Table of Contents Author Guidelines Submit a Manuscript
Journal of Immunology Research
Volume 2017, Article ID 9361802, 17 pages
https://doi.org/10.1155/2017/9361802
Review Article

Getting “Inside” Type I IFNs: Type I IFNs in Intracellular Bacterial Infections

Department of Microbiology and Immunology, Montana State University, Bozeman, MT, USA

Correspondence should be addressed to Jodi F. Hedges; moc.liamg@segdeh.idoj

Received 21 January 2017; Revised 20 March 2017; Accepted 27 March 2017; Published 26 April 2017

Academic Editor: Chen Zhao

Copyright © 2017 Deann T. Snyder et al. 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. V. van Pesch, H. Lanaya, J. C. Renauld, and T. Michiels, “Characterization of the murine alpha interferon gene family,” Journal of Virology, vol. 78, no. 15, pp. 8219–8228, 2004. View at Publisher · View at Google Scholar · View at Scopus
  2. C. Dunn, M. Brunetto, G. Reynolds et al., “Cytokines induced during chronic hepatitis B virus infection promote a pathway for NK cell-mediated liver damage,” Journal Experimental Medicine, vol. 204, no. 3, pp. 667–680, 2007. View at Publisher · View at Google Scholar · View at Scopus
  3. M. Sarasin-Filipowicz, E. J. Oakeley, F. H. T. Duong et al., “Interferon signaling and treatment outcome in chronic hepatitis C,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 19, pp. 7034–7039, 2008. View at Publisher · View at Google Scholar · View at Scopus
  4. E. B. Wilson, D. H. Yamada, H. Elsaesser et al., “Blockade of chronic type I interferon signaling to control persistent LCMV infection,” Science, vol. 340, no. 6129, pp. 202–207, 2013. View at Publisher · View at Google Scholar · View at Scopus
  5. K. A. Hofmeyer, H. Jeon, and X. Zang, “The PD-1/PD-L1 (B7-H1) pathway in chronic infection-induced cytotoxic T lymphocyte exhaustion,” Journal of Biomedicine & Biotechnology, vol. 2011, Article ID 451694, p. 9, 2011. View at Publisher · View at Google Scholar · View at Scopus
  6. I. Teige, A. Treschow, A. Teige et al., “IFN-beta gene deletion leads to augmented and chronic demyelinating experimental autoimmune encephalomyelitis,” Journal of Immunology, vol. 170, no. 9, pp. 4776–4784, 2003. View at Publisher · View at Google Scholar
  7. C. Guiducci, M. Gong, Z. Xu et al., “TLR recognition of self nucleic acids hampers glucocorticoid activity in lupus,” Nature, vol. 465, no. 7300, pp. 937–941, 2010. View at Publisher · View at Google Scholar · View at Scopus
  8. T. Goldmann, T. Blank, and M. Prinz, “Fine-tuning of type I IFN-signaling in microglia—implications for homeostasis, CNS autoimmunity and interferonopathies,” Current Opinion in Neurobiology, vol. 36, pp. 38–42, 2016. View at Publisher · View at Google Scholar · View at Scopus
  9. A. N. Theofilopoulos, R. Baccala, B. Beutler, and D. H. Kono, “Type I interferons (alpha-beta) in immunity and autoimmunity,” Annual Review of Immunology, vol. 23, pp. 307–335, 2004. View at Google Scholar
  10. R. Hernández-Pando, H. Orozcoe, A. Sampieri et al., “Correlation between the kinetics of Th1, Th2 cells and pathology in a murine model of experimental pulmonary tuberculosis,” Immunology, vol. 89, no. 1, pp. 26–33, 1996. View at Google Scholar
  11. E. C. Borden, G. C. Sen, G. Uze et al., “Interferons at age 50: past, current and future impact on biomedicine,” Nature Reviews. Drug Discovery, vol. 6, no. 12, pp. 975–990, 2007. View at Publisher · View at Google Scholar · View at Scopus
  12. H. M. Lazear, T. J. Nice, and M. S. Diamond, “Interferon-λ: immune functions at barrier surfaces and beyond,” Immunity, vol. 43, no. 1, pp. 15–28, 2015. View at Publisher · View at Google Scholar · View at Scopus
  13. N. A. de Weerd, J. P. Vivian, T. K. Nguyen et al., “Structural basis of a unique interferon-[beta] signaling axis mediated via the receptor IFNAR1,” Nature Immunology, vol. 14, no. 9, pp. 901–907, 2013. View at Publisher · View at Google Scholar · View at Scopus
  14. L. B. Ivashkiv and L. T. Donlin, “Regulation of type I interferon responses,” Nature Reviews. Immunology, vol. 14, no. 1, pp. 36–49, 2014. View at Publisher · View at Google Scholar · View at Scopus
  15. P. Fitzgerald-Bocarsly, M. Feldman, M. Mendelsohn, S. Curl, and C. Lopez, “Human mononuclear cells which produce interferon-alpha during NK(HSV-FS) assays are HLA-DR positive cells distinct from cytolytic natural killer effectors,” Journal of Leukocyte Biology, vol. 43, no. 4, pp. 323–334, 1988. View at Google Scholar
  16. D. Parker and A. Prince, “Type I interferon response to extracellular bacteria in the airway epithelium,” Trends in Immunology, vol. 32, no. 12, pp. 582–588, 2011. View at Publisher · View at Google Scholar · View at Scopus
  17. M. Charrel-Dennis, E. Latz, K. A. Halmen et al., “TLR-independent type I interferon induction in response to an extracellular bacterial pathogen via intracellular recognition of its DNA,” Cell Host & Microbe, vol. 4, no. 6, pp. 543–554, 2008. View at Publisher · View at Google Scholar · View at Scopus
  18. T. B. Clarke and J. N. Weiser, “Intracellular sensors of extracellular bacteria,” Immunological Reviews, vol. 243, no. 1, pp. 9–25, 2011. View at Publisher · View at Google Scholar · View at Scopus
  19. G. M. Boxx and G. Cheng, “The roles of type I interferon in bacterial infection,” Cell Host & Microbe, vol. 19, no. 6, pp. 760–769, 2016. View at Publisher · View at Google Scholar · View at Scopus
  20. F. McNab, K. Mayer-Barber, A. Sher, A. Wack, and A. O’Garra, “Type I interferons in infectious disease,” Nature Reviews. Immunology, vol. 15, no. 2, pp. 87–103, 2015. View at Publisher · View at Google Scholar · View at Scopus
  21. L. Zitvogel, L. Galluzzi, O. Kepp, M. J. Smyth, and G. Kroemer, “Type I interferons in anticancer immunity,” Nature Reviews. Immunology, vol. 15, no. 7, pp. 405–414, 2015. View at Publisher · View at Google Scholar · View at Scopus
