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Canadian Journal of Infectious Diseases and Medical Microbiology
Volume 2017, Article ID 2309478, 9 pages
https://doi.org/10.1155/2017/2309478
Review Article

Inflammasomes in Mycobacterium tuberculosis-Driven Immunity

Division of Cell Immunology, Department of Immunology and Infectious Biology, Institute of Microbiology, Biotechnology and Immunology, Faculty of Biology and Environmental Protection, University of Lodz, Banacha 12/16, 90-237 Lodz, Poland

Correspondence should be addressed to Sebastian Wawrocki; lp.zdol.inu.loib@ikcorwaw.naitsabes

Received 3 July 2017; Revised 30 September 2017; Accepted 18 October 2017; Published 4 December 2017

Academic Editor: Maria L. Tornesello

Copyright © 2017 Sebastian Wawrocki and Magdalena Druszczynska. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. A. Welin, D. Eklund, O. Stendahl, and M. Lerm, “Human macrophages infected with a high burden of ESAT-6-expressing M. tuberculosis undergo caspase-1- and cathepsin B-independent necrosis,” PLoS One, vol. 6, no. 5, p. e20302, 2011. View at Publisher · View at Google Scholar · View at Scopus
  2. T. R. Lerner, S. Borel, and M. G. Gutierrez, “The innate immune response in human tuberculosis,” Cellular Microbiology, vol. 17, no. 9, pp. 1277–1285, 2015. View at Publisher · View at Google Scholar · View at Scopus
  3. V. C. Korb, A. A. Chuturgoon, and D. Moodley, “Mycobacterium tuberculosis: manipulator of protective immunity,” International Journal of Molecular Sciences, vol. 17, no. 3, p. 131, 2016. View at Publisher · View at Google Scholar · View at Scopus
  4. H. Saiga, N. Nieuwenhuizen, M. Gengenbacher et al., “The recombinant BCG ΔureC::hly vaccine targets the AIM2 inflammasome to induce autophagy and inflammation,” Journal of Infectious Diseases, vol. 211, no. 11, pp. 1831–1841, 2015. View at Publisher · View at Google Scholar · View at Scopus
  5. H. E. Barksby, S. R. Lea, P. M. Preshaw, and J. J. Taylor, “The expanding family of interleukin-1 cytokines and their role in destructive inflammatory disorders,” Clinical & Experimental Immunology, vol. 149, no. 2, pp. 217–225, 2007. View at Publisher · View at Google Scholar · View at Scopus
  6. D. Novick, S. Kim, G. Kaplanski, and C. A. Dinarello, “Interleukin-18, more than a Th1 cytokine,” Seminars in Immunology, vol. 25, no. 6, pp. 439–448, 2013. View at Publisher · View at Google Scholar · View at Scopus
  7. C. A. Dinarello and F. Giamila, “Interleukin-18 and host defense against infection,” Journal of Infectious Diseases, vol. 187, no. 2, pp. 370–384, 2003. View at Publisher · View at Google Scholar · View at Scopus
  8. C. A. Dinarello, D. Novick, S. Kim, and G. Kaplanski, “Interleukin-18 and IL-18 binding protein,” Frontiers in Immunology, vol. 4, pp. 1–10, 2013. View at Publisher · View at Google Scholar · View at Scopus
  9. C. A. Dinarello, “Interleukin-1, interleukin-1 receptors and interleukin-1 receptor antagonist,” International Reviews of Immunology, vol. 16, no. 5-6, pp. 457–499, 1998. View at Publisher · View at Google Scholar
  10. R. Gutzmer, K. Langer, S. Mommert, M. Wittmann, A. Kapp, and T. Werfel, “Human dendritic cells express the IL-18R and are chemoattracted to IL-18,” Journal of Immunology, vol. 171, no. 12, pp. 6363–6371, 2003. View at Publisher · View at Google Scholar
