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Details on Person Viral infection produces dsRNA that activates the 2'-5' olig...
| Class:Id | Summation:9615040 |
|---|---|
| _displayName | Viral infection produces dsRNA that activates the 2'-5' olig... |
| _timestamp | 2018-07-31 02:59:58 |
| created | [InstanceEdit:9615041] Shamovsky, Veronica, 2018-07-30 |
| literatureReference | [LiteratureReference:9614479] Small self-RNA generated by RNase L amplifies antiviral innate immunity [LiteratureReference:9614534] RNase L activates the NLRP3 inflammasome during viral infections [LiteratureReference:9614527] Viral phosphodiesterases that antagonize double-stranded RNA signaling to RNase L by degrading 2-5A [LiteratureReference:9614513] Murine AKAP7 has a 2',5'-phosphodiesterase domain that can complement an inactive murine coronavirus ns2 gene [LiteratureReference:9614518] Antagonism of the interferon-induced OAS-RNase L pathway by murine coronavirus ns2 protein is required for virus replication and liver pathology [LiteratureReference:9614493] Homologous 2',5'-phosphodiesterases from disparate RNA viruses antagonize antiviral innate immunity [LiteratureReference:9614521] Structural basis for 2'-5'-oligoadenylate binding and enzyme activity of a viral RNase L antagonist [LiteratureReference:9614500] Crystal structure of the mouse hepatitis virus ns2 phosphodiesterase domain that antagonizes RNase L activation [LiteratureReference:9614495] Middle East Respiratory Syndrome Coronavirus NS4b Protein Inhibits Host RNase L Activation [LiteratureReference:9614516] Lineage A Betacoronavirus NS2 Proteins and the Homologous Torovirus Berne pp1a Carboxy-Terminal Domain Are Phosphodiesterases That Antagonize Activation of RNase L [LiteratureReference:9614441] pppA2'p5'A2'p5'A: an inhibitor of protein synthesis synthesized with an enzyme fraction from interferon-treated cells [LiteratureReference:9615066] Crystal structure of the C-terminal 2',5'-phosphodiesterase domain of group A rotavirus protein VP3 [LiteratureReference:9615063] AKAP18 contains a phosphoesterase domain that binds AMP [LiteratureReference:9012235] Viral encounters with 2',5'-oligoadenylate synthetase and RNase L during the interferon antiviral response [LiteratureReference:9615070] Detection of novel members, structure-function analysis and evolutionary classification of the 2H phosphoesterase superfamily |
| modified | [InstanceEdit:9615060] Shamovsky, Veronica, 2018-07-31 [InstanceEdit:9615061] Shamovsky, Veronica, 2018-07-31 [InstanceEdit:9615065] Shamovsky, Veronica, 2018-07-31 |
| text | Viral infection produces dsRNA that activates the 2'-5' oligoadenylate synthetase (OAS) to synthesize 5'-triphosphorylated 2'-5'-linked oligoadenylate from ATP. The 2'-5'-linked oligoadenylate with a chemical structure of ppp5'A(2'p5'A)n contain 2 to greater than 5 adenylyl residues (n>2) and are commonly referred to as 2-5A (Kerr IM & Brown RE 1978). The 2-5As bind latent ribonuclease L (RNase L) which in human is encoded by RNASEL gene. RNase L oligomerizes into an active complex capable of cleaving viral ssRNA and cellular ssRNA to inhibit viral replication and spread (Silverman RH 2007; Malathi K et al. 2007; Chakrabarti A et al. 2015). Viruses have developed diverse strategies to escape the host antiviral effects. Several viruses, including some coronaviruses and rotaviruses, encode structurally related 2H phosphoesterases with two conserved His-x-Ser/Thr motifs in their catalytic sites. The NS4b protein of Middle East respiratory syndrome coronavirus (MERS-CoV), the protein VP3 of rotavirus A (RVA), the non-structural 2 (NS2) protein of human respiratory coronavirus HCoV-OC43 and its homologue ns2 protein of mouse hepatitis virus (MHV) possess enzymatic 2′,5-phosphodiesterase (PDE) activity that is capable of antagonizing RNase L and thus countering a potent host antiviral response in mammals (Mazumder R et al., 2002; Zhao L et al. 2012; Zhang R et al. 2013; Silverman RH & Weiss SR 2014; Ogden KM et al. 2015; Sui B et al. 2016; Thornbrough JM et al. 2016; Goldstein SA et al. 2017). The viral 2',5'-PDEs are phylogenetically related to the cellular 2',5'-PDE, a kinase anchoring protein 7 (AKAP7) (Mazumder R et al., 2002; Gold MG et al. 2008; Ogden KM et al. 2015; Brandmann T & Jinek M 2015). Murine AKAP7 was found to cleave the phosphodiester bonds of 2-5A in vitro with rates similar to its viral homologues, ns2 of MHV and VP3 of RVA (Gusho E et al. 2014). Murine AKAP7 (full length and central domain) also effectively degraded 2-5A in intact pIC-transfected human ovarian carcinoma Hey1B cells (Gusho E et al. 2014). The proviral effect of murine AKAP7 required cytoplasmic localization of the PDE domain of AKAP7, whereas full-length AKAP7 was observed only in nuclei. Further studies are needed to identify the subcellular compartment of 2′,5′-PDE activity of AKAP7. The Reactome event shows a cleavage of 2-5A by RVA protein VP3 as an example of viral 2',5'-PDE activity that antagonizes dsRNA signaling to RNase L. |
| (summation) | [Depolymerisation:9615042] Viral 2',5'-PDE cleaves 2'-5' oligoadenylates [Homo sapiens] |
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