1887

Abstract

Orf virus (ORFV) is the type species of the genus of the family. Genetic and functional studies have revealed ORFV has multiple immunomodulatory genes that manipulate innate immune responses, during the early stage of infection. is a novel gene of ORFV with hitherto unknown function. Characterization of an deletion mutant showed that it replicated in primary lamb testis cells with reduced levels compared to the wild-type and produced a smaller plaque phenotype. was shown to be expressed prior to DNA replication. The potential function of was investigated by gene-expression microarray analysis in HeLa cells infected with wild-type ORFV or the ORF116 deletion mutant. The analysis of differential cellular gene expression revealed a number of interferon-stimulated genes (ISGs) differentially expressed at either 4 or 6 h post infection. showed the greatest differential expression (4.17-fold) between wild-type and knockout virus. Other ISGs that were upregulated in the knockout included and and in addition the inflammatory cytokine . These findings were validated by infecting HeLa cells with an ORF116 revertant recombinant virus and analysis of transcript expression by quantitative real time-PCR (qRT-PCR). These observations suggested a role for the ORFV gene in modulating the IFN response and inflammatory cytokines. This study represents the first functional analysis of .

Funding
This study was supported by the:
  • health research council of new zealand (Award Grant 13/774.)
    • Principle Award Recipient: AndrewA Mercer
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/content/journal/jgv/10.1099/jgv.0.001695
2021-12-10
2024-03-28
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References

  1. Fleming SB, Mercer AA. Genus Parapoxvirus. In Mercer AA, Schmidt A, Schmidt O. eds Poxviruses Basel: Birkhäuser Basel; 2007 p 127
    [Google Scholar]
  2. Mercer A, Fleming S. Parapoxvirus. In Tidona C, Darai G. eds The Springer Index of Viruses New York, NY: Springer New York; 2011 p 1495
    [Google Scholar]
  3. Haig DM, Thomson J, McInnes C, McCaughan C, Imlach W et al. Orf virus immuno-modulation and the host immune response. Vet Immunol Immunopathol 2002; 87:395–399 [PubMed]
    [Google Scholar]
  4. Haig DM, McInnes CJ. Immunity and counter-immunity during infection with the parapoxvirus orf virus. Virus Res 2002; 88:3–16 [View Article] [PubMed]
    [Google Scholar]
  5. Lazear HM, Schoggins JW, Diamond MS. Shared and distinct functions of type I and type III interferons. Immunity 2019; 50:907–923 [View Article] [PubMed]
    [Google Scholar]
  6. Takeuchi O, Akira S. Pattern recognition receptors and inflammation. Cell 2010; 140:805–820 [View Article] [PubMed]
    [Google Scholar]
  7. Takaoka A, Wang Z, Choi MK, Yanai H, Negishi H et al. DAI (DLM-1/ZBP1) is a cytosolic DNA sensor and an activator of innate immune response. Nature 2007; 448:501–505 [View Article] [PubMed]
    [Google Scholar]
  8. MacMicking JD. Interferon-inducible effector mechanisms in cell-autonomous immunity. Nat Rev Immunol 2012; 12:367–382 [View Article] [PubMed]
    [Google Scholar]
  9. Schoggins JW, Wilson SJ, Panis M, Murphy MY, Jones CT et al. A diverse range of gene products are effectors of the type I interferon antiviral response. Nature 2011; 472:481–485 [View Article] [PubMed]
    [Google Scholar]
  10. Schoggins JW, Rice CM. Interferon-stimulated genes and their antiviral effector functions. Curr Opin Virol 2011; 1:519–525 [View Article] [PubMed]