  11. S. Gardella, C. Andrei, S. Costigliolo, A. Poggi, M. R. Zocchi, and A. Rubartelli, “Interleukin-18 synthesis and secretion by dendritic cells are modulated by interaction with antigen-specific T cells,” Journal of Leukocyte Biology, vol. 66, no. 2, pp. 237–241, 1999. View at Google Scholar
  12. D. V. Pechkovsky, T. Goldmann, E. Vollmer, J. Müller-Quernheim, and G. Zissel, “Interleukin-18 expression by alveolar epithelial cells type II in tuberculosis and sarcoidosis,” FEMS Immunology & Medical Microbiology, vol. 46, no. 1, pp. 30–38, 2006. View at Publisher · View at Google Scholar · View at Scopus
  13. S. El-Masry, M. Lotfy, W. Nasif, I. El-Kady, and M. Al-Badrawy, “Elevated serum level of interleukin (IL)-18, interferon (IFN)-γ and soluble fas in patients with pulmonary complications in tuberculosis,” Acta Microbiologica et Immunologica Hungarica, vol. 54, no. 1, pp. 65–67, 2007. View at Publisher · View at Google Scholar · View at Scopus
  14. K. Nakanishi, T. Yoshimoto, H. Tsutsui, and H. Okamura, “Interleukin-18 regulates both Th1 and Th2 responses,” Annual Review of Immunology, vol. 19, no. 1, pp. 423–474, 2001. View at Publisher · View at Google Scholar · View at Scopus
  15. N. A. Turner, “Effects of interleukin-1 on cardiac fibroblast function: relevance to post-myocardial infarction remodeling,” Vascular Pharmacology, vol. 60, no. 1, pp. 1–7, 2014. View at Publisher · View at Google Scholar · View at Scopus
  16. C. Duque, L. Arroyo, H. Ortega et al., “Different responses of human mononuclear phagocyte populations to Mycobacterium tuberculosis,” Tuberculosis, vol. 94, no. 2, pp. 111–122, 2014. View at Publisher · View at Google Scholar · View at Scopus
  17. G. Lopez-Castejon and D. Brough, “Understanding the mechanism of IL-1β secretion,” Cytokine & Growth Factor Reviews, vol. 22, no. 4, pp. 189–195, 2011. View at Publisher · View at Google Scholar · View at Scopus
  18. L. D. Church, G. P. Cook, and M. F. McDermott, “Primer: inflammasomes and interleukin 1β in inflammatory disorders,” Nature Clinical Practice Rheumatology, vol. 4, no. 1, pp. 34–42, 2008. View at Publisher · View at Google Scholar · View at Scopus
  19. M. Ricote, I. García-Tuñón, F. R. Bethencourt, B. Fraile, R. Paniagua, and M. Royuela, “Interleukin-1 (IL-1alpha and IL-1beta) and its receptors (IL-1RI, IL-1RII, and IL-1Ra) in prostate carcinoma,” Cancer, vol. 100, no. 7, pp. 1388–1396, 2004. View at Publisher · View at Google Scholar · View at Scopus
  20. F. L. van de Veerdonk, M. G. Netea, C. A. Dinarello, and L. A. B. Joosten, “Inflammasome activation and IL-1β and IL-18 processing during infection,” Trends in Immunology, vol. 32, no. 3, pp. 110–116, 2011. View at Publisher · View at Google Scholar · View at Scopus
  21. M. G. Netea, A. Simon, F. van de Veerdonk, B.-J. Kullberg, J. W. M. Van der Meer, and L. A. B. Joosten, “IL-1β processing in host defense: beyond the inflammasomes,” PLoS One, vol. 6, no. 2, p. e10000661, 2010. View at Publisher · View at Google Scholar · View at Scopus
  22. A. Halle, V. Hornung, G. C. Petzold et al., “The NALP3 inflammasome is involved in the innate immune response to amyloid-beta,” Nature Immunology, vol. 9, no. 8, pp. 857–865, 2008. View at Publisher · View at Google Scholar · View at Scopus
