Adenosine Deaminase Acting on RNA 1 Associates with Orf Virus OV20.0 and Enhances Viral Replication
Orf virus (ORFV) infects sheep and goats and is also an important zoonotic pathogen. The viral protein OV20.0 has been shown to suppress innate immunity by targeting the double-stranded RNA (dsRNA)-activated protein kinase (PKR) by multiple mechanisms. These mechanisms include a direct interaction w...
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| Abstract | Orf virus (ORFV) infects sheep and goats and is also an important zoonotic pathogen. The viral protein OV20.0 has been shown to suppress innate immunity by targeting the double-stranded RNA (dsRNA)-activated protein kinase (PKR) by multiple mechanisms. These mechanisms include a direct interaction with PKR and binding with two PKR activators, dsRNA and the cellular PKR activator (PACT), which ultimately leads to the inhibition of PKR activation. In the present study, we identified a novel association between OV20.0 and adenosine deaminase acting on RNA 1 (ADAR1). OV20.0 bound directly to the dsRNA binding domains (RBDs) of ADAR1 in the absence of dsRNA. Additionally, OV20.0 preferentially interacted with RBD1 of ADAR1, which was essential for its dsRNA binding ability and for the homodimerization that is critical for intact adenosine (A)-to-inosine (I) editing activity. Finally, the association with OV20.0 suppressed the A-to-I editing ability of ADAR1, while ADAR1 played a proviral role during ORFV infection by inhibiting PKR phosphorylation. These observations revealed a new strategy used by OV20.0 to evade antiviral responses via PKR. |
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| AbstractList | Orf virus (ORFV) infects sheep and goats and is also an important zoonotic pathogen. The viral protein OV20.0 has been shown to suppress innate immunity by targeting the double-stranded RNA (dsRNA)-activated protein kinase (PKR) by multiple mechanisms. These mechanisms include a direct interaction with PKR and binding with two PKR activators, dsRNA and the cellular PKR activator (PACT), which ultimately leads to the inhibition of PKR activation. In the present study, we identified a novel association between OV20.0 and adenosine deaminase acting on RNA 1 (ADAR1). OV20.0 bound directly to the dsRNA binding domains (RBDs) of ADAR1 in the absence of dsRNA. Additionally, OV20.0 preferentially interacted with RBD1 of ADAR1, which was essential for its dsRNA binding ability and for the homodimerization that is critical for intact adenosine (A)-to-inosine (I) editing activity. Finally, the association with OV20.0 suppressed the A-to-I editing ability of ADAR1, while ADAR1 played a proviral role during ORFV infection by inhibiting PKR phosphorylation. These observations revealed a new strategy used by OV20.0 to evade antiviral responses via PKR. Orf virus (ORFV) infects sheep and goats and is also an important zoonotic pathogen. The viral protein OV20.0 has been shown to suppress innate immunity by targeting the double-stranded RNA (dsRNA)-activated protein kinase (PKR) by multiple mechanisms. These mechanisms include a direct interaction with PKR and binding with two PKR activators, dsRNA and the cellular PKR activator (PACT), which ultimately leads to the inhibition of PKR activation. In the present study, we identified a novel association between OV20.0 and adenosine deaminase acting on RNA 1 (ADAR1). OV20.0 bound directly to the dsRNA binding domains (RBDs) of ADAR1 in the absence of dsRNA. Additionally, OV20.0 preferentially interacted with RBD1 of ADAR1, which was essential for its dsRNA binding ability and for the homodimerization that is critical for intact adenosine (A)-to-inosine (I) editing activity. Finally, the association with OV20.0 suppressed the A-to-I editing ability of ADAR1, while ADAR1 played a proviral role during ORFV infection by inhibiting PKR phosphorylation. These observations revealed a new strategy used by OV20.0 to evade antiviral responses via PKR. Viruses evolve specific strategies to counteract host innate immunity. ORFV, an important zoonotic pathogen, encodes OV20.0 to suppress PKR activation via multiple mechanisms, including interactions with PKR and two PKR activators. In this study, we demonstrated that OV20.0 interacts with ADAR1, a cellular enzyme responsible for converting adenosine (A) to inosine (I) in RNA. The RNA binding domains, but not the catalytic domain, of ADAR1 are required for this interaction. The OV20.0-ADAR1 association affects the functions of both proteins; OV20.0 suppressed the A-to-I editing of ADAR1, while ADAR1 elevated OV20.0 expression. The proviral role of ADAR1 is likely due to the inhibition of PKR phosphorylation. As RNA editing by ADAR1 contributes to the stability of the genetic code and the structure of RNA, these observations suggest that in addition to serving as a PKR inhibitor, OV20.0 might modulate ADAR1-dependent gene expression to combat antiviral responses or achieve efficient viral infection. |