    [Google Scholar]
  11. Schneider WM, Chevillotte MD, Rice CM. Interferon-stimulated genes: a complex web of host defenses. Annu Rev Immunol 2014; 32:513–545 [View Article] [PubMed]
    [Google Scholar]
  12. Wathelet MG, Berr PM, Huez GA. Regulation of gene expression by cytokines and virus in human cells lacking the type-I interferon locus. Eur J Biochem 1992; 206:901–910 [View Article] [PubMed]
    [Google Scholar]
  13. Hertzog P, Forster S, Samarajiwa S. Systems biology of interferon responses. J Interferon Cytokine Res 2011; 31:5–11 [View Article]
    [Google Scholar]
  14. Schoggins JW. Interferon-stimulated genes: what do they all do?. Annu Rev Virol 2019; 6:567–584 [View Article] [PubMed]
    [Google Scholar]
  15. Pindel A, Sadler A. The role of protein kinase R in the interferon response. J Interferon Cytokine Res 2011; 31:59–70 [View Article]
    [Google Scholar]
  16. Kristiansen H, Gad HH, Eskildsen-Larsen S, Despres P, Hartmann R. The oligoadenylate synthetase family: an ancient protein family with multiple antiviral activities. J Interferon Cytokine Res 2011; 31:41–47 [View Article]
    [Google Scholar]
  17. Chakrabarti A, Jha BK, Silverman RH. New Insights into the Role of RNase L in Innate Immunity. J Interferon Cytokine Res 2011; 31:49–57 [View Article]
    [Google Scholar]
  18. Spence JS, He R, Hoffmann H-H, Das T, Thinon E et al. IFITM3 directly engages and shuttles incoming virus particles to lysosomes. Nat Chem Biol 2019; 15:259–268 [View Article] [PubMed]
    [Google Scholar]
  19. Haller O, Staeheli P, Schwemmle M, Kochs G. Mx GTPases: dynamin-like antiviral machines of innate immunity. Trends Microbiol 2015; 23:154–163 [View Article] [PubMed]
    [Google Scholar]
  20. Tanaka M, Shimbo T, Kikuchi Y, Matsuda M, Kaneda Y. Sterile alpha motif containing domain 9 is involved in death signaling of malignant glioma treated with inactivated Sendai virus particle (HVJ-E) or type I interferon. Int J Cancer 2010; 126:1982–1991 [View Article] [PubMed]
    [Google Scholar]
  21. Lemos de Matos A, Liu J, McFadden G, Esteves PJ. Evolution and divergence of the mammalian SAMD9/SAMD9L gene family. BMC Evol Biol 2013; 13:121 [View Article] [PubMed]
    [Google Scholar]
  22. Liu J, McFadden G. SAMD9 is an innate antiviral host factor with stress response properties that can be antagonized by poxviruses. J Virol 2015; 89:1925–1931 [View Article] [PubMed]
    [Google Scholar]
  23. Meng X, Jiang C, Arsenio J, Dick K, Cao J et al. Vaccinia Virus K1L and C7L inhibit antiviral activities induced by type I interferons. J Virol 2009; 83:10627–10636 [View Article] [PubMed]
    [Google Scholar]
  24. Meng X, Schoggins J, Rose L, Cao J, Ploss A et al. C7L family of poxvirus host range genes inhibits antiviral activities induced by type i interferons and interferon regulatory factor 1. J Virol 2012; 86:4538–4547 [View Article] [PubMed]
    [Google Scholar]
  25. Smith GL, Talbot-Cooper C, Lu Y. Chapter fourteen - how does vaccinia virus interfere with interferon?. In Kielian M, Mettenleiter TC, Roossinck MJ. eds Advances in Virus Research 100: Academic Press; 2018 p 355
    [Google Scholar]
  26. Valentine R, Smith GL. hibition of the RNA polymerase III-mediated dsDNA-sensing pathway of innate immunity by vaccinia virus protein E3. J Gen Virol 2010; 91:2221–2229 [View Article] [PubMed]
    [Google Scholar]
  27. Marq J-B, Hausmann S, Luban J, Kolakofsky D, Garcin D. The double-stranded RNA binding domain of the vaccinia virus E3L protein inhibits both RNA- and DNA-induced activation of interferon beta. J Biol Chem 2009; 284:25471–25478 [View Article] [PubMed]