  22. O. Takeuchi and S. Akira, “Pattern recognition receptors and inflammation,” Cell, vol. 140, no. 6, pp. 805–820, 2010. View at Publisher · View at Google Scholar · View at Scopus
  23. S. Pandey, T. Kawai, and S. Akira, “Microbial sensing by Toll-like receptors and intracellular nucleic acid sensors,” Cold Spring Harbor Perspectives in Biology, vol. 7, no. 1, article a016246, 2015. View at Publisher · View at Google Scholar · View at Scopus
  24. A. M. Lundberg, S. K. Drexler, C. Monaco et al., “Key differences in TLR3/poly I:C signaling and cytokine induction by human primary cells: a phenomenon absent from murine cell systems,” Blood, vol. 110, no. 9, p. 3245, 2007. View at Publisher · View at Google Scholar · View at Scopus
  25. R. Barbalat, L. Lau, R. M. Locksley, and G. M. Barton, “Toll-like receptor 2 on inflammatory monocytes induces type I interferon in response to viral but not bacterial ligands,” Nature Immunology, vol. 10, no. 11, pp. 1200–1207, 2009. View at Publisher · View at Google Scholar · View at Scopus
  26. S. Uematsu and S. Akira, “Toll-like receptors and type I interferons,” The Journal of Biological Chemistry, vol. 282, no. 21, pp. 15319–15323, 2007. View at Publisher · View at Google Scholar · View at Scopus
  27. T. W. Kim, K. Staschke, K. Bulek et al., “A critical role for IRAK4 kinase activity in Toll-like receptor-mediated innate immunity,” The Journal of Experimental Medicine, vol. 204, no. 5, pp. 1025–1036, 2007. View at Publisher · View at Google Scholar · View at Scopus
  28. H. Hemmi, O. Takeuchi, T. Kawai et al., “A Toll-like receptor recognizes bacterial DNA,” Nature, vol. 408, no. 6813, pp. 740–745, 2000. View at Publisher · View at Google Scholar · View at Scopus
  29. A. Eaton-Bassiri, S. B. Dillon, M. Cunningham et al., “Toll-like receptor 9 can be expressed at the cell surface of distinct populations of tonsils and human peripheral blood mononuclear cells,” Infection and Immunity, vol. 72, no. 12, pp. 7202–7211, 2004. View at Publisher · View at Google Scholar · View at Scopus
  30. M. Adib-Conquy, D. Scott-Algara, J. M. Cavaillon, and F. Souza-Fonseca-Guimaraes, “TLR-mediated activation of NK cells and their role in bacterial/viral immune responses in mammals,” Immunology and Cell Biology, vol. 92, no. 3, pp. 256–262, 2014. View at Publisher · View at Google Scholar · View at Scopus
  31. T. Kawai and S. Akira, “Pathogen recognition with Toll-like receptors,” Current Opinion in Immunology, vol. 17, no. 4, pp. 338–344, 2005. View at Publisher · View at Google Scholar · View at Scopus
  32. R. Zhan, Q. Han, C. Zhang, Z. Tian, and J. Zhang, “Toll-like receptor 2 (TLR2) and TLR9 play opposing roles in host innate immunity against Salmonella enterica serovar Typhimurium infection,” Infection and Immunity, vol. 83, no. 4, pp. 1641–1649, 2015. View at Publisher · View at Google Scholar · View at Scopus
  33. U. Bhan, G. Trujillo, K. Lyn-Kew et al., “Toll-like receptor 9 regulates the lung macrophage phenotype and host immunity in murine pneumonia caused by Legionella pneumophila,” Infection and Immunity, vol. 76, no. 7, pp. 2895–2904, 2008. View at Publisher · View at Google Scholar · View at Scopus
  34. N. Arpaia, J. Godec, L. Lau et al., “TLR signaling is required for Salmonella typhimurium virulence,” Cell, vol. 144, no. 5, pp. 675–688, 2011. View at Publisher · View at Google Scholar · View at Scopus
  35. L. Y. Huang, K. J. Ishii, S. Akira, J. Aliberti, and B. Golding, “Th1-like cytokine induction by heat-killed Brucella abortus is dependent on triggering of TLR9,” Journal of Immunology, vol. 175, no. 6, p. 3964, 2005. View at Publisher · View at Google Scholar
  36. N. Lapaque, A. Muller, L. Alexopoulou, J. C. Howard, and J. P. Gorvel, “Brucella abortus induces Irgm3 and Irga6 expression via type-I IFN by a MyD88-dependent pathway, without the requirement of TLR2, TLR4, TLR5 and TLR9,” Microbial Pathogenesis, vol. 47, no. 6, pp. 299–304, 2009. View at Publisher · View at Google Scholar · View at Scopus
  37. S. R. Paludan and A. G. Bowie, “Immune sensing of DNA,” Immunity, vol. 38, no. 5, pp. 870–880, 2013. View at Publisher · View at Google Scholar · View at Scopus
  38. E. E. Gray, D. Winship, J. M. Snyder, S. J. Child, A. P. Geballe, and D. B. Stetson, “The AIM2-like receptors are dispensable for the interferon response to intracellular DNA,” Immunity, vol. 45, no. 2, pp. 255–266, 2016. View at Publisher · View at Google Scholar
  39. L. Sun, J. Wu, F. Du, X. Chen, and Z. J. Chen, “Cyclic GMP-AMP synthase is a cytosolic DNA sensor that activates the type-I interferon pathway,” Science, vol. 339, no. 6121, p. 10, 2013. View at Publisher · View at Google Scholar · View at Scopus
  40. A. C. Collins, H. Cai, T. Li et al., “Cyclic GMP-AMP synthase (cGAS) is an innate immune DNA sensor for Mycobacterium tuberculosis,” Cell Host & Microbe, vol. 17, no. 6, pp. 820–828, 2015. View at Publisher · View at Google Scholar · View at Scopus
  41. R. Wassermann, M. 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
  42. R. O. Watson, S. L. Bell, D. A. MacDuff et al., “The cytosolic sensor cGAS detects Mycobacterium tuberculosis DNA to induce type I interferons and activate autophagy,” Cell Host & Microbe, vol. 17, no. 6, pp. 811–819, 2015. View at Publisher · View at Google Scholar · View at Scopus
  43. K. Hansen, T. Prabakaran, A. Laustsen et al., “Listeria monocytogenes induces IFNβ expression through an IFI16-, cGAS- and STING-dependent pathway,” The EMBO Journal, vol. 33, no. 15, pp. 1654–1666, 2014. View at Publisher · View at Google Scholar · View at Scopus
  44. Y. Zhang, L. Yeruva, A. Marinov et al., “The DNA sensor, cyclic GMP-AMP synthase, is essential for induction of IFN-β during chlamydia trachomatis infection,” Journal of Immunology, vol. 193, no. 5, pp. 2394–2404, 2014. View at Publisher · View at Google Scholar · View at Scopus