  23. H. Yamada, S. Mizumo, R. Horai, Y. Iwakura, and I. Sugawara, “Protective role of interleukin-1 in mycobacterial infection in IL-1 alpha/beta double-knockout mice,” Laboratory Investigation, vol. 80, no. 5, pp. 759–767, 2000. View at Publisher · View at Google Scholar
  24. H. Guo, J. B. Callaway, and J. P. Ting, “Inflammasomes: mechanism of action, role in disease, and therapeutics,” Nature Medicine, vol. 21, no. 7, pp. 677–687, 2015. View at Publisher · View at Google Scholar · View at Scopus
  25. G. dos Santos, M. A. Kutuzov, and K. M. Ridge, “The inflammasome in lung diseases,” American Journal of Physiology-Lung Cellular and Molecular Physiology, vol. 303, no. 8, pp. 627–633, 2012. View at Publisher · View at Google Scholar · View at Scopus
  26. X. Liu and J. Lieberman, “A mechanistic understanding of pyroptosis: the fiery death triggered by invasive infection,” Advances in Immunology, vol. 135, pp. 81–117, 2017. View at Publisher · View at Google Scholar
  27. D. R. McIlwain, T. Berger, and T. W. Mak, “Caspase functions in cell death and disease,” Cold Spring Harbor Perspectives in Biology, vol. 5, no. 4, p. a008656, 2013. View at Publisher · View at Google Scholar · View at Scopus
  28. F. Martinon, K. Burns, and J. Tschopp, “The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta,” Molecular Cell, vol. 10, no. 2, pp. 417–426, 2002. View at Publisher · View at Google Scholar · View at Scopus
  29. A. J. S. Choi and S. W. Ryter, “Inflammasomes: molecular regulation and implications for metabolic and cognitive diseases,” Molecules and Cells, vol. 37, no. 6, pp. 441–448, 2014. View at Publisher · View at Google Scholar · View at Scopus
  30. B. K. Davis, H. Wen, and J. P. Ting, “The inflammasome NLRs in immunity, inflammation, and associated diseases,” Annual Review of Immunology, vol. 29, no. 1, pp. 707–735, 2011. View at Publisher · View at Google Scholar · View at Scopus
  31. J. P. Ting, R. C. Lovering, E. S. Alnemri et al., “The NLR gene family: a standard nomenclature,” Immunity, vol. 28, no. 3, pp. 285–287, 2008. View at Publisher · View at Google Scholar · View at Scopus
  32. Y. K. Kim, J. S. Shin, and M. H. Nahm, “NOD-like receptors in infection, immunity, and diseases,” Yonsei Medical Journal, vol. 57, no. 1, pp. 5–14, 2016. View at Publisher · View at Google Scholar · View at Scopus
  33. J. Bertin, W. J. Nir, C. M. Fischer et al., “Human CARD4 protein is a novel CED-4/Apaf-1 cell death family member that activates NF-kB,” Journal of Biological Chemistry, vol. 274, no. 19, pp. 12955–12958, 1999. View at Publisher · View at Google Scholar · View at Scopus
  34. N. Roy, M. S. Mahadevan, M. McLean et al., “The gene for neuronal apoptosis inhibitory protein is partially deleted in individuals with spinal muscular atrophy,” Cell, vol. 80, no. 1, pp. 167–178, 1995. View at Publisher · View at Google Scholar · View at Scopus
  35. K. Schroder and J. Tschopp, “The inflammasomes,” Cell, vol. 140, no. 6, pp. 821–832, 2010. View at Publisher · View at Google Scholar · View at Scopus
  36. B. Faustin, L. Lartigue, J. M. Bruey et al., “Reconstituted NALP1 inflammasome reveals two-step mechanism of caspase-1 activation,” Molecular Cell, vol. 25, no. 5, pp. 713–724, 2007. View at Publisher · View at Google Scholar · View at Scopus
  37. J. Chavarría-Smith and R. E. F. Vance, “The NLRP1 inflammasomes,” Immunology Reviews, vol. 265, no. 1, pp. 33-34, 2015. View at Publisher · View at Google Scholar · View at Scopus