    [Google Scholar]
  28. Chang HW, Watson JC, Jacobs BL. The E3L gene of vaccinia virus encodes an inhibitor of the interferon-induced, double-stranded RNA-dependent protein kinase. Proc Natl Acad Sci U S A 1992; 89:4825–4829 [View Article] [PubMed]
    [Google Scholar]
  29. Langland JO, Jacobs BL. The role of the PKR-inhibitory genes, E3L and K3L, in determining vaccinia virus host range. Virology 2002; 299:133–141 [View Article] [PubMed]
    [Google Scholar]
  30. Peters NE, Ferguson BJ, Mazzon M, Fahy AS, Krysztofinska E et al. A Mechanism for the Inhibition of DNA-PK-Mediated DNA Sensing by a Virus. PLoS Pathog 2013; 9:e1003649 [View Article]
    [Google Scholar]
  31. Fahy AS, Clark RH, Glyde EF, Smith GL. Vaccinia virus protein C16 acts intracellularly to modulate the host response and promote virulence. J Gen Virol 2008; 89:2377–2387 [View Article] [PubMed]
    [Google Scholar]
  32. Unterholzner L, Sumner RP, Baran M, Ren H, Mansur DS et al. Vaccinia virus protein C6 is a virulence factor that binds TBK-1 adaptor proteins and inhibits activation of IRF3 and IRF7. PLoS Pathog 2011; 7:e1002247 [View Article] [PubMed]
    [Google Scholar]
  33. Schröder M, Baran M, Bowie AG. Viral targeting of DEAD box protein 3 reveals its role in TBK1/IKKepsilon-mediated IRF activation. EMBO J 2008; 27:2147–2157 [View Article] [PubMed]
    [Google Scholar]
  34. Soulat D, Bürckstümmer T, Westermayer S, Goncalves A, Bauch A et al. The DEAD-box helicase DDX3X is a critical component of the TANK-binding kinase 1-dependent innate immune response. EMBO J 2008; 27:2135–2146 [View Article] [PubMed]
    [Google Scholar]
  35. Oda S-I, Schröder M, Khan AR. Structural basis for targeting of human RNA helicase DDX3 by poxvirus protein K7. Structure 2009; 17:1528–1537 [View Article] [PubMed]
    [Google Scholar]
  36. Ferguson BJ, Benfield CTO, Ren H, Lee VH, Frazer GL et al. Vaccinia virus protein N2 is a nuclear IRF3 inhibitor that promotes virulence. J Gen Virol 2013; 94:2070–2081 [View Article] [PubMed]
    [Google Scholar]
  37. Fleming SB. Viral inhibition of the IFN-Induced JAK/STAT signalling pathway: development of live attenuated vaccines by mutation of viral-encoded IFN-antagonists. Vaccines (Basel) 2016; 4:23 [View Article] [PubMed]
    [Google Scholar]
  38. Najarro P, Traktman P, Lewis JA. Vaccinia virus blocks gamma interferon signal transduction: viral VH1 phosphatase reverses stat1 activation. J Virol 2001; 75:3185–3196 [View Article] [PubMed]
    [Google Scholar]
  39. Stuart JH, Sumner RP, Lu Y, Snowden JS, Smith GL. Vaccinia Virus Protein C6 Inhibits Type I IFN Signalling in the Nucleus and Binds to the Transactivation Domain of STAT2. PLoS Pathog 2016; 12:12e1005955 [View Article] [PubMed]
    [Google Scholar]
  40. Alcamí A, Smith GL. A soluble receptor for interleukin-1 beta encoded by vaccinia virus: a novel mechanism of virus modulation of the host response to infection. Cell 1992; 71:153–167 [View Article] [PubMed]
    [Google Scholar]
  41. Alcamí A, Smith GL. Vaccinia, cowpox, and camelpox viruses encode soluble gamma interferon receptors with novel broad species specificity. J Virol 1995; 69:4633–4639 [View Article] [PubMed]
    [Google Scholar]
  42. Colamonici OR, Domanski P, Sweitzer SM, Larner A, Buller RML. Vaccinia virus B18R gene encodes a type I interferon-binding protein that blocks interferon alpha transmembrane signaling. J Biol Chem 1995; 270:15974–15978 [View Article] [PubMed]