  45. S. R. Paludan, “Activation and regulation of DNA-driven immune responses,” Microbiology and Molecular Biology Reviews, vol. 79, no. 2, pp. 225–241, 2015. View at Publisher · View at Google Scholar · View at Scopus
  46. A. Ablasser, F. Bauernfeind, G. Hartmann, E. Latz, K. A. Fitzgerald, and V. Hornung, “RIG-I dependent sensing of poly(dA-dT) via the induction of an RNA polymerase III transcribed RNA intermediate,” Nature Immunology, vol. 10, no. 10, pp. 1065–1072, 2009. View at Publisher · View at Google Scholar · View at Scopus
  47. Y. H. Chiu, J. B. MacMillan, and Z. J. Chen, “RNA polymerase III detects cytosolic DNA and induces type-I interferons through the RIG-I pathway,” Cell, vol. 138, no. 3, pp. 576–591, 2009. View at Publisher · View at Google Scholar · View at Scopus
  48. C. X. Koo, K. Kobiyama, Y. J. Shen et al., “RNA polymerase III regulates cytosolic RNA:DNA hybrids and intracellular microRNA expression,” The Journal of Biological Chemistry, vol. 290, no. 12, pp. 7463–7473, 2015. View at Publisher · View at Google Scholar · View at Scopus
  49. Z. Abdullah, M. Schlee, S. Roth et al., “RIG-I detects infection with live Listeria by sensing secreted bacterial nucleic acids,” The EMBO Journal, vol. 31, no. 21, pp. 4153–4164, 2012. View at Publisher · View at Google Scholar · View at Scopus
  50. E. Dixit and J. C. Kagan, “Intracellular pathogen detection by RIG-I-like receptors,” Advances in Immunology, vol. 117, pp. 99–125, 2013. View at Publisher · View at Google Scholar · View at Scopus
  51. H. Kato, O. Takeuchi, E. Mikamo-Satoh et al., “Length-dependent recognition of double-stranded ribonucleic acids by retinoic acid-inducible gene-I and melanoma differentiation-associated gene 5,” Journal of Experimental Medicine, vol. 205, no. 7, pp. 1601–1610, 2008. View at Publisher · View at Google Scholar · View at Scopus
  52. S. Jensen and A. R. Thomsen, “Sensing of RNA viruses: a review of innate immune receptors involved in recognizing RNA virus invasion,” Journal of Virology, vol. 86, no. 6, pp. 2900–2910, 2012. View at Publisher · View at Google Scholar · View at Scopus
  53. S. Reikine, J. B. Nguyen, and Y. Modis, “Pattern recognition and signaling mechanisms of RIG-I and MDA5,” Frontiers in Immunology, vol. 5, p. 342, 2014. View at Publisher · View at Google Scholar · View at Scopus
  54. K. R. Rodriguez, A. M. Bruns, and C. M. Horvath, “MDA5 and LGP2: accomplices and antagonists of antiviral signal transduction,” Journal of Virology, vol. 88, no. 15, pp. 8194–8200, 2014. View at Publisher · View at Google Scholar · View at Scopus
  55. V. Motta, F. Soares, T. Sun, and D. J. Philpott, “NOD-like receptors: versatile cytosolic sentinels,” Physiological Reviews, vol. 95, no. 1, p. 149, 2014. View at Publisher · View at Google Scholar · View at Scopus
  56. G. Chen, M. H. Shaw, Y. G. Kim, and G. Nunez, “NOD-like receptors: role in innate immunity and inflammatory disease,” Annual Review of Pathology: Mechanisms of Disease, vol. 4, pp. 365–398, 2009. View at Publisher · View at Google Scholar · View at Scopus
  57. S. E. Girardin, I. G. Boneca, J. Viala et al., “Nod2 is a general sensor of peptidoglycan through Muramyl dipeptide (MDP) detection,” The Journal of Biological Chemistry, vol. 278, no. 11, pp. 8869–8872, 2003. View at Publisher · View at Google Scholar · View at Scopus
  58. S. E. Girardin, I. G. Boneca, L. A. M. Carneiro et al., “Nod1 detects a unique muropeptide from gram-negative bacterial peptidoglycan,” Science, vol. 300, no. 5625, p. 1584, 2003. View at Publisher · View at Google Scholar · View at Scopus
  59. Y. Zhong, A. Kinio, and M. Saleh, “Functions of NOD-like receptors in human diseases,” Frontiers in Immunology, vol. 4, p. 333, 2013. View at Publisher · View at Google Scholar
  60. A. Sabbah, T. H. Chang, R. Harnack et al., “Activation of innate immune antiviral responses by Nod2,” Nature Immunology, vol. 10, no. 10, pp. 1073–1080, 2009. View at Publisher · View at Google Scholar · View at Scopus
  61. T. Watanabe, N. Asano, A. Kitani, I. J. Fuss, T. Chiba, and W. Strober, “NOD1-mediated mucosal host defense against helicobacter pylori,” International Journal of Inflammation, vol. 2010, Article ID 476482, p. 6, 2010. View at Publisher · View at Google Scholar
  62. I. M. Dambuza and G. D. Brown, “C-type lectins in immunity: recent developments,” Current Opinion in Immunology, vol. 32, pp. 21–27, 2015. View at Publisher · View at Google Scholar · View at Scopus
  63. J. C. Hoving, G. J. Wilson, and G. D. Brown, “Signalling C-type lectin receptors, microbial recognition and immunity,” Cellular Microbiology, vol. 16, no. 2, pp. 185–194, 2014. View at Publisher · View at Google Scholar · View at Scopus
  64. G. Trinchieri, “Type I interferon: friend or foe?” The Journal of Experimental Medicine, vol. 207, no. 10, pp. 2053–2063, 2010. View at Publisher · View at Google Scholar · View at Scopus
  65. S. Kaur and L. C. Platanias, “IFN-[beta]-specific signaling via a unique IFNAR1 interaction,” Nature Immunology, vol. 14, no. 9, pp. 884–885, 2013. View at Publisher · View at Google Scholar · View at Scopus
  66. L. C. Platanias, “Mechanisms of type-I- and type-II-interferon-mediated signalling,” Nature Reviews. Immunology, vol. 5, no. 5, pp. 375–386, 2005. View at Publisher · View at Google Scholar · View at Scopus
  67. A. K. Perry, G. Chen, D. Zheng, H. Tang, and G. Cheng, “The host type I interferon response to viral and bacterial infections,” Cell Research, vol. 15, no. 6, pp. 407–422, 2005. View at Publisher · View at Google Scholar · View at Scopus
  68. H. Cho and B. L. Kelsall, “The role of type I interferons in intestinal infection, homeostasis, and inflammation,” Immunological Reviews, vol. 260, no. 1, pp. 145–167, 2014. View at Publisher · View at Google Scholar · View at Scopus