  38. J. L. Poyet, S. M. Srinivasula, M. Tnani, M. Razmara, T. Fernandes-Alnemri, and E. S. Alnemri, “Identification of Ipaf, a human caspase-1-activating protein related to Apaf-1,” Journal of Biological Chemistry, vol. 276, no. 30, pp. 28309–28313, 2001. View at Publisher · View at Google Scholar · View at Scopus
  39. J. A. Cridland, E. Z. Curley, M. N. Wykes et al., “The mammalian PYHIN gene family: phylogeny, evolution and expression,” BMC Evolutionary Biology, vol. 12, no. 1, pp. 140–156, 2012. View at Publisher · View at Google Scholar · View at Scopus
  40. J.-W. Yu, J. Wu, Z. Zhang et al., “Cryopyrin and pyrin activate caspase-1, but not NF-κβ, via ASC oligomerization,” Cell Death and Differentiation, vol. 13, no. 2, pp. 236–249, 2006. View at Publisher · View at Google Scholar · View at Scopus
  41. C. de Torre-Minguela, P. M. de Castillo, and P. Pelegrin, “The NLRP3 and pyrin inflammasomes: implications in the pathophysiology of autoinflammatory diseases,” Frontiers in Immunology, vol. 8, p. 43, 2017. View at Publisher · View at Google Scholar
  42. K. D. Mayer-Barber, D. L. Barber, K. Shenderov et al., “Cutting edge: caspase-1 independent IL-1β production is critical for host resistance to Mycobacterium tuberculosis and does not require TLR signaling in vivo,” Journal of Immunology, vol. 184, no. 7, pp. 3326–3330, 2010. View at Publisher · View at Google Scholar · View at Scopus
  43. I. Sugawara, H. Yamada, H. Kaneko, S. Mizuno, K. Takeda, and S. Akira, “Role of interleukin-18 (IL-18) in mycobacterial infection in IL-18-gene-disrupted mice,” Infection and Immunity, vol. 67, no. 5, pp. 2585–2589, 1999. View at Google Scholar
  44. I. Sugawara, H. Yamada, S. Hua, and S. Mizuno, “Role of interleukin (IL)-1 type 1 receptor in mycobacterial infection,” Microbiology and Immunology, vol. 45, no. 11, pp. 743–750, 2001. View at Publisher · View at Google Scholar
  45. C. M. Fremond, D. Togbe, E. Doz et al., “IL-1 receptor-mediated signal is an essential component of MyD88-dependent innate response to Mycobacterium tuberculosis infection,” Journal of Immunology, vol. 179, no. 2, pp. 1178–1189, 2007. View at Publisher · View at Google Scholar
  46. B. E. Schneider, D. Korbel, K. Hagens et al., “A role for IL-18 in protective immunity against Mycobacterium tuberculosis,” European Journal of Immunology, vol. 40, no. 2, pp. 396–405, 2010. View at Publisher · View at Google Scholar · View at Scopus
  47. V. Briken, S. E. Ahlbrand, and S. Shah, “Mycobacterium tuberculosis and the host cell inflammasome: a complex relationship,” Frontiers in Cellular and Infection Microbiology, vol. 9, no. 3, p. 62, 2013. View at Publisher · View at Google Scholar · View at Scopus
  48. R. Wassermann, M. F. Gulen, C. Sala et al., “Mycobacterium tuberculosis differentially activates cGAS- and inflammasome-dependent intracellular immune responses through ESX-1,” Cell Host Microbe, vol. 17, no. 6, pp. 799–810, 2015. View at Publisher · View at Google Scholar · View at Scopus
  49. O. Gross, H. Poeck, M. Bscheider et al., “Syk kinase signalling couples to the Nlrp3 inflammasome for anti-fungal host defence,” Nature, vol. 459, no. 7245, pp. 433–436, 2009. View at Publisher · View at Google Scholar · View at Scopus