    [Google Scholar]
  43. Alcamí A, Symons JA, Smith GL. The Vaccinia Virus Soluble Alpha/Beta Interferon (IFN) receptor binds to the cell surface and protects cells from the antiviral effects of IFN. J Virol 2000; 74:11230–11239 [View Article] [PubMed]
    [Google Scholar]
  44. Symons JA, Alcamí A, Smith GL. Vaccinia virus encodes a soluble type I interferon receptor of novel structure and broad species specificity. Cell 1995; 81:551–560 [View Article] [PubMed]
    [Google Scholar]
  45. Fleming SB, McCaughan CA, Andrews AE, Nash AD, Mercer AA. A homolog of interleukin-10 is encoded by the poxvirus orf virus. J Virol 1997; 71:4857–4861 [View Article] [PubMed]
    [Google Scholar]
  46. Savory LJ, Stacker SA, Fleming SB, Niven BE, Mercer AA. Viral vascular endothelial growth factor plays a critical role in orf virus infection. J Virol 2000; 74:10699–10706 [View Article] [PubMed]
    [Google Scholar]
  47. Fleming SB, McCaughan C, Lateef Z, Dunn A, Wise LM et al. Deletion of the chemokine binding protein gene from the parapoxvirus orf virus reduces virulence and pathogenesis in sheep. Front Microbiol 2017; 8:46 [View Article] [PubMed]
    [Google Scholar]
  48. Seet BT, McCaughan CA, Handel TM, Mercer A, Brunetti C et al. Analysis of an orf virus chemokine-binding protein: Shifting ligand specificities among a family of poxvirus viroceptors. Proc Natl Acad Sci U S A 2003; 100:15137–15142 [View Article] [PubMed]
    [Google Scholar]
  49. Smith CA, Smith TD, Smolak PJ, Friend D, Hagen H et al. Poxvirus genomes encode a secreted, soluble protein that preferentially inhibits beta chemokine activity yet lacks sequence homology to known chemokine receptors. Virology 1997; 236:316–327 [View Article] [PubMed]
    [Google Scholar]
  50. Haig D, McInnes C, Deane D, Lear A, Myatt N et al. Cytokines and their inhibitors in orf virus infection. Vet Immunol Immunopathol 1996; 54:261–267 [View Article] [PubMed]
    [Google Scholar]
  51. Franklin E, Khan AR. Poxvirus antagonism of innate immunity by Bcl-2 fold proteins. J Struct Biol 2013; 181:1–10 [View Article] [PubMed]
    [Google Scholar]
  52. Westphal D, Ledgerwood EC, Tyndall JDA, Hibma MH, Ueda N et al. The orf virus inhibitor of apoptosis functions in a Bcl-2-like manner, binding and neutralizing a set of BH3-only proteins and active Bax. Apoptosis 2009; 14:1317–1330 [View Article]
    [Google Scholar]
  53. Robinson AJ, Ellis G, Balassu T. The genome of orf virus: Restriction endonuclease analysis of viral DNA isolated from lesions of orf in sheep. Arch Virol 1982; 71:43–55 [View Article] [PubMed]
    [Google Scholar]
  54. Balassu TC, Robinson AJ. Orf virus replication in bovine testis cells: kinetics of viral DNA, polypeptide, and infectious virus production and analysis of virion polypeptides. Arch Virol 1987; 97:267–281 [View Article] [PubMed]
    [Google Scholar]
  55. Fleming SB, Anderson IE, Thomson J, Deane DL, McInnes CJ et al. fection with recombinant orf viruses demonstrates that the viral interleukin-10 is a virulence factor. J Gen Virol 2007; 88:1922–1927 [View Article] [PubMed]
    [Google Scholar]
  56. Rosel JL, Earl PL, Weir JP, Moss B. Conserved TAAATG sequence at the transcriptional and translational initiation sites of vaccinia virus late genes deduced by structural and functional analysis of the HindIII H genome fragment. J Virol 1986; 60:436–449 [View Article] [PubMed]
    [Google Scholar]
