxin Res. 12, 251–256 (2006).
  Article CAS PubMed Google Scholar
• Ogura, Y., Sutterwala, F. S. & Flavell, R. A. The inflammasome: first line of the immune response to cell stress. Cell 126, 659–662 (2006).
  Article CAS PubMed Google Scholar
• Drenth, J. P. & van der Meer, J. W. The inflammasome — a linebacker of innate defense. N. Engl. J. Med. 355, 730–732 (2006).
  Article CAS PubMed Google Scholar
• Franchi, L., McDonald, C., Kanneganti, T. D., Amer, A. & Nunez, G. Nucleotide-binding oligomerization domain-like receptors: intracellular pattern recognition molecules for pathogen detection and host defense. J. Immunol. 177, 3507–3513 (2006).
  Article CAS PubMed Google Scholar
• Masumoto, J. et al. ASC, a novel 22-kDa protein, aggregates during apoptosis of human promyelocytic leukemia HL-60 cells. J. Biol. Chem. 274, 33835–33838 (1999).
  Article CAS PubMed Google Scholar
• Conway, K. E. et al. TMS1, a novel proapoptotic caspase recruitment domain protein, is a target of methylation-induced gene silencing in human breast cancers. Cancer Res. 60, 6236–6242 (2000).
  CAS PubMed Google Scholar
• Martinon, F. & Tschopp, J. Inflammatory caspases: linking an intracellular innate immune system to autoinflammatory diseases. Cell 117, 561–574 (2004).
  Article CAS PubMed Google Scholar
• Agostini, L. et al. NALP3 forms an IL-1β-processing inflammasome with increased activity in Muckle–Wells autoinflammatory disorder. Immunity 20, 319–325 (2004).
  Article CAS PubMed Google Scholar
• Dowds, T. A., Masumoto, J., Zhu, L., Inohara, N. & Nunez, G. Cryopyrin-induced interleukin 1β secretion in monocytic cells: enhanced activity of disease-associated mutants and requirement for ASC. J. Biol. Chem. 279, 21924–21928 (2004).
  Article CAS PubMed Google Scholar
• Yu, J. W. et al. Cryopyrin and pyrin activate caspase-1, but not NF-κB, via ASC oligomerization. Cell Death Differ. 13, 236–249 (2006).
  Article CAS PubMed Google Scholar
• Hoffman, H. M., Mueller, J. L., Broide, D. H., Wanderer, A. A. & Kolodner, R. D. Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle–Wells syndrome. Nature Genet. 29, 301–305 (2001). Describes the first evidence for an association between NALP3/cryopyrin variants and Muckle–Wells syndrome.
  Article CAS PubMed Google Scholar
• McDermott, M. F. & Aksentijevich, I. The autoinflammatory syndromes. Curr. Opin. Allergy Clin. Immunol. 2, 511–516 (2002).
  Article PubMed Google Scholar
• Feldmann, J. et al. Chronic infantile neurological cutaneous and articular syndrome is caused by mutations in CIAS1, a gene highly expressed in polymorphonuclear cells and chondrocytes. Am. J. Hum. Genet. 71, 198–203 (2002).
  Article CAS PubMed PubMed Central Google Scholar
• Mariathasan, S. et al. Cryopyrin activates the inflammasome in response to toxins and ATP. Nature 440, 228–232 (2006). Describes NALP3/cyropyrin deficient mice and its requirement for inflammsome activation in response to toxins, ATP, S. aureus , and L. monocytogenes.
  Article CAS PubMed Google Scholar
• Kanneganti, T. D. et al. Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3. Nature 440, 233–236 (2006). Describes NALP3-deficient mice and its requirement for inflammasome activation in response to bacterial RNA and small antiviral compounds.
  Article CAS PubMed Google Scholar
• Martinon, F., Petrilli, V., Mayor, A., Tardivel, A. & Tschopp, J. Gout-associated uric acid crystals activate the NALP3 inflammasome. Nature 440, 237–241 (2006). Describes NALP3 involvement in inflammasome activation in response to danger signals such as uric acid crystals.
  Article CAS PubMed Google Scholar
• Sutterwala, F. S. et al. Critical role for NALP3/CIAS1/cryopyrin in innate and adaptive immunity through its regulation of caspase-1. Immunity 24, 317–327 (2006).
  Article CAS PubMed Google Scholar
• Geddes, B. J. et al. Human CARD12 is a novel CED4/Apaf-1 family member that induces apoptosis. Biochem. Biophys. Res. Commun. 284, 77–82 (2001).
  Article CAS PubMed 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).
  Article CAS PubMed Google Scholar
• Dinarello, C. A. Biologic basis for interleukin-1 in disease. Blood 87, 2095–2147 (1996).
  Article CAS PubMed Google Scholar
• Messud-Petit, F. et al. Serp2, an inhibitor of the interleukin-1β-converting enzyme, is critical in the pathobiology of myxoma virus. J. Virol. 72, 7830–7839 (1998).
  Article CAS PubMed PubMed Central 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. Immunity 23, 587–598 (2005).