  50. J. A. Duncan, X. Gao, M. T. Huang et al., “Neisseria gonorrhoeae activates the proteinase cathepsin B to mediate the signaling activities of the NLRP3 and ASC-containing inflammasome,” Journal of Immunology, vol. 182, no. 10, pp. 6460–6469, 2009. View at Publisher · View at Google Scholar · View at Scopus
  51. S. Mariathasan, D. S. Weiss, K. Newton et al., “Cryopyrin activates the inflammasome in response to toxins and ATP,” Nature, vol. 440, no. 7081, pp. 228–232, 2006. View at Publisher · View at Google Scholar · View at Scopus
  52. K. Yamasaki, J. Muto, K. R. Taylor et al., “NLRP3/cryopyrin is necessary for interleukin-1beta (IL-1beta) release in response to hyaluronan, an endogenous trigger of inflammation in response to injury,” Journal of Biological Chemistry, vol. 284, no. 19, pp. 12762–12771, 2009. View at Publisher · View at Google Scholar · View at Scopus
  53. H. Watanabe, O. Gaide, V. Pétrilli et al., “Activation of the IL-1beta-processing inflammasome is involved in contact hypersensitivity,” Journal of Investigative Dermatology, vol. 127, no. 8, pp. 1956–1963, 2007. View at Publisher · View at Google Scholar · View at Scopus
  54. D. Eklund, A. Welin, H. Andersson et al., “Human gene variants linked to enhanced NLRP3 activity limit intramacrophage growth of Mycobacterium tuberculosis,” Journal of Infectious Diseases, vol. 209, no. 5, pp. 749–753, 2014. View at Publisher · View at Google Scholar · View at Scopus
  55. P. J. Shaw, M. F. McDermott, and T. D. Kanneganti, “Inflammasomes and autoimmunity,” Trends in Molecular Medicine, vol. 17, no. 2, pp. 57–64, 2011. View at Publisher · View at Google Scholar · View at Scopus
  56. V. Pétrilli, S. Papin, C. Dostert, A. Mayor, F. Martinon, and J. Tschopp, “Activation of the NALP3 inflammasome is triggered by low intracellular potassium concentration,” Cell Death and Differentiation, vol. 14, no. 9, pp. 1583–1589, 2007. View at Publisher · View at Google Scholar · View at Scopus
  57. R. Muñoz-Planillo, L. Franchi, L. S. Miller, and G. Núñez, “A critical role for hemolysins and bacterial lipoproteins in Staphylococcus aureus-induced activation of the Nlrp3 inflammasome,” Journal of Immunology, vol. 183, no. 6, pp. 3942–3948, 2009. View at Publisher · View at Google Scholar · View at Scopus
  58. Y. He, M. Y. Zeng, D. Yang, B. Motro, and G. Núñez, “NEK7 is an essential mediator of NLRP3 activation downstream of potassium efflux,” Nature, vol. 530, no. 7590, pp. 354–369, 2016. View at Publisher · View at Google Scholar · View at Scopus
  59. V. Hornung, F. Bauernfeind, and A. Halle, “Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization,” Nature Immunology, vol. 9, no. 8, pp. 847–856, 2008. View at Publisher · View at Google Scholar · View at Scopus
  60. M. E. Heid, P. A. Keyel, C. Kamga et al., “Mitochondrial reactive oxygen species induces NLRP3-dependent lysosomal damage and inflammasome activation,” Journal of Immunology, vol. 191, no. 10, pp. 5230–5238, 2013. View at Publisher · View at Google Scholar · View at Scopus
  61. M. T. Sorbara and S. E. Girardin, “Mitochondrial ROS fuel the inflammasome,” Cell Research, vol. 21, no. 4, pp. 558–560, 2011. View at Publisher · View at Google Scholar · View at Scopus
  62. R. Zhou, A. S. Yazdi, P. Menu, and J. Tschopp, “A role for mitochondria in NLRP3 inflammasome activation,” Nature, vol. 469, no. 7329, pp. 221–225, 2011. View at Publisher · View at Google Scholar · View at Scopus