  57. Mercer AA, Ueda N, Friederichs S-M, Hofmann K, Fraser KM et al. Comparative analysis of genome sequences of three isolates of Orf virus reveals unexpected sequence variation. Virus Res 2006; 116:146–158 [View Article] [PubMed]
    [Google Scholar]
  58. Fleming SB, Blok J, Fraser KM, Mercer AA, Robinson AJ. Conservation of gene structure and arrangement between vaccinia virus and orf virus. Virology 1993; 195:175–184 [View Article] [PubMed]
    [Google Scholar]
  59. Pfaffl MW. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res 2001; 29:e45 [View Article] [PubMed]
    [Google Scholar]
  60. Evans MJ, Hartman SL, Wolff DW, Rollins SA, Squinto SP. Rapid expression of an anti-human C5 chimeric Fab utilizing a vector that replicates in COS and 293 cells. J Immunol Methods 1995; 184:123–138 [View Article] [PubMed]
    [Google Scholar]
  61. Huang DW, Sherman BT, Lempicki RA. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat Protoc 2009; 4:44–57 [View Article] [PubMed]
    [Google Scholar]
  62. Huang DW, Sherman BT, Lempicki RA. Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists. Nucleic Acids Res 2009; 37:1–13 [View Article] [PubMed]
    [Google Scholar]
  63. Delhon G, Tulman ER, Afonso CL, Lu Z, de la Concha-Bermejillo A et al. Genomes of the Parapoxviruses Orf Virus and Bovine Papular Stomatitis Virus. J Virol 2004; 78:168–177 [View Article] [PubMed]
    [Google Scholar]
  64. Kosugi S, Hasebe M, Matsumura N, Takashima H, Miyamoto-Sato E et al. Six Classes of Nuclear Localization Signals Specific to Different Binding Grooves of Importin α. Journal of Biological Chemistry 2009; 284:478–485 [View Article]
    [Google Scholar]
  65. Bolender N, Sickmann A, Wagner R, Meisinger C, Pfanner N. Multiple pathways for sorting mitochondrial precursor proteins. EMBO Rep 2008; 9:42–49 [View Article] [PubMed]
    [Google Scholar]
  66. Brix J, Dietmeier K, Pfanner N. Differential recognition of preproteins by the purified cytosolic domains of the mitochondrial import receptors Tom20, Tom22, and Tom70. J Biol Chem 1997; 272:20730–20735 [View Article] [PubMed]
    [Google Scholar]
  67. Kalderon D, Richardson WD, Markham AF, Smith AE. Sequence requirements for nuclear location of simian virus 40 large-T antigen. Nature 1984; 311:33–38 [View Article] [PubMed]
    [Google Scholar]
  68. Kalderon D, Roberts BL, Richardson WD, Smith AE. A short amino acid sequence able to specify nuclear location. Cell 1984; 39:499–509 [View Article] [PubMed]
    [Google Scholar]
  69. Riad S, Xiang Y, AlDaif B, Mercer AA, Fleming SB. Rescue of a Vaccinia Virus Mutant Lacking IFN Resistance Genes K1L and C7L by the Parapoxvirus Orf Virus. Front Microbiol 2020; 11:1797 [View Article] [PubMed]
    [Google Scholar]
  70. Diel DG, Delhon G, Luo S, Flores EF, Rock DL. A novel inhibitor of the NF-{kappa}B signaling pathway encoded by the parapoxvirus orf virus. J Virol 2010; 84:3962–3973 [View Article] [PubMed]
    [Google Scholar]
  71. Ablasser A, Bauernfeind F, Hartmann G, Latz E, Fitzgerald KA et al. RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate. Nat Immunol 2009; 10:1065–1072 [View Article] [PubMed]
    [Google Scholar]
  72. Chiu Y-H, Macmillan JB, Chen ZJ. RNA Polymerase III Detects Cytosolic DNA and Induces Type I Interferons through the RIG-I Pathway. Cell 2009; 138:576–591 [View Article] [PubMed]
    [Google Scholar]
  73. Fleming SB, Fraser KM, Mercer AA, Robinson AJ. Vaccinia virus-like early transcriptional control sequences flank an early gene in orf virus. Gene 1991; 97:207–212 [View Article] [PubMed]
