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RNA-binding protein that plays a role in the inhibition of multiple cellular antiviral responses activated by double-stranded RNA (dsRNA), such as inhibition of PKR activation, necroptosis, and IFN-mediated antiviral activities. Recognizes and binds Z-RNA structures via its Z-binding domain and dsRNA via its DRBM domain: RNA-binding activity is required to escape host ZBP1-dependent necroptosis. Mechanistically, the Z-binding domain binds Z-RNAs that are produced during vaccinia virus infection, thereby competing with Z-RNA detection by host ZBP1, suppressing ZBP1-dependent necroptosis. Acts as a key inhibitor of the interferon response by blocking the phosphorylation and subsequent activation of IRF3 and IRF7 kinases that are required for interferon-alpha gene expression. Inhibits NF-kappa-B activation and the ubiquitin-like protein ISG15, which is an early antiviral protein. The binding with host ISG15 subsequently blocks host ISGylation.
Protein E3
100 µL