  Article CAS PubMed Google Scholar
• Mariathasan, S. et al. Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf. Nature 430, 213–218 (2004). Describes the role of ASC in response to ATP and of ASC and IPAF in response to the intracellular pathogen S. typhimurium.
  Article CAS PubMed Google Scholar
• Thornberry, N. A. & Molineaux, S. M. Interleukin-1β converting enzyme: a novel cysteine protease required for IL-1β production and implicated in programmed cell death. Protein Sci. 4, 3–12 (1995).
  Article CAS PubMed PubMed Central Google Scholar
• Burns, K., Martinon, F. & Tschopp, J. New insights into the mechanism of IL-1β maturation. Curr. Opin. Immunol. 15, 26–30 (2003).
  Article CAS PubMed Google Scholar
• Wang, S. et al. Murine caspase-11, an ICE-interacting protease, is essential for the activation of ICE. Cell 92, 501–509 (1998).
  Article CAS PubMed Google Scholar
• Hogquist, K. A., Nett, M. A., Unanue, E. R. & Chaplin, D. D. Interleukin 1 is processed and released during apoptosis. Proc. Natl Acad. Sci. USA 88, 8485–8489 (1991).
  Article CAS PubMed PubMed Central Google Scholar
• Solle, M. et al. Altered cytokine production in mice lacking P2X7 receptors. J. Biol. Chem. 276, 125–132 (2001).
  Article CAS PubMed Google Scholar
• Di Virgilio, F., Baricordi, O. R., Romagnoli, R. & Baraldi, P. G. Leukocyte P2 receptors: a novel target for anti-inflammatory and anti-tumor therapy. Curr. Drug Targets Cardiovasc. Haematol. Disord. 5, 85–99 (2005).
  Article CAS PubMed Google Scholar
• Perregaux, D. & Gabel, C. A. Interleukin-1β maturation and release in response to ATP and nigericin. Evidence that potassium depletion mediated by these agents is a necessary and common feature of their activity. J. Biol. Chem. 269, 15195–15203 (1994).
  Article CAS PubMed Google Scholar
• Walev, I., Reske, K., Palmer, M., Valeva, A. & Bhakdi, S. Potassium-inhibited processing of IL-1β in human monocytes. EMBO J. 14, 1607–1614 (1995).
  Article CAS PubMed PubMed Central Google Scholar
• Walev, I. et al. Potassium regulates IL-1β processing via calcium-independent phospholipase A2 . J. Immunol. 164, 5120–5124 (2000).
  Article CAS PubMed Google Scholar
• Andrei, C. et al. Phospholipases C and A2 control lysosome-mediated IL-1β secretion: Implications for inflammatory processes. Proc. Natl Acad. Sci. USA 101, 9745–9750 (2004).
  Article CAS PubMed PubMed Central Google Scholar
• Yamamoto, M. et al. ASC is essential for LPS-induced activation of procaspase-1 independently of TLR-associated signal adaptor molecules. Genes Cells 9, 1055–1067 (2004).
  Article CAS PubMed Google Scholar
• Kuida, K. et al. Altered cytokine export and apoptosis in mice deficient in interleukin-1β converting enzyme. Science 267, 2000–2003 (1995).
  Article CAS PubMed 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. Cell 80, 401–411 (1995).
  Article CAS PubMed Google Scholar
• Ozoren, N. et al. Distinct roles of TLR2 and the adaptor ASC in IL-1β/IL-18 secretion in response to Listeria monocytogenes. J. Immunol. 176, 4337–4342 (2006).
  Article PubMed 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).
  Article CAS PubMed PubMed Central Google Scholar
• 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).
  Article CAS PubMed PubMed 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).
  Article CAS PubMed Google Scholar
• 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).
  Article CAS PubMed Google Scholar
• Lara-Tejero, M. et al. Role of the caspase-1 inflammasome in Salmonella typhimurium pathogenesis. J. Exp. Med. 203, 1407–1412 (2006).
  Article CAS PubMed PubMed 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 (2006).
• Galan, J. E. Salmonella interactions with host cells: type III secretion at work. Annu. Rev. Cell Dev. Biol. 17, 53–86 (2001).
  Article CAS PubMed Google Scholar
• Goosney, D. L., Knoechel, D. G. & Finlay, B. B. Enteropathogenic E. coli, Salmonella, and Shigella: masters of host cell cytoskeletal exploitation. Emerg. Infect. Dis. 5, 216–223 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• Cossart, P. & Sansonetti, P. J. Bacterial invasion: the paradigms of enteroinvasive pathogens. Science 304, 242–248 (2004).
  Article CAS PubMed Google Scholar
• Lee, S. H. & Galan, J. E. Salmonella type III secretion-associated chaperones confer secretion-pathway specificity. Mol. Microbiol. 51, 483–495 (2004).
  Article CAS PubMed 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). Describes the requirement of NAIP5/Birc1e and IPAF for recognition of the intracellular pathogen L. pneumophila and activation of the inflammasome.
  Article CAS Google Scholar
• Yamamoto, Y., Klein, T. W., Newton, C. A., Widen, R. & Friedman, H. Growth of Legionella pneumophila in thioglycolate-elicited peritoneal macrophages from A/J mice. Infect. Immun. 56, 370–375 (1988).
