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Details on Person Antiviral innate immune response receptor RIG-I (also known ...
| Class:Id | Summation:9717499 |
|---|---|
| _displayName | Antiviral innate immune response receptor RIG-I (also known ... |
| _timestamp | 2021-03-10 21:47:36 |
| created | [InstanceEdit:9717460] Shamovsky, Veronica, 2021-03-10 |
| literatureReference | [LiteratureReference:918161] TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity [LiteratureReference:936427] Riplet/RNF135, a RING finger protein, ubiquitinates RIG-I to promote interferon-beta induction during the early phase of viral infection [LiteratureReference:9717517] Influenza A virus NS1 targets the ubiquitin ligase TRIM25 to evade recognition by the host viral RNA sensor RIG-I [LiteratureReference:9717462] Molecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition [LiteratureReference:9717487] Species-specific inhibition of RIG-I ubiquitination and IFN induction by the influenza A virus NS1 protein [LiteratureReference:9717524] Viral Evasion of RIG-I-Like Receptor-Mediated Immunity through Dysregulation of Ubiquitination and ISGylation [LiteratureReference:1237356] Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses |
| text | Antiviral innate immune response receptor RIG-I (also known as retinoic acid-inducible gene I protein RIG-1 or DDX58) directly recognizes and binds to viral 5′-PPP RNA and short dsRNA through its helicase and repressor domain (Kato H et al. 2006). After recognition, the N-terminal caspase recruitment domains (CARDs) of DDX58 (RIG-1) are modified by ubiquitin. The ubiquitination is mediated by the E3 ubiquitin/ISG15 ligase tripartite motif protein 25 (TRIM25) and and E3 ubiquitin-protein ligase RNF135 (RNF135, REUL) (Gack MU et al. 2007; Oshiumi H et al 2009). Co-immunoprecipitation assay showed that the influenza A virus (IAV) non-structural protein 1 (NS1) binds TRIM25 upon co-expression in human embryonic kidney 293T (HEK293T) cells (Gack MU et al. 2009; reviewed in Chiang C et al. 2021). Viral NS1 interacted with endogenous TRIM25 in HEK293T cells infected with various IAV strains (Gack MU et al. 2009). Confocal microscopy revealed that TRIM25 and NS1 co-localized in the cytoplasm upon co-expression in HeLa cells (Gack MU et al. 2009). Mutagenesis studies showed that NS1 targets a central coiled-coil domain (CCD) of TRIM25 suppressing TRIM25 oligomerization and subsequent TRIM25-dependent ubiquitination of the N-terminal CARDs of DDX58 (RIG-1) in HEK293T cells (Gack MU et al. 2009). Structural studies confirmed interaction between viral NS1 and CCD of TRIM25 (Koliopoulos MG et al. 2018). However, the structures, together with biochemical and mutagenesis studies suggest that the CCD-mediated dimerization of TRIM25 is not affected by NS1. Instead, the NS1 binding interfered with the correct positioning of the substrate-binding PRY/SPRY domain of TRIM25 thus preventing the K63-linked ubiquitination of DDX58 (Koliopoulos MG et al. 2018). Further, NS1 was found to antagonize the mouse DDX58 signaling pathway in the TRIM25-independent manner suggesting that IAV develops evasion strategies adjusting to different host species (Rajsbaum R et al. 2012). IAV NS1 was also reported to interact with RNF135 to suppress RNF135-mediated DDX58 ubiquitination in human non-small cell lung cancer A549 cell and in mouse Hepa 1.6 cells (Rajsbaum R et al. 2012). |
| (summation) | [Reaction:9717470] IAV NS1 binds TRIM25 [Homo sapiens] |
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