| Author | Fong-Yuan, Lin Yamada, Yumiko Chih-Ying Kuan Jing-Yu, Tseng Hao-Ping, Liu Wei-Li, Hsu Guan-Ru Liao Yeu-Yang Tseng |
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| References | Barraud, Banerjee, Mohamed, Jantsch, Allain (459149v1.34) 2014; 111 Cachat, Alais, Chevalier, Journo, Fusil, Dutartre, Boniface, Ko, Gessain, Cosset, Suspene, Vartanian, Mahieux (459149v1.40) 2014; 11 George, Samuel (459149v1.13) 1999; 229 Yang, Nie, Zhao, Su, Pypaert, Su, Rabinovici (459149v1.14) 2003; 278 Gallo, Keegan, Ring, O’Connell (459149v1.29) 2003; 22 Herbert, Alfken, Kim, Mian, Nishikura, Rich (459149v1.12) 1997; 94 Haig, McInnes, Thomson, Wood, Bunyan, Mercer (459149v1.3) 1998; 93 Nie, Zhao, Su, Yang (459149v1.30) 2004; 279 Liu, Samuel (459149v1.38) 1996; 70 Wong, Sato, Lazinski (459149v1.28) 2001; 7 Nie, Zhao, Su, Yang (459149v1.32) 2004; 279 Scott, Troshin, Barton (459149v1.33) 2011; 12 Kumar, Haque, Lacoste, Hiscott, Williams (459149v1.24) 1994; 91 Harashima, Pfeifer, Elsby, Konno, Barber (459149v1.5) 2009; 48 Phuphuakrat, Kraiwong, Boonarkart, Lauhakirti, Lee, Auewarakul (459149v1.18) 2008; 82 Sallusto, Baggiolini (459149v1.1) 2008; 9 Clerzius, Gelinas, Daher, Bonnet, Meurs, Gatignol (459149v1.19) 2009; 83 Tian, Bevilacqua, Diegelman-Parente, Mathews (459149v1.31) 2004; 5 Samuel (459149v1.35) 2012; 353 George, Gan, Liu, Samuel (459149v1.9) 2011; 31 Strehblow, Hallegger, Jantsch (459149v1.7) 2002; 13 Samuel (459149v1.27) 2011; 411 Taylor, Puig, Darnell, Mihalik, Feinstone (459149v1.37) 2005; 79 Chen, Cho, Wang, Lai, Carter, Nishikura (459149v1.10) 2000; 6 Dauber, Wolff (459149v1.39) 2009; 1 Valente, Nishikura (459149v1.25) 2007; 282 Gelinas, Clerzius, Shaw, Gatignol (459149v1.15) 2011; 85 Schwartz, Rould, Lowenhaupt, Herbert, Rich (459149v1.8) 1999; 284 Chung, Calis, Wu, Sun, Yu, Sarbanes, Dao Thi, Shilvock, Hoffmann, Rosenberg, Rice (459149v1.26) 2018; 172 Pfeifer, Elsby, Fernandez, Faria, Nussenzveig, Lossos, Fontoura, Martin, Barber (459149v1.6) 2008; 105 Li, Banerjee, Goldstein, Dong, Gaughan, Rath, Donovan, Korennykh, Silverman, Weiss (459149v1.4) 2017; 6 Alcami, Saraiva (459149v1.2) 2009; 666 Stark, Kerr, Williams, Silverman, Schreiber (459149v1.11) 1998; 67 de Chassey, Aublin-Gex, Ruggieri, Meyniel-Schicklin, Pradezynski, Davoust, Chantier, Tafforeau, Mangeot, Ciancia, Perrin-Cocon, Bartenschlager, Andre, Lotteau (459149v1.36) 2013; 9 Doria, Neri, Gallo, Farace, Michienzi (459149v1.17) 2009; 37 Pfaller, Li, George, Samuel (459149v1.16) 2011; 23 Toth, Li, Cattaneo, Samuel (459149v1.20) 2009; 284 Gandy, Linnstaedt, Muralidhar, Cashman, Rosenthal, Casey (459149v1.21) 2007; 81 Iizasa, Wulff, Alla, Maragkakis, Megraw, Hatzigeorgiou, Iwakiri, Takada, Wiedmer, Showe, Lieberman, Nishikura (459149v1.22) 2010; 285 Liu, Wolff, Jacobs, Samuel (459149v1.23) 2001; 289 |
| References_xml | – volume: 284 start-page: 1841 year: 1999 end-page: 1845 ident: 459149v1.8 article-title: Crystal structure of the Zalpha domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA publication-title: Science – volume: 94 start-page: 8421 year: 1997 end-page: 8426 ident: 459149v1.12 article-title: A Z-DNA binding domain present in the human editing enzyme, double-stranded RNA adenosine deaminase publication-title: Proc Natl Acad Sci U S A – volume: 105 start-page: 4173 year: 2008 end-page: 4178 ident: 459149v1.6 article-title: NFAR-1 and-2 modulate translation and are required for efficient host defense publication-title: P Natl Acad Sci USA – volume: 13 start-page: 3822 year: 2002 end-page: 3835 ident: 459149v1.7 article-title: Nucleocytoplasmic distribution of human RNA-editing enzyme ADAR1 is modulated by double-stranded RNA-binding domains, a leucine-rich export signal, and a putative