  69. J. Kazar, J. D. Gillmore, and F. B. Gordon, “Effect of interferon and interferon inducers on infections with a nonviral intracellular microorganism, chlamydia trachomatis,” Infection and Immunity, vol. 3, no. 6, pp. 825–832, 1971. View at Google Scholar
  70. L. M. de la Maza, E. M. Peterson, J. M. Goebel, C. W. Fennie, and C. W. Czarniecki, “Interferon-induced inhibition of chlamydia trachomatis: dissociation from antiviral and antiproliferative effects,” Infection and Immunity, vol. 47, no. 3, pp. 719–722, 1985. View at Google Scholar
  71. T. Ishihara, M. Aga, K. Hino et al., “Inhibition of Chlamydia trachomatis growth by human interferon-alpha: mechanisms and synergistic effect with interferon-gamma; and tumor necrosis factor-alpha,” Biomedical Research, vol. 26, no. 4, pp. 179–185, 2005. View at Publisher · View at Google Scholar · View at Scopus
  72. P. Puccetti, “On watching the watchers: IDO and type I/II IFN,” European Journal of Immunology, vol. 37, no. 4, pp. 876–879, 2007. View at Publisher · View at Google Scholar · View at Scopus
  73. U. M. Nagarajan, D. Prantner, J. D. Sikes et al., “Type I interferon signaling exacerbates Chlamydia muridarum genital infection in a murine model,” Infection and Immunity, vol. 76, no. 10, pp. 4642–4648, 2008. View at Publisher · View at Google Scholar · View at Scopus
  74. M. Rayamajhi, J. Humann, K. Penheiter, K. Andreasen, and L. L. Lenz, “Induction of IFN-alpha-beta enables Listeria monocytogenes to suppress macrophage activation by IFN-gamma,” The Journal of Experimental Medicine, vol. 207, no. 2, pp. 327–337, 2010. View at Publisher · View at Google Scholar · View at Scopus
  75. B. Lukas and J. Hruskova, “A virus inhibitor circulating in the blood of chickens, induced by Francisella tularensis and Listeria monocytogenes,” Folia Microbiologia (Praha), vol. 12, no. 2, pp. 157–161, 1967. View at Publisher · View at Google Scholar · View at Scopus
  76. E. A. Havell, “Augmented induction of interferons during Listeria monocytogenes infection,” The Journal of Infectious Diseases, vol. 153, no. 5, pp. 960–969, 1986. View at Publisher · View at Google Scholar · View at Scopus
  77. E. A. Havell, “Listeria monocytogenes-induced interferon-gamma primes the host for production of tumor necrosis factor and interferon-alpha/beta,” The Journal of Infectious Diseases, vol. 167, no. 6, pp. 1364–1371, 1993. View at Publisher · View at Google Scholar · View at Scopus
  78. C. E. Witte, K. A. Archer, C. S. Rae, J. D. Sauer, J. J. Woodward, and D. A. Portnoy, “Chapter 8 - innate immune pathways triggered by Listeria monocytogenes and their role in the induction of cell-mediated immunity,” in Advances in Immunology Immunity to Listeria monocytogenes, R. U. A. J. Emil, Ed., vol. 113, pp. 135–156, Academic Press, Cambridge, MA, USA, 2012. View at Google Scholar
  79. K. A. Archer, J. Durack, and D. A. Portnoy, “STING-dependent type I IFN production inhibits cell-mediated immunity to Listeria monocytogenes,” PLoS Pathogens, vol. 10, no. 1, article e1003861, 2014. View at Publisher · View at Google Scholar · View at Scopus
  80. C. A. Hagmann, A. M. Herzner, Z. Abdullah et al., “RIG-I detects triphosphorylated RNA of Listeria monocytogenes during infection in non-immune cells,” PLoS One, vol. 8, no. 4, article e62872, 2013. View at Publisher · View at Google Scholar · View at Scopus
  81. J. H. Leber, G. T. Crimmins, S. Raghavan, N. P. Meyer-Morse, J. S. Cox, and D. A. Portnoy, “Distinct TLR- and NLR-mediated transcriptional responses to an intracellular pathogen,” PLoS Pathogens, vol. 4, no. 1, article e6, 2008. View at Publisher · View at Google Scholar · View at Scopus
  82. D. B. Stetson and R. Medzhitov, “Recognition of cytosolic DNA activates an IRF3-dependent innate immune response,” Immunity, vol. 24, no. 1, pp. 93–103, 2006. View at Publisher · View at Google Scholar · View at Scopus
  83. J. J. Woodward, A. T. Iavarone, and D. A. Portnoy, “C-di-AMP secreted by intracellular Listeria monocytogenes activates a host type I interferon response,” Science, vol. 328, no. 5986, pp. 1703–1705, 2010. View at Publisher · View at Google Scholar · View at Scopus
  84. D. L. Burdette, K. M. Monroe, K. Sotelo-Troha et al., “STING is a direct innate immune sensor of cyclic-di-GMP,” Nature, vol. 478, no. 7370, pp. 515–518, 2011. View at Publisher · View at Google Scholar · View at Scopus
  85. K. T. Schwartz, J. D. Carleton, S. J. Quillin, S. D. Rollins, D. A. Portnoy, and J. H. Leber, “Hyperinduction of host beta interferon by a Listeria monocytogenes strain naturally overexpressing the multidrug efflux pump MdrT,” Infection and Immunity, vol. 80, no. 4, pp. 1537–1545, 2012. View at Publisher · View at Google Scholar · View at Scopus
  86. K. J. Ishii, T. Kawagoe, S. Koyama et al., “TANK-binding kinase-1 delineates innate and adaptive immune responses to DNA vaccines,” Nature, vol. 451, no. 7179, pp. 725–729, 2008. View at Publisher · View at Google Scholar · View at Scopus
  87. R. M. O’Connell, S. K. Saha, S. A. Vaidya et al., “Type I interferon production enhances susceptibility to Listeria monocytogenes infection,” Journal Experimental Medicine, vol. 200, no. 4, pp. 437–445, 2004. View at Publisher · View at Google Scholar · View at Scopus
  88. J. A. Carrero, B. Calderon, and E. R. Unanue, “Type I interferon sensitizes lymphocytes to apoptosis and reduces resistance to Listeria infection,” Journal Experimental Medicine, vol. 200, no. 4, p. 535, 2004. View at Publisher · View at Google Scholar · View at Scopus
  89. V. Auerbuch, D. G. Brockstedt, N. Meyer-Morse, M. O’Riordan, and D. A. Portnoy, “Mice lacking the type I interferon receptor are resistant to Listeria monocytogenes,” The Journal of Experimental Medicine, vol. 200, no. 4, pp. 527–533, 2004. View at Publisher · View at Google Scholar · View at Scopus