    [Google Scholar]
  74. Maniatis T, Falvo JV, Kim TH, Kim TK, Lin CH et al. Structure and function of the interferon-beta enhanceosome. Cold Spring Harb Symp Quant Biol 1998; 63:609–620 [View Article] [PubMed]
    [Google Scholar]
  75. Darnell JE Jr, Kerr IM, Stark GR. Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science 1994; 264:1415–1421 [View Article] [PubMed]
    [Google Scholar]
  76. Tanaka N, Kawakami T, Taniguchi T. Recognition DNA sequences of interferon regulatory factor 1 (IRF-1) and IRF-2, regulators of cell growth and the interferon system. Mol Cell Biol 1993; 13:4531–4538 [View Article] [PubMed]
    [Google Scholar]
  77. Guerra S, Nájera JL, González JM, López-Fernández LA, Climent N et al. Distinct Gene Expression Profiling after Infection of Immature Human Monocyte-Derived Dendritic Cells by the Attenuated Poxvirus Vectors MVA and NYVAC. J Virol 2007; 81:8707–8721 [View Article] [PubMed]
    [Google Scholar]
  78. Tartaglia J, Perkus ME, Taylor J, Norton EK, Audonnet JC et al. NYVAC: a highly attenuated strain of vaccinia virus. Virology 1992; 188:217–232 [View Article] [PubMed]
    [Google Scholar]
  79. Chang YE, Laimins LA. Microarray Analysis Identifies Interferon-Inducible Genes and Stat-1 as Major Transcriptional Targets of Human Papillomavirus Type 31. J Virol 2000; 74:4174–4182 [View Article] [PubMed]
    [Google Scholar]
  80. Kaczkowski B, Rossing M, Andersen DK, Dreher A, Morevati M et al. tegrative analyses reveal novel strategies in HPV11,-16 and -45 early infection. Sci Rep 2012; 2:515 [View Article] [PubMed]
    [Google Scholar]
  81. Harman AN, Lai J, Turville S, Samarajiwa S, Gray L et al. HIV infection of dendritic cells subverts the IFN induction pathway via IRF-1 and inhibits type 1 IFN production. Blood 2011; 118:298–308 [View Article] [PubMed]
    [Google Scholar]
  82. Sadler AJ, Williams BRG. terferon-inducible antiviral effectors. Nat Rev Immunol 2008; 8:559–568 [View Article] [PubMed]
    [Google Scholar]
  83. Schoggins JW. Recent advances in antiviral interferon-stimulated gene biology. F1000Res 2018; 7:309 [View Article] [PubMed]
    [Google Scholar]
  84. Yoneyama M, Kikuchi M, Natsukawa T, Shinobu N, Imaizumi T et al. The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses. Nat Immunol 2004; 5:730–737 [View Article] [PubMed]
    [Google Scholar]
  85. Wang F, Gao X, Barrett JW, Shao Q, Bartee E et al. RIG-I Mediates the Co-Induction of Tumor Necrosis Factor and Type I Interferon Elicited by Myxoma Virus in Primary Human Macrophages. PLoS Pathog 2008; 4:e1000099 [View Article] [PubMed]
    [Google Scholar]
  86. Cheng G, Zhong J, Chung J, Chisari FV. Double-stranded DNA and double-stranded RNA induce a common antiviral signaling pathway in human cells. Proceedings of the National Academy of Sciences 2007; 104:9035–9040 [View Article]
    [Google Scholar]
  87. Gitlin L, Barchet W, Gilfillan S, Cella M, Beutler B et al. Essential role of mda-5 in type I IFN responses to polyriboinosinic:polyribocytidylic acid and encephalomyocarditis picornavirus. Proc Natl Acad Sci U S A 2006; 103:8459–8464 [View Article] [PubMed]
    [Google Scholar]
  88. Delaloye J, Roger T, Steiner-Tardivel Q-G, Le Roy D, Knaup Reymond M et al. nate Immune Sensing of Modified Vaccinia Virus Ankara (MVA) Is Mediated by TLR2-TLR6, MDA-5 and the NALP3 Inflammasome. PLoS Pathog 2009; 5:e1000480 [View Article] [PubMed]
    [Google Scholar]