dimerization domain publication-title: Mol Biol Cell – volume: 411 start-page: 180 year: 2011 end-page: 193 ident: 459149v1.27 article-title: Adenosine deaminases acting on RNA (ADARs) are both antiviral and proviral publication-title: Virology – volume: 278 start-page: 45833 year: 2003 end-page: 45842 ident: 459149v1.14 article-title: Intracellular localization of differentially regulated RNA-specific adenosine deaminase isoforms in inflammation publication-title: J Biol Chem – volume: 279 start-page: 13249 year: 2004 end-page: 13255 ident: 459149v1.32 article-title: Subcellular distribution of ADAR1 isoforms is synergistically determined by three nuclear discrimination signals and a regulatory motif publication-title: J Biol Chem – volume: 85 start-page: 8460 year: 2011 end-page: 8466 ident: 459149v1.15 article-title: Enhancement of Replication of RNA Viruses by ADAR1 via RNA Editing and Inhibition of RNA-Activated Protein Kinase publication-title: Journal of virology – volume: 12 year: 2011 ident: 459149v1.33 article-title: NoD: a Nucleolar localization sequence detector for eukaryotic and viral proteins publication-title: Bmc Bioinformatics – volume: 7 start-page: 846 year: 2001 end-page: 858 ident: 459149v1.28 article-title: Substrate recognition by ADAR1 and ADAR2 publication-title: RNA – volume: 666 start-page: 167 year: 2009 end-page: 179 ident: 459149v1.2 article-title: Chemokine Binding Proteins Encoded by Pathogens publication-title: Adv Exp Med Biol – volume: 279 start-page: 13249 year: 2004 end-page: 13255 ident: 459149v1.30 article-title: Subcellular distribution of ADAR1 isoforms is synergistically determined by three nuclear discrimination signals and a regulatory motif publication-title: J Biol Chem – volume: 282 start-page: 16054 year: 2007 end-page: 16061 ident: 459149v1.25 article-title: RNA binding-independent dimerization of adenosine deaminases acting on RNA and dominant negative effects of nonfunctional subunits on dimer functions publication-title: J Biol Chem – volume: 5 start-page: 1013 year: 2004 end-page: 1023 ident: 459149v1.31 article-title: The double-stranded-RNA-binding motif: Interference and much more publication-title: Nat Rev Mol Cell Bio – volume: 23 start-page: 573 year: 2011 end-page: 582 ident: 459149v1.16 article-title: Protein kinase PKR and RNA adenosine deaminase ADAR1: new roles for old players as modulators of the interferon response publication-title: Curr Opin Immunol – volume: 83 start-page: 10119 year: 2009 end-page: 10128 ident: 459149v1.19 article-title: ADAR1 Interacts with PKR during Human Immunodeficiency Virus Infection of Lymphocytes and Contributes to Viral Replication publication-title: Journal of virology – volume: 22 start-page: 3421 year: 2003 end-page: 3430 ident: 459149v1.29 article-title: An ADAR that edits transcripts encoding ion channel subunits functions as a dimer publication-title: Embo Journal – volume: 79 start-page: 6291 year: 2005 end-page: 6298 ident: 459149v1.37 article-title: New antiviral pathway that mediates hepatitis C virus replicon interferon sensitivity through ADAR1 publication-title: Journal of virology – volume: 284 start-page: 29350 year: 2009 end-page: 29356 ident: 459149v1.20 article-title: RNA-specific adenosine deaminase ADAR1 suppresses measles virus-induced apoptosis and activation of protein kinase PKR publication-title: J Biol Chem – volume: 172 start-page: 811 year: 2018 end-page: 824 ident: 459149v1.26 article-title: Human ADAR1 Prevents Endogenous RNA from Triggering Translational Shutdown publication-title: Cell – volume: 353 start-page: 163 year: 2012 end-page: 195 ident: 459149v1.35 article-title: ADARs: viruses and innate immunity publication-title: Curr Top Microbiol Immunol – volume: 93 start-page: 335 year: 1998 end-page: 340 ident: 459149v1.3 article-title: The orf virus OV20.0L gene product is involved in interferon resistance and inhibits an interferon-inducible, double-stranded RNA-dependent kinase publication-title: Immunology – volume: 82 start-page: 10864 year: 2008 end-page: 10872 ident: 459149v1.18 article-title: Double-stranded RNA adenosine deaminases enhance expression of human immunodeficiency virus type 1 proteins publication-title: Journal of virology – volume: 289 start-page: 378 year: 2001 end-page: 387 ident: 459149v1.23 article-title: Vaccinia virus E3L interferon resistance protein