  90. T. Reimer, M. Schweizer, and T. W. Jungi, “Type I IFN induction in response to Listeria monocytogenes in human macrophages: evidence for a differential activation of IFN regulatory factor 3 (IRF3),” Journal of Immunology, vol. 179, no. 2, p. 1166, 2007. View at Publisher · View at Google Scholar
  91. T. Henry, G. S. Kirimanjeswara, T. Ruby et al., “Type I interferon signaling constrains IL-17A/F secretion by γδ T cells during bacterial infections,” Journal of Immunology, vol. 184, no. 7, pp. 3755–3767, 2010. View at Publisher · View at Google Scholar · View at Scopus
  92. S. E. Osborne, B. Sit, A. Shaker et al., “Type I interferon promotes cell-to-cell spread of Listeria monocytogenes,” Cellular Microbiology, vol. 19, no. 3, 2017. View at Publisher · View at Google Scholar
  93. S. J. Kearney, C. Delgado, E. M. Eshleman, K. K. Hill, B. P. O’Connor, and L. L. Lenz, “Type I interferons down regulate myeloid cell IFNGR by inducing recruitment of an Egr3/Nab1 complex that silences ifngr1 transcription,” Journal of Immunology, vol. 191, no. 6, pp. 3384–3392, 2013. View at Publisher · View at Google Scholar · View at Scopus
  94. M. G. Pitts, T. Myers-Morales, and S. E. F. D’Orazio, “Type I IFN does not promote susceptibility to foodborne Listeria monocytogene,” Journal of Immunology, vol. 196, no. 7, p. 3109, 2016. View at Publisher · View at Google Scholar · View at Scopus
  95. E. Kernbauer, V. Maier, I. Rauch, M. Müller, and T. Decker, “Route of infection determines the impact of type I interferons on innate immunity to Listeria monocytogenes,” PLoS One, vol. 8, no. 6, article e65007, 2013. View at Publisher · View at Google Scholar · View at Scopus
  96. B. Lechartier, J. Rybniker, A. Zumla, and S. T. Cole, “Tuberculosis drug discovery in the post-post-genomic era,” EMBO Molecular Medicine, vol. 6, no. 2, pp. 158–168, 2014. View at Publisher · View at Google Scholar · View at Scopus
  97. C. Manca, L. Tsenova, S. Freeman et al., “Hypervirulent M. Tuberculosis W/Beijing strains upregulate type I IFNs and increase expression of negative regulators of the Jak-Stat pathway,” Journal of Interferon & Cytokine Research, vol. 25, no. 11, pp. 694–701, 2005. View at Publisher · View at Google Scholar · View at Scopus
  98. A. Dorhoi, V. Yeremeev, G. Nouailles et al., “Type I IFN signaling triggers immunopathology in tuberculosis-susceptible mice by modulating lung phagocyte dynamics,” European Journal of Immunology, vol. 44, no. 8, pp. 2380–2393, 2014. View at Publisher · View at Google Scholar · View at Scopus
  99. S. A. Stanley, J. E. Johndrow, P. Manzanillo, and J. S. Cox, “The type I IFN response to infection with Mycobacterium tuberculosis requires ESX-1-mediated secretion and contributes to pathogenesis,” Journal of Immunology, vol. 178, no. 5, p. 3143, 2007. View at Publisher · View at Google Scholar
  100. M. P. R. Berry, C. M. Graham, F. W. McNab et al., “An interferon-inducible neutrophil-driven blood transcriptional signature in human tuberculosis,” Nature, vol. 466, no. 7309, pp. 973–977, 2010. View at Publisher · View at Google Scholar · View at Scopus
  101. A. K. Pandey, Y. Yang, Z. Jiang et al., “NOD2, RIP2 and IRF5 play a critical role in the type I interferon response to Mycobacterium tuberculosis,” PLoS Pathogens, vol. 5, no. 7, article e1000500, 2009. View at Publisher · View at Google Scholar · View at Scopus
  102. E. J. M. Stoop, W. Bitter, and A. M. van der Sar, “Tubercle bacilli rely on a type VII army for pathogenicity,” Trends in Microbiology, vol. 20, no. 10, pp. 477–484, 2012. View at Publisher · View at Google Scholar · View at Scopus
  103. B. B. Mishra, P. Moura-Alves, A. Sonawane et al., “Mycobacterium tuberculosis protein ESAT-6 is a potent activator of the NLRP3/ASC inflammasome,” Cellular Microbiology, vol. 12, no. 8, pp. 1046–1063, 2010. View at Publisher · View at Google Scholar · View at Scopus
  104. 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
  105. C. Manca, L. Tsenova, A. Bergtold et al., “Virulence of a Mycobacterium tuberculosis clinical isolate in mice is determined by failure to induce Th1 type immunity and is associated with induction of IFN-alpha-beta,” PNAS, vol. 98, no. 10, pp. 5752–5757, 2001. View at Publisher · View at Google Scholar · View at Scopus
  106. F. Bouchonnet, N. Boechat, M. Bonay, and A. J. Hance, “Alpha/Beta interferon impairs the ability of human macrophages to control growth of Mycobacterium bovis BCG,” Infection and Immunity, vol. 70, no. 6, pp. 3020–3025, 2002. View at Publisher · View at Google Scholar · View at Scopus
  107. L. Moreira-Teixeira, J. Sousa, F. W. McNab et al., “Type I IFN inhibits alternative macrophage activation during Mycobacterium tuberculosis infection and leads to enhanced protection in the absence of IFN-γ signaling,” Journal of Immunology, vol. 197, no. 12, pp. 4714–4726, 2016. View at Publisher · View at Google Scholar
  108. M. Lorkowski, A. Felipe-López, C. A. Danzer, N. Hansmeier, and M. Hensel, “Salmonella enterica invasion of polarized epithelial cells is a highly cooperative effort,” Infection and Immunity, vol. 82, no. 6, pp. 2657–2667, 2014. View at Publisher · View at Google Scholar · View at Scopus
  109. C. G. Forest, E. Ferraro, S. C. Sabbagh, and F. Daigle, “Intracellular survival of Salmonella enterica serovar Typhi in human macrophages is independent of Salmonella pathogenicity island (SPI)-2,” Microbiology, vol. 156, Part 12, pp. 3689–3698, 2010. View at Publisher · View at Google Scholar · View at Scopus
  110. O. Steele-Mortimer, J. H. Brumell, L. A. Knodler, S. Méresse, A. Lopez, and B. B. Finlay, “The invasion-associated type III secretion system of Salmonella enterica serovar Typhimurium is necessary for intracellular proliferation and vacuole biogenesis in epithelial cells,” Cellular Microbiology, vol. 4, no. 1, pp. 43–54, 2002. View at Publisher · View at Google Scholar · View at Scopus