  89. Hartmann R, Olsen HS, Widder S, Jorgensen R, Justesen J. p59OASL, a 2’-5’ oligoadenylate synthetase like protein: a novel human gene related to the 2’-5’ oligoadenylate synthetase family. Nucleic Acids Res 1998; 26:4121–4128 [View Article] [PubMed]
    [Google Scholar]
  90. Marques J, Anwar J, Eskildsen-Larsen S, Rebouillat D, Paludan SR et al. The p59 oligoadenylate synthetase-like protein possesses antiviral activity that requires the C-terminal ubiquitin-like domain. J Gen Virol 2008; 89:2767–2772 [View Article] [PubMed]
    [Google Scholar]
  91. Melchjorsen J, Kristiansen H, Christiansen R, Rintahaka J, Matikainen S et al. Differential Regulation of the OASL and OAS1 Genes in Response to Viral Infections. Journal of Interferon & Cytokine Research 2009; 29:199–208 [View Article]
    [Google Scholar]
  92. Zhu J, Zhang Y, Ghosh A, Cuevas RA, Forero A et al. Antiviral Activity of Human OASL Protein Is Mediated by Enhancing Signaling of the RIG-I RNA Sensor. Immunity 2014; 40:936–948 [View Article] [PubMed]
    [Google Scholar]
  93. Fensterl V, Sen GC. The ISG56/IFIT1 Gene Family. Journal of Interferon & Cytokine Research 2011; 31:71–78 [View Article]
    [Google Scholar]
  94. Liu R, Moss B. Vaccinia Virus C9 Ankyrin Repeat/F-Box Protein Is a Newly Identified Antagonist of the Type I Interferon-Induced Antiviral State. J Virol 2018; 92:e00053-18 [View Article] [PubMed]
    [Google Scholar]
  95. Liu R, Olano LR, Mirzakhanyan Y, Gershon PD, Moss B. Vaccinia Virus Ankyrin-Repeat/F-Box Protein Targets Interferon-Induced IFITs for Proteasomal Degradation. Cell Rep 2019; 29:816–828 [View Article] [PubMed]
    [Google Scholar]
  96. Gongora C, Degols G, Espert L, Hua TD, Mechti N. A unique ISRE, in the TATA-less human Isg20 promoter, confers IRF-1-mediated responsiveness to both interferon type I and type II. Nucleic Acids Res 2000; 28:2333–2341 [View Article] [PubMed]
    [Google Scholar]
  97. Espert L, Rey C, Gonzalez L, Degols G, Chelbi-Alix MK et al. The exonuclease ISG20 is directly induced by synthetic dsRNA via NF-kappaB and IRF1 activation. Oncogene 2004; 23:4636–4640 [View Article] [PubMed]
    [Google Scholar]
  98. Espert L, Degols G, Lin Y-L, Vincent T, Benkirane M et al. terferon-induced exonuclease ISG20 exhibits an antiviral activity against human immunodeficiency virus type 1. J Gen Virol 2005; 86:2221–2229 [View Article] [PubMed]
    [Google Scholar]
  99. Weiss CM, Trobaugh DW, Sun C, Lucas TM, Diamond MS et al. The Interferon-Induced Exonuclease ISG20 Exerts Antiviral Activity through Upregulation of Type I Interferon Response Proteins. mSphere 2018; 3:e00209-18 [View Article] [PubMed]
    [Google Scholar]
  100. Miyashita M, Oshiumi H, Matsumoto M, Seya T. DDX60, a DEXD/H Box Helicase, Is a Novel Antiviral Factor Promoting RIG-I-Like Receptor-Mediated Signaling. Mol Cell Biol 2011; 31:3802–3819 [View Article] [PubMed]
    [Google Scholar]
  101. Fernandes-Alnemri T, Yu J-W, Datta P, Wu J, Alnemri ES. AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA. Nature 2009; 458:509–513 [View Article] [PubMed]
    [Google Scholar]
  102. Hornung V, Ablasser A, Charrel-Dennis M, Bauernfeind F, Horvath G et al. AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC. Nature 2009; 458:514–518 [View Article] [PubMed]
    [Google Scholar]
  103. Rathinam VAK, Jiang Z, Waggoner SN, Sharma S, Cole LE et al. The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses. Nat Immunol 2010; 11:395–402 [View Article] [PubMed]
    [Google Scholar]