  63. K. Nakahira, J. A. Haspel, V. A. Rathinam et al., “Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome,” Nature Immunology, vol. 12, no. 3, pp. 222–230, 2011. View at Publisher · View at Google Scholar · View at Scopus
  64. H. M. Lee, J. J. Kim, H. J. Kim et al., “Upregulated NLRP3 inflammasome activation in patients with type 2 diabetes,” Diabetes, vol. 62, no. 1, pp. 194–204, 2013. View at Publisher · View at Google Scholar · View at Scopus
  65. C. Juliana, T. Fernandes-Alnemri, S. Kang, A. Farias, F. Qin, and E. S. Alnemri, “Non-transcriptional priming and deubiquitination regulate NLRP3 inflammasome activation,” Journal of Biological Chemistry, vol. 287, no. 43, pp. 36617–36622, 2012. View at Publisher · View at Google Scholar · View at Scopus
  66. V. Hornung, A. Ablasser, M. Charrel-Dennis et al., “AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC,” Nature, vol. 458, no. 7237, pp. 514–518, 2009. View at Publisher · View at Google Scholar · View at Scopus
  67. T. Fernandes-Alnemri, J. W. Yu, P. Datta, J. Wu, and E. S. Alnemri, “AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA,” Nature, vol. 458, no. 7237, pp. 509–513, 2009. View at Publisher · View at Google Scholar · View at Scopus
  68. H. Saiga, S. Kitada, Y. Shimada et al., “Critical role of AIM2 in Mycobacterium tuberculosis infection,” International Immunology, vol. 24, no. 10, pp. 637–644, 2012. View at Publisher · View at Google Scholar · View at Scopus
  69. V. A. K. Rathinam, Z. Jiang, S. N. Waggoner et al., “The AIM2 inflammasome is essential for host-defense against cytosolic bacteria and DNA viruses,” Nature Immunology, vol. 11, no. 5, pp. 395–402, 2010. View at Publisher · View at Google Scholar · View at Scopus
  70. J.-D. Sauer, C. E. Witte, J. Zemansky, B. Hanson, P. Lauer, and D. A. Portnoy, “Listeria monocytogenes triggers AIM2-mediated pyroptosis upon infrequent bacteriolysis in the macrophage cytosol,” Cell Host & Microbe, vol. 7, no. 5, pp. 412–419, 2010. View at Publisher · View at Google Scholar · View at Scopus
  71. T. L. Roberts, A. Idris, J. A. Dunn et al., “HIN-200 proteins regulate caspase activation in response to foreign cytoplasmic DNA,” Science, vol. 323, no. 5917, pp. 1057–1060, 2009. View at Publisher · View at Google Scholar · View at Scopus
  72. T. Jin, A. Perry, J. Jiang et al., “Structures of the HIN domain: DNA complexes reveal ligand binding and activation mechanisms of the AIM2 inflammasome and IFI16 receptor,” Immunity, vol. 36, no. 4, pp. 561–571, 2012. View at Publisher · View at Google Scholar · View at Scopus
  73. T. Jin, A Perry, P. Smith, J. Jiang, and T. S. Xiao, “Structure of the absent in melanoma 2 (AIM2) pyrin domain provides insights into the mechanisms of AIM2 autoinhibition and inflammasome assembly,” Journal of Biological Chemistry, vol. 288, no. 19, pp. 13225–13235, 2013. View at Publisher · View at Google Scholar · View at Scopus
  74. S. M. Man, R. Kark, and T. D. Kanneganti, “AIM2 inflammasome in infection, cancer, and autoimmunity: role in DNA sensing, inflammation, and innate immunity,” European Journal of Immunology, vol. 46, no. 2, pp. 269–280, 2016. View at Publisher · View at Google Scholar · View at Scopus
  75. R. P. Lai, G. Meintjes, K. A. Wilkinson et al., “HIV-tuberculosis-associated immune reconstitution inflammatory syndrome is characterized by Toll-like receptor and inflammasome signaling,” Nature Communications, vol. 6, p. 8451, 2015. View at Publisher · View at Google Scholar · View at Scopus