  111. P. Broz, K. Newton, M. Lamkanfi, S. Mariathasan, V. M. Dixit, and D. M. Monack, “Redundant roles for inflammasome receptors NLRP3 and NLRC4 in host defense against Salmonella,” The Journal of Experimental Medicine, vol. 207, no. 8, pp. 1745–1755, 2010. View at Publisher · View at Google Scholar · View at Scopus
  112. P. Broz, T. Ruby, K. Belhocine et al., “Caspase-11 increases susceptibility to Salmonella infection in the absence of caspase-1,” Nature, vol. 490, no. 7419, pp. 288–291, 2012. View at Publisher · View at Google Scholar · View at Scopus
  113. K. A. Owen, C. J. Anderson, and J. E. Casanova, “Salmonella suppresses the TRIF-dependent type I interferon response in macrophages,” MBio, vol. 7, no. 1, article e02051–15, 2016. View at Publisher · View at Google Scholar · View at Scopus
  114. M. Schmolke, J. R. Patel, E. de Castro et al., “RIG-I detects mRNA of intracellular Salmonella enterica serovar Typhimurium during bacterial infection,” MBio, vol. 5, no. 2, article e01006–14, 2014. View at Publisher · View at Google Scholar · View at Scopus
  115. M. Lara-Tejero, F. S. Sutterwala, Y. Ogura et al., “Role of the caspase-1 inflammasome in Salmonella typhimurium pathogenesis,” The Journal of Experimental Medicine, vol. 203, no. 6, pp. 1407–1412, 2006. View at Publisher · View at Google Scholar · View at Scopus
  116. B. Raupach, S. K. Peuschel, D. M. Monack, and A. Zychlinsky, “Caspase-1-mediated activation of interleukin-1b (IL-1β) and IL-18 contributes to innate immune defenses against Salmonella enterica serovar Typhimurium infection,” Infection and Immunity, vol. 74, no. 8, pp. 4922–4926, 2006. View at Publisher · View at Google Scholar · View at Scopus
  117. N. Kayagaki, S. Warming, M. Lamkanfi et al., “Non-canonical inflammasome activation targets caspase-11,” Nature, vol. 479, no. 7371, pp. 117–121, 2011. View at Publisher · View at Google Scholar · View at Scopus
  118. E. A. Miao, D. P. Mao, N. Yudkovsky et al., “Innate immune detection of the type III secretion apparatus through the NLRC4 inflammasome,” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 7, pp. 3076–3080, 2010. View at Publisher · View at Google Scholar · View at Scopus
  119. G. Bukholm, B. P. Berdal, C. Haug, and M. Degré, “Mouse fibroblast interferon modifies Salmonella typhimurium infection in infant mice,” Infection and Immunity, vol. 45, no. 1, pp. 62–66, 1984. View at Google Scholar
  120. N. Robinson, S. McComb, R. Mulligan, R. Dudani, L. Krishnan, and S. Sad, “Type I interferon induces necroptosis in macrophages during infection with Salmonella enterica serovar Typhimurium,” Nature Immunology, vol. 13, no. 10, pp. 954–962, 2012. View at Publisher · View at Google Scholar · View at Scopus
  121. P. Vandenabeele, W. Declercq, F. Van Herreweghe, and T. Vanden Berghe, “The role of the kinases RIP1 and RIP3 in TNF-induced necrosis,” Science Signaling, vol. 3, no. 115, p. re4, 2010. View at Publisher · View at Google Scholar · View at Scopus
  122. D. J. Perkins, R. Rajaiah, S. M. Tennant et al., “Salmonella typhimurium co-opts the host type I IFN system to restrict macrophage innate immune transcriptional responses selectively,” Journal of Immunology, vol. 195, no. 5, pp. 2461–2471, 2015. View at Publisher · View at Google Scholar · View at Scopus
  123. C. Dilantika, E. R. Sedyaningsih, M. R. Kasper et al., “Influenza virus infection among pediatric patients reporting diarrhea and influenza-like illness,” BMC Infectious Diseases, vol. 10, no. 1, p. 3, 2010. View at Publisher · View at Google Scholar · View at Scopus
  124. E. Deriu, G. M. Boxx, X. He et al., “Influenza virus affects intestinal microbiota and secondary Salmonella infection in the gut through type I interferons,” PLoS Pathogens, vol. 12, no. 5, article e1005572, 2016. View at Publisher · View at Google Scholar · View at Scopus
  125. M. A. Freudenberg, T. Merlin, C. Kalis, Y. Chvatchko, H. Stübig, and C. Galanos, “Cutting edge: a murine, IL-12-independent pathway of IFN-gamma induction by gram-negative bacteria based on STAT4 activation by type I IFN and IL-18 signaling,” Journal of Immunology, vol. 169, no. 4, pp. 1665–1668, 2002. View at Publisher · View at Google Scholar
  126. T. Henry, A. Brotcke, D. S. Weiss, L. J. Thompson, and D. M. Monack, “Type I interferon signaling is required for activation of the inflammasome during Francisella infection,” The Journal of Experimental Medicine, vol. 204, no. 5, pp. 987–994, 2007. View at Publisher · View at Google Scholar · View at Scopus
  127. C. Checroun, T. D. Wehrly, E. R. Fischer, S. F. Hayes, and J. Celli, “Autophagy-mediated reentry of Francisella tularensis into the endocytic compartment after cytoplasmic replication,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 39, pp. 14578–14583, 2006. View at Publisher · View at Google Scholar · View at Scopus
  128. L. A. Allen, “Interview with Dr. Lee-Ann Allen regarding pivotal advance: Francisella tularensis LVS evades killing by human neutrophils via inhibition of the respiratory burst and phagosome escape,” Journal of Leukocyte Biology, vol. 80, no. 6, pp. 1222–1223, 2006. View at Publisher · View at Google Scholar · View at Scopus
  129. J. D. Hall, M. D. Woolard, B. M. Gunn et al., “Infected-host-cell repertoire and cellular response in the lung following inhalation of Francisella tularensis Schu S4, LVS, or U112,” Infection and Immunity, vol. 76, no. 12, pp. 5843–5852, 2008. View at Publisher · View at Google Scholar · View at Scopus
  130. G. S. Baron and F. E. Nano, “MglA and MglB are required for the intramacrophage growth of Francisella novicida,” Molecular Microbiology, vol. 29, no. 1, pp. 247–259, 1998. View at Publisher · View at Google Scholar · View at Scopus