  Article CAS PubMed PubMed Central Google Scholar
• Diez, E. et al. Birc1e is the gene within the Lgn1 locus associated with resistance to Legionella pneumophila. Nature Genet. 33, 55–60 (2003).
  Article CAS PubMed Google Scholar
• Wright, E. K. et al. Naip5 affects host susceptibility to the intracellular pathogen Legionella pneumophila. Curr. Biol. 13, 27–36 (2003).
  Article CAS PubMed Google Scholar
• Miller, L. K. An exegesis of IAPs: salvation and surprises from BIR motifs. Trends Cell Biol. 9, 323–328 (1999).
  Article CAS PubMed Google Scholar
• Damiano, J. S., Oliveira, V., Welsh, K. & Reed, J. C. Heterotypic interactions among NACHT domains: implications for regulation of innate immune responses. Biochem. J. 381, 213–219 (2004).
  Article CAS PubMed PubMed Central 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). References 9 and 73 provide evidence that caspase-1 is activated in response to flagellin that is secreted by the intracellular pathogen L. pneumophila.
  Article CAS PubMed PubMed Central Google Scholar
• Roy, D. et al. A process for controlling intracellular bacterial infections induced by membrane injury. Science 304, 1515–1518 (2004).
  Article CAS PubMed 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). Describes the role of ASC in activating the inflammasome in response to the intracellular pathogen F. tularensis.
  Article CAS PubMed PubMed Central Google Scholar
• Gavrilin, M. A. et al. Internalization and phagosome escape required for Francisella to induce human monocyte IL-1β processing and release. Proc. Natl Acad. Sci. USA 103, 141–146 (2006).
  Article CAS PubMed Google Scholar
• Grenier, J. M. et al. Functional screening of five PYPAF family members identifies PYPAF5 as a novel regulator of NF-κB and caspase-1. FEBS Lett. 530, 73–78 (2002).
  Article CAS PubMed Google Scholar
• Wang, L. et al. PYPAF7, a novel PYRIN-containing Apaf1-like protein that regulates activation of NF-κB and caspase-1-dependent cytokine processing. J. Biol. Chem. 277, 29874–29880 (2002).
  Article CAS PubMed Google Scholar
• Boyden, E. D. & Dietrich, W. F. Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin. Nature Genet. 38, 240–244 (2006).
  Article CAS PubMed Google Scholar
• Annand, R. R. et al. Caspase-1 (interleukin-1β-converting enzyme) is inhibited by the human serpin analogue proteinase inhibitor 9. Biochem. J. 342, 655–665 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• Saleh, M. et al. Enhanced bacterial clearance and sepsis resistance in caspase-12-deficient mice. Nature 440, 1064–1068 (2006).
  Article CAS PubMed Google Scholar
• Humke, E. W., Shriver, S. K., Starovasnik, M. A., Fairbrother, W. J. & Dixit, V. M. ICEBERG: a novel inhibitor of interleukin-1β generation. Cell 103, 99–111 (2000).
  Article CAS PubMed Google Scholar
• Druilhe, A., Srinivasula, S. M., Razmara, M., Ahmad, M. & Alnemri, E. S. Regulation of IL-1β generation by pseudo-ICE and ICEBERG, two dominant negative caspase recruitment domain proteins. Cell Death Differ. 8, 649–657 (2001).
  Article CAS PubMed Google Scholar
• Lee, S. H., Stehlik, C. & Reed, J. C. COP, a caspase recruitment domain-containing protein and inhibitor of caspase-1 activation processing. J. Biol. Chem. 276, 34495–34500 (2001).
  Article CAS PubMed Google Scholar
• Razmara, M. et al. CARD-8 protein, a new CARD family member that regulates caspase-1 activation and apoptosis. J. Biol. Chem. 277, 13952–13958 (2002).
  Article CAS PubMed Google Scholar
• Lamkanfi, M. et al. INCA, a novel human caspase recruitment domain protein that inhibits interleukin-1β generation. J. Biol. Chem. 279, 51729–51738 (2004).
  Article CAS PubMed Google Scholar
• Aksentijevich, I. et al. Mutation and haplotype studies of familial Mediterranean fever reveal new ancestral relationships and evidence for a high carrier frequency with reduced penetrance in the Ashkenazi Jewish population. Am. J. Hum. Genet. 64, 949–962 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• Chae, J. J. et al. Targeted disruption of pyrin, the FMF protein, causes heightened sensitivity to endotoxin and a defect in macrophage apoptosis. Mol. Cell 11, 591–604 (2003).
  Article CAS PubMed Google Scholar
• Chae, J. J. et al. The B30.2 domain of pyrin, the familial Mediterranean fever protein, interacts directly with caspase-1 to modulate IL-1β production. Proc. Natl Acad. Sci. USA 103, 9982–9987 (2006).
  Article CAS PubMed PubMed Central Google Scholar
• Salvesen, G. S. & Dixit, V. M. Caspase activation: the induced-proximity model. Proc. Natl Acad. Sci. USA 96, 10964–10967 (1999).
  Article CAS PubMed PubMed Central Google Scholar