  76. W. C. Chao, C. L. Yen, and Y. H. Wu, “Increased resistin may suppress reactive oxygen species production and inflammasome activation in type 2 diabetic patients with pulmonary tuberculosis infection,” Microbes and Infection, vol. 17, no. 3, pp. 195–204, 2015. View at Publisher · View at Google Scholar · View at Scopus
  77. M. Galle, P. Schotte, M. Haegman et al., “The Pseudomonas aeruginosa type III secretion system plays a dual role in the regulation of caspase-1 mediated IL-1beta maturation,” Journal of Cellular and Molecular Medicine, vol. 12, no. 5, pp. 1767–1776, 2008. View at Publisher · View at Google Scholar · View at Scopus
  78. I. E. Brodsky, N. W. Palm, S. Sadanand et al., “A Yersinia effector protein promotes virulence by preventing inflammasome recognition of the type III secretion system,” Cell Host & Microbe, vol. 7, no. 5, pp. 376–387, 2010. View at Publisher · View at Google Scholar · View at Scopus
  79. S. S. Master, S. K. Rampini, A. S. Davis et al., “Mycobacterium tuberculosis prevents inflammasome activation,” Cell Host & Microbe, vol. 3, no. 4, pp. 224–232, 2008. View at Publisher · View at Google Scholar · View at Scopus
  80. J. Wang, P. Ge, L. Qiang et al., “The mycobacterial phosphatase PtpA regulates the expression of host genes and promotes cell proliferation,” Nature Communications, vol. 8, no. 1, p. 244, 2017. View at Publisher · View at Google Scholar
  81. T. D. Kanneganti, M. Lamkanfi, and Y. G. Kim, “Pannexin-1-mediated recognition of bacterial molecules activates the cryopyrin inflammasome independent of Toll-like receptor signalling,” Immunity, vol. 26, no. 4, pp. 433–443, 2007. View at Publisher · View at Google Scholar · View at Scopus
  82. J. W. Jones, N. Kayagaki, P. Broz et al., “Absent in melanoma 2 is required for innate immune recognition of Francisella tularensis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 21, pp. 9771–9776, 2010. View at Publisher · View at Google Scholar · View at Scopus
  83. K. Tsuchiya, H. Hara, I. Kawamura et al., “Involvement of absent in melanoma 2 in inflammasome activation in macrophages infected with Listeria monocytogenes,” Journal of Immunology, vol. 185, no. 2, pp. 1186–1195, 2010. View at Publisher · View at Google Scholar · View at Scopus
  84. S. Shah, A. Bohsali, S. E. Ahlbrand et al., “Cutting edge: Mycobacterium tuberculosis but not nonvirulent mycobacteria inhibits IFN-β and AIM2 inflammasome-dependent IL-1β production via its ESX-1 secretion system,” Journal of Immunology, vol. 191, no. 7, pp. 3514–3518, 2013. View at Publisher · View at Google Scholar · View at Scopus
  85. K. D. Mayer-Barber, B. B. Andrade, D. L. Barber et al., “Innate and adaptive interferons suppress IL-1α and IL-1β production by distinct pulmonary myeloid subsets during Mycobacterium tuberculosis infection,” Immunity, vol. 35, no. 6, pp. 1023–1034, 2011. View at Publisher · View at Google Scholar · View at Scopus
  86. A. Novikov, M. Cardone, R. Thompson et al., “Mycobacterium tuberculosis triggers host type I IFN signaling to regulate IL-1β production in human macrophages,” Journal of Immunology, vol. 187, no. 5, pp. 2540–2537, 2011. View at Publisher · View at Google Scholar · View at Scopus