  131. M. Santic, M. Molmeret, K. E. Klose, S. Jones, and Y. A. Kwaik, “The Francisella tularensis pathogenicity island protein IglC and its regulator MglA are essential for modulating phagosome biogenesis and subsequent bacterial escape into the cytoplasm,” Cellular Microbiology, vol. 7, no. 7, pp. 969–979, 2005. View at Publisher · View at Google Scholar · View at Scopus
  132. S. Mariathasan, D. S. Weiss, V. M. Dixit, and D. M. Monack, “Innate immunity against Francisella tularensis is dependent on the ASC/caspase-1 axis,” The Journal of Experimental Medicine, vol. 202, no. 8, pp. 1043–1049, 2005. View at Publisher · View at Google Scholar · View at Scopus
  133. M. A. Gavrilin, I. J. Bouakl, N. L. Knatz et al., “Internalization and phagosome escape required for Francisella to induce human monocyte IL-1β processing and release,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 1, pp. 141–146, 2006. View at Publisher · View at Google Scholar · View at Scopus
  134. A. M. Hajjar, M. D. Harvey, S. A. Shaffer et al., “Lack of in vitro and in vivo recognition of Francisella tularensis subspecies lipopolysaccharide by Toll-like receptors,” Infection and Immunity, vol. 74, no. 12, pp. 6730–6738, 2006. View at Publisher · View at Google Scholar · View at Scopus
  135. K. M. Storek, N. A. Gertsvolf, M. B. Ohlson, and D. M. Monack, “cGAS and Ifi204 cooperate to produce type I IFNs in response to Francisella infection,” Journal of Immunology, vol. 194, no. 7, pp. 3236–3245, 2015. View at Publisher · View at Google Scholar · View at Scopus
  136. K. A. Fitzgerald and V. A. K. Rathinam, “GBPs take AIM at Francisella,” Nature Immunology, vol. 16, no. 5, pp. 443–444, 2015. View at Publisher · View at Google Scholar · View at Scopus
  137. S. M. Man, R. Karki, R. K. S. Malireddi et al., “The transcription factor IRF1 and guanylate-binding proteins target activation of the AIM2 inflammasome by Francisella infection,” Nature Immunology, vol. 16, no. 5, pp. 467–475, 2015. View at Publisher · View at Google Scholar · View at Scopus
  138. E. Meunier, P. Wallet, R. F. Dreier et al., “Guanylate-binding proteins promote activation of the AIM2 inflammasome during infection with Francisella novicida,” Nature Immunology, vol. 16, no. 5, pp. 476–484, 2015. View at Publisher · View at Google Scholar · View at Scopus
  139. B. H. Kim, A. R. Shenoy, P. Kumar, R. Das, S. Tiwari, and J. D. MacMicking, “A family of IFN-gamma-inducible 65-kD GTPases protects against bacterial infection,” Science, vol. 332, no. 6030, pp. 717–721, 2011. View at Publisher · View at Google Scholar · View at Scopus
  140. J. Celli, C. de Chastellier, D. M. Franchini, J. Pizarro-Cerda, E. Moreno, and J. P. Gorvel, “Brucella evades macrophage killing via VirB-dependent sustained interactions with the endoplasmic reticulum,” Journal Experimental. Medicine, vol. 198, no. 4, pp. 545–556, 2003. View at Publisher · View at Google Scholar · View at Scopus
  141. S. P. Salcedo, M. I. Marchesini, H. Lelouard et al., “Brucella control of dendritic cell maturation is dependent on the TIR-containing protein Btp1,” PLoS Pathogens, vol. 4, no. 2, article e21, 2008. View at Publisher · View at Google Scholar · View at Scopus
  142. X. Li and Y. He, “Caspase-2-dependent dendritic cell death, maturation, and priming of T cells in response to Brucella abortus infection,” PLoS One, vol. 7, no. 8, article e43512, 2012. View at Publisher · View at Google Scholar · View at Scopus
  143. M. T. Gomes, P. C. Campos, L. A. de Almeida et al., “The role of innate immune signals in immunity to Brucella abortus,” Frontiers in Cellular and Infection Microbiology, vol. 2, p. 130, 2012. View at Publisher · View at Google Scholar
  144. L. A. de Almeida, N. B. Carvalho, F. S. Oliveira et al., “MyD88 and STING signaling pathways are required for IRF3-mediated IFN−+¦ induction in response to Brucella abortus infection,” PLoS One, vol. 6, no. 8, article e23135, 2011. View at Publisher · View at Google Scholar · View at Scopus
  145. C. M. Roux, H. G. Rolán, R. L. Santos et al., “Brucella requires a functional Type IV secretion system to elicit innate immune responses in mice,” Cellular Microbiology, vol. 9, no. 7, pp. 1851–1869, 2007. View at Publisher · View at Google Scholar · View at Scopus
  146. A. L. Neild and C. R. Roy, “Immunity to vacuolar pathogens: what can we learn from Legionella?” Cellular Microbiology, vol. 6, no. 11, pp. 1011–1018, 2004. View at Publisher · View at Google Scholar · View at Scopus
  147. G. Segal, M. Feldman, and T. Zusman, “The Icm/Dot type-IV secretion systems of Legionella pneumophila and Coxiella burnetii,” FEMS Microbiology Reviews, vol. 29, no. 1, pp. 65–81, 2005. View at Publisher · View at Google Scholar · View at Scopus
  148. A. M. Richards, J. E. Von Dwingelo, C. T. Price, and Y. Abu Kwaik, “Cellular microbiology and molecular ecology of Legionella-amoeba interaction,” Virulence, vol. 4, no. 4, pp. 307–314, 2013. View at Publisher · View at Google Scholar · View at Scopus
  149. G. Schiavoni, C. Mauri, D. Carlei, F. Belardelli, M. Castellani Pastoris, and E. Proietti, “Type I IFN protects permissive macrophages from Legionella pneumophila infection through an IFN-γ-independent pathway,” Journal of Immunology, vol. 173, no. 2, pp. 1266–1275, 2004. View at Publisher · View at Google Scholar
  150. B. Opitz, M. Vinzing, V. van Laak et al., “Legionella pneumophila induces IFNβ in lung epithelial cells via IPS-1 and IRF3, which also control bacterial replication,” The Journal of Biological Chemistry, vol. 281, no. 47, pp. 36173–36179, 2006. View at Publisher · View at Google Scholar · View at Scopus
  151. K. M. Monroe, S. M. McWhirter, and R. E. Vance, “Identification of host cytosolic sensors and bacterial factors regulating the type I interferon response to Legionella pneumophila,” PLoS Pathogens, vol. 5, no. 11, article e1000665, 2009. View at Publisher · View at Google Scholar · View at Scopus