  104. Unterholzner L, Keating SE, Baran M, Horan KA, Jensen SB et al. IFI16 is an innate immune sensor for intracellular DNA. Nat Immunol 2010; 11:997–1004 [View Article] [PubMed]
    [Google Scholar]
  105. Carlton-Smith C, Elliott RM. Viperin, MTAP44, and Protein Kinase R Contribute to the interferon-induced inhibition of bunyamwera orthobunyavirus replication. J Virol 2012; 86:11548–11557 [View Article] [PubMed]
    [Google Scholar]
  106. Pasieka TJ, Baas T, Carter VS, Proll SC, Katze MG et al. Functional genomic analysis of herpes simplex virus type 1 counteraction of the host innate response. J Virol 2006; 80:7600–7612 [View Article] [PubMed]
    [Google Scholar]
  107. Busse DC, Habgood-Coote D, Clare S, Brandt C, Bassano I et al. Interferon-induced protein 44 and interferon-induced protein 44-Like restrict replication of respiratory syncytial virus. J Virol 2020; 94: [View Article]
    [Google Scholar]
  108. Hallen LC, Burki Y, Ebeling M, Broger C, Siegrist F et al. Antiproliferative activity of the human IFN- α -inducible protein IFI44. J Interferon Cytokine Res 2007; 27:675–680 [View Article]
    [Google Scholar]
  109. Honda Y, Kondo J, Maeda T, Yoshiyama Y, Yamada E et al. Isolation and purification of a non-A, non-B hepatitis-associated microtubular aggregates protein. J Gen Virol 1990; 71 (Pt 9):1999–2004 [View Article] [PubMed]
    [Google Scholar]
  110. Kitamura A, Takahashi K, Okajima A, Kitamura N. Induction of the human gene for p44, a hepatitis-C-associated microtubular aggregate protein, by interferon-alpha/beta. Eur J Biochem 1994; 224:877–883 [View Article] [PubMed]
    [Google Scholar]
  111. Moens B, Pannecouque C, López G, Talledo M, Gotuzzo E et al. Simultaneous RNA quantification of human and retroviral genomes reveals intact interferon signaling in HTLV-1-infected CD4+ T cell lines. Virol J 2012; 9:171 [View Article] [PubMed]
    [Google Scholar]
  112. Bourquain D, Nitsche A. Cowpox virus but not Vaccinia virus induces secretion of CXCL1, IL-8 and IL-6 and chemotaxis of monocytes in vitro. Virus Res 2013; 171:161–167 [View Article] [PubMed]
    [Google Scholar]
  113. Czerkies M, Korwek Z, Prus W, Kochańczyk M, Jaruszewicz-Błońska J et al. Cell fate in antiviral response arises in the crosstalk of IRF, NF-κB and JAK/STAT pathways. Nat Commun 2018; 9:493 [View Article] [PubMed]
    [Google Scholar]
  114. Freaney JE, Kim R, Mandhana R, Horvath CM. Extensive cooperation of immune master regulators IRF3 and NFκB in RNA Pol II recruitment and pause release in human innate antiviral transcription. Cell Rep 2013; 4:959–973 [View Article] [PubMed]
    [Google Scholar]
  115. Iwanaszko M, Kimmel M. NF-κB and IRF pathways: cross-regulation on target genes promoter level. BMC Genomics 2015; 16:307 [View Article] [PubMed]
    [Google Scholar]
  116. Oeckinghaus A, Hayden MS, Ghosh S. Crosstalk in NF-κB signaling pathways. Nat Immunol 2011; 12:695–708 [View Article] [PubMed]
    [Google Scholar]
  117. Rubio D, Xu R-H, Remakus S, Krouse TE, Truckenmiller ME et al. Crosstalk between the type 1 interferon and nuclear factor kappa B pathways confers resistance to a lethal virus infection. Cell Host & Microbe 2013; 13:701–710 [View Article]
    [Google Scholar]
  118. Yum S, Li M, Fang Y, Chen ZJ. TBK1 recruitment to STING activates both IRF3 and NF-κB that mediate immune defense against tumors and viral infections. Proc Natl Acad Sci USA 2021; 118:e2100225118 [View Article]
    [Google Scholar]
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