  87. H. B. Huante, S. Gupta, V. C. Calderon et al., “Differential inflammasome activation signatures following intracellular infection of human macrophages with Mycobacterium bovis BCG or Trypanosoma cruzi,” Tuberculosis, vol. 110, pp. S35–S44, 2016. View at Publisher · View at Google Scholar · View at Scopus
  88. A. Dorhoi, G. Nouailles, S. Jörg et al., “Activation of the NLRP3 inflammasome by Mycobacterium tuberculosis is uncoupled from susceptibility to active tuberculosis,” European Journal of Immunology, vol. 42, no. 2, pp. 374–384, 2012. View at Publisher · View at Google Scholar · View at Scopus
  89. T. Bergsbaken, S. L. Fink, and B. T. Cookson, “Pyroptosis: host cell death and inflammation,” Nature Reviews Microbiology, vol. 7, no. 2, pp. 99–109, 2009. View at Publisher · View at Google Scholar · View at Scopus
  90. L. Sborgi, S. Rühl, E. Mulvihill et al., “GSDMD membrane pore formation constitutes the mechanism of pyroptotic cell death,” EMBO Journal, vol. 35, no. 16, pp. 1766–1778, 2016. View at Publisher · View at Google Scholar · View at Scopus
  91. M. M. Gaidt and V. Hornung, “Pore formation by GSDMD is the effector mechanism of pyroptosis,” EMBO Journal, vol. 35, no. 20, pp. 2167–2169, 2016. View at Publisher · View at Google Scholar · View at Scopus
  92. T. L. M. Thurston, S. A. Matthews, E. Jennings et al., “Growth inhibition of cytosolic Salmonella by caspase-1 and caspase-11 precedes host death,” Nature Communications, vol. 7, p. 13292, 2016. View at Publisher · View at Google Scholar · View at Scopus
  93. J. Lukens, V. D. Dixit, and T.-D. Kanneganti, “Inflammasome activation in obesity-related inflammatory diseases and autoimmunity,” Discovery Medicine, vol. 12, no. 62, pp. 65–74, 2014. View at Google Scholar
  94. P. Gurung and T.-D. Kanneganti, “Autoinflammatory skin disorders: the inflammasome in focus,” Trends in Molecular Medicine, vol. 22, no. 7, pp. 545–564, 2016. View at Publisher · View at Google Scholar · View at Scopus
  95. D. De Nardo, C. M. De Nardo, and E. Latz, “New insights into mechanisms controlling the NLRP3 inflammasome and its role in lung disease,” American Journal of Pathology, vol. 184, no. 1, pp. 42–54, 2014. View at Publisher · View at Google Scholar · View at Scopus
  96. G. Szabo and T. Csak, “Inflammasomes in liver diseases,” Journal of Hepatology, vol. 57, no. 3, pp. 642–654, 2012. View at Publisher · View at Google Scholar · View at Scopus
  97. H. J. Anders and D. A. Muruve, “The inflammasomes in kidney disease,” Journal of the American Society of Nephrology, vol. 22, no. 6, pp. 1007–1018, 2011. View at Publisher · View at Google Scholar · View at Scopus
  98. A. P. Demidowich, A. I. Davis, N. Dedhia, and J. A. Yanovski, “Colchicine to decrease NLRP3-activated inflammation and improve obesity-related metabolic dysregulation,” Medical Hypotheses, vol. 92, pp. 67–73, 2016. View at Publisher · View at Google Scholar · View at Scopus
  99. G. Nuki, “Colchicine: its mechanism of action and efficacy in crystal-induced inflammation,” Current Rheumatology Reports, vol. 10, no. 3, pp. 218–227, 2008. View at Publisher · View at Google Scholar · View at Scopus
  100. A. A. Jesus and R. Goldbach-Mansky, “IL-1 blockade in autoinflammatory syndromes,” Annual Review of Medicine, vol. 65, no. 1, pp. 223–244, 2014. View at Publisher · View at Google Scholar · View at Scopus