inhibits the interferon-induced adenosine deaminase A-to-I editing activity publication-title: Virology – volume: 70 start-page: 1961 year: 1996 end-page: 1968 ident: 459149v1.38 article-title: Mechanism of interferon action: Functionally distinct RNA-binding and catalytic domains in the interferon-inducible, double-stranded RNA-Specific adenosine deaminase publication-title: Journal of virology – volume: 67 start-page: 227 year: 1998 end-page: 264 ident: 459149v1.11 article-title: How cells respond to interferons publication-title: Annual Review of Biochemistry – volume: 31 start-page: 99 year: 2011 end-page: 117 ident: 459149v1.9 article-title: Adenosine deaminases acting on RNA, RNA editing, and interferon action publication-title: J Interferon Cytokine Res – volume: 37 start-page: 5848 year: 2009 end-page: 5858 ident: 459149v1.17 article-title: Editing of HIV-1 RNA by the double-stranded RNA deaminase ADAR1 stimulates viral infection publication-title: Nucleic Acids Res – volume: 91 start-page: 6288 year: 1994 end-page: 6292 ident: 459149v1.24 article-title: Double-stranded RNA-dependent protein kinase activates transcription factor NF-kappa B by phosphorylating I kappa B publication-title: Proc Natl Acad Sci U S A – volume: 229 start-page: 203 year: 1999 end-page: 213 ident: 459149v1.13 article-title: Characterization of the 5’-flanking region of the human RNA-specific adenosine deaminase ADAR1 gene and identification of an interferon-inducible ADAR1 promoter publication-title: Gene – volume: 1 start-page: 523 year: 2009 end-page: 544 ident: 459149v1.39 article-title: Activation of the Antiviral Kinase PKR and Viral Countermeasures publication-title: Viruses – volume: 9 year: 2013 ident: 459149v1.36 article-title: The Interactomes of Influenza Virus NS1 and NS2 Proteins Identify New Host Factors and Provide Insights for ADAR1 Playing a Supportive Role in Virus Replication publication-title: Plos Pathog – volume: 6 year: 2017 ident: 459149v1.4 article-title: Ribonuclease L mediates the cell-lethal phenotype of double-stranded RNA editing enzyme ADAR1 deficiency in a human cell line publication-title: eLife – volume: 6 start-page: 755 year: 2000 end-page: 767 ident: 459149v1.10 article-title: A third member of the RNA-specific adenosine deaminase gene family, ADAR3, contains both single- and double-stranded RNA binding domains publication-title: RNA – volume: 81 start-page: 13544 year: 2007 end-page: 13551 ident: 459149v1.21 article-title: RNA editing of the human herpesvirus 8 kaposin transcript eliminates its transforming activity and is induced during lytic replication publication-title: Journal of virology – volume: 11 start-page: 93 year: 2014 ident: 459149v1.40 article-title: ADAR1 enhances HTLV-1 and HTLV-2 replication through inhibition of PKR activity publication-title: Retrovirology – volume: 111 start-page: E1852 year: 2014 end-page: E1861 ident: 459149v1.34 article-title: A bimodular nuclear localization signal assembled via an extended doublestranded RNA-binding domain acts as an RNA-sensing signal for transportin 1 publication-title: P Natl Acad Sci USA – volume: 9 start-page: 949 year: 2008 end-page: 952 ident: 459149v1.1 article-title: Chemokines and leukocyte traffic publication-title: Nat Immunol – volume: 48 start-page: 89 year: 2009 end-page: 90 ident: 459149v1.5 article-title: NFAR-1 and NFAR-2 modulate translation and are required for efficient host defense publication-title: Cytokine – volume: 285 start-page: 33358 year: 2010 end-page: 33370 ident: 459149v1.22 article-title: Editing of Epstein-Barr virus-encoded BART6 microRNAs controls their dicer targeting and consequently affects viral latency publication-title: J Biol Chem |
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| Snippet | Orf virus (ORFV) infects sheep and goats and is also an important zoonotic pathogen. The viral protein OV20.0 has been shown to suppress innate immunity by... |
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| SubjectTerms | Adenosine Adenosine deaminase Double-stranded RNA eIF-2 kinase Innate immunity Interferon Kinases Microbiology Orf Phosphorylation Protein kinase |
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| Title | Adenosine Deaminase Acting on RNA 1 Associates with Orf Virus OV20.0 and Enhances Viral Replication |
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