  152. A. A. Abdul-Sater, I. Tattoli, L. Jin et al., “Cyclic-di-GMP and cyclic-di-AMP activate the NLRP3 inflammasome,” EMBO Reports, vol. 14, no. 10, pp. 900–906, 2013. View at Publisher · View at Google Scholar · View at Scopus
  153. J. Lippmann, H. C. Müller, J. Naujoks et al., “Dissection of a type I interferon pathway in controlling bacterial intracellular infection in mice,” Cellular Microbiology, vol. 13, no. 11, pp. 1668–1682, 2011. View at Publisher · View at Google Scholar · View at Scopus
  154. C. R. Plumlee, C. Lee, A. A. Beg, T. Decker, H. A. Shuman, and C. Schindler, “Interferons direct an effective innate response to Legionella pneumophila infection,” The Journal of Biological Chemistry, vol. 284, no. 44, pp. 30058–30066, 2009. View at Publisher · View at Google Scholar · View at Scopus
  155. A. A. Abdul-Sater, A. Majoros, C. Plumlee et al., “Different STAT transcription complexes drive early and delayed responses to type I IFNs,” Journal of Immunology, vol. 195, no. 1, pp. 210–216, 2015. View at Publisher · View at Google Scholar · View at Scopus
  156. D. K. Y. Ang, C. V. L. Oates, R. Schuelein et al., “Cutting edge: pulmonary Legionella pneumophila is controlled by Plasmacytoid dendritic cells but not type I IFN,” Journal of Immunology, vol. 184, no. 10, pp. 5429–5433, 2010. View at Publisher · View at Google Scholar · View at Scopus
  157. M. Calverley, S. Erickson, A. J. Read, and A. G. Harmsen, “Resident alveolar macrophages are susceptible to and permissive of Coxiella burnetii infection,” PLoS One, vol. 7, no. 12, article e51941, 2012. View at Publisher · View at Google Scholar · View at Scopus
  158. R. A. Heinzen, M. A. Scidmore, D. D. Rockey, and T. Hackstadt, “Differential interaction with endocytic and exocytic pathways distinguish parasitophorous vacuoles of Coxiella burnetii and chlamydia trachomatis,” Infection and Immunity, vol. 64, no. 3, pp. 796–809, 1996. View at Google Scholar
  159. S. Meconi, C. Capo, M. Remacle-Bonnet, G. Pommier, D. Raoult, and J. L. Mege, “Activation of protein tyrosine kinases by Coxiella burnetii: role in actin cytoskeleton reorganization and bacterial phagocytosis,” Infection and Immunity, vol. 69, no. 4, pp. 2520–2526, 2001. View at Publisher · View at Google Scholar · View at Scopus
  160. P. S. Romano, M. G. Gutierrez, W. Berón, M. Rabinovitch, and M. I. Colombo, “The autophagic pathway is actively modulated by phase II Coxiella burnetii to efficiently replicate in the host cell,” Cellular Microbiology, vol. 9, no. 4, pp. 891–909, 2007. View at Publisher · View at Google Scholar · View at Scopus
  161. A. O. Barry, N. Boucherit, G. Mottola et al., “Impaired stimulation of p38α-MAPK/Vps41-HOPS by LPS from pathogenic Coxiella burnetii prevents trafficking to microbicidal phagolysosomes,” Cell Host & Microbe, vol. 12, no. 6, pp. 751–763, 2012. View at Publisher · View at Google Scholar · View at Scopus
  162. J. Dellacasagrande, C. Capo, D. Raoult, and J. L. Mege, “IFN-γ mediated control of Coxiella burnetii survival in monocytes: the role of cell apoptosis and TNF,” Journal of Immunology, vol. 162, no. 4, pp. 2259–2265, 1999. View at Google Scholar
  163. A. Honstettre, G. Imbert, E. Ghigo et al., “Dysregulation of cytokines in acute Q fever: role of interleukin-10 and tumor necrosis factor in chronic evolution of Q fever,” The Journal of Infectious Diseases, vol. 187, no. 6, pp. 956–962, 2003. View at Publisher · View at Google Scholar · View at Scopus
  164. E. Ghigo, A. Honstettre, C. Capo, J. P. Gorvel, D. Raoult, and J. L. Mege, “Link between impaired maturation of phagosomes and defective Coxiella burnetii killing in patients with chronic Q fever,” The Journal of Infectious Diseases, vol. 190, no. 10, pp. 1767–1772, 2004. View at Publisher · View at Google Scholar · View at Scopus
  165. S. Meghari, Y. Bechah, C. Capo et al., “Persistent Coxiella burnetii infection in mice overexpressing IL-10: an efficient model for chronic Q fever pathogenesis,” PLoS Pathogens, vol. 4, no. 2, article e23, 2008. View at Publisher · View at Google Scholar · View at Scopus
  166. K. P. Williams, J. J. Gillespie, B. W. S. Sobral et al., “Phylogeny of gammaproteobacteria,” Journal of Bacteriology, vol. 192, no. 9, pp. 2305–2314, 2010. View at Publisher · View at Google Scholar · View at Scopus
  167. J. F. Hedges, A. Robison, E. Kimmel et al., “Type I IFN counters or promotes Coxiella burnetii replication dependent on tissue,” Infection and Immunity, vol. 84, no. 6, pp. 1815–1825, 2016. View at Publisher · View at Google Scholar · View at Scopus
  168. E. J. van Schaik, C. Chen, K. Mertens, M. M. Weber, and J. E. Samuel, “Molecular pathogenesis of the obligate intracellular bacterium Coxiella burnetii,” Nature Reviews. Microbiology, vol. 11, no. 8, pp. 561–573, 2013. View at Publisher · View at Google Scholar · View at Scopus
  169. M. B. Ka, S. Mezouar, A. Ben Amara et al., “Coxiella burnetii induces inflammatory interferon-like signature in plasmacytoid dendritic cells: a new feature of immune response in Q fever,” Frontiers in Cellular and Infection Microbiology, vol. 6, p. 70, 2016. View at Publisher · View at Google Scholar
  170. P. S. Redford, K. D. Mayer-Barber, F. W. McNab et al., “Influenza a virus impairs control of Mycobacterium tuberculosis coinfection through a type I interferon receptor-dependent pathway,” The Journal of Infectious Diseases, vol. 209, no. 2, pp. 270–274, 2014. View at Publisher · View at Google Scholar · View at Scopus
  171. G. J. Kersh, “Antimicrobial therapies for Q fever,” Expert Review of Anti-Infective Therapy, vol. 11, no. 11, pp. 1207–1214, 2013. View at Publisher · View at Google Scholar · View at Scopus