PMC:7352545 / 12447-14467 JSONTXT

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Nsp3 is a multi-domain transmembrane (TM) protein with diverse activities. Ubiquitin-like 1 and acidic domains bind to N protein and ADP-ribose-1′-phosphatase (ADRP) activity induces cytokine expression. The papain-like protease (PLpro)(PDB:6WX4)/ deubiquitinase domain cleaves virus-produced polyprotein. Nsp4 is a TM scaffold protein for double-membrane vesicle structure. Nsp5 has a main protease domain which also cleaves virus-produced polyprotein and Nsp6 acts as a TM scaffold protein. The Nsp7 and Nsp8 proteins form the Nsp7-Nsp8 hexadecameric complex, which functions as an RNA polymerase-specific clamp and a primase enzyme. Nsp9 is an RNA-binding protein that activates ExoN and 2-O-methyltrnasferase (MTase) enzyme activity. Nsp10 binds to Nsp16 and Nsp14 to form a heterodimeric complex. Nsp12 is the RdRp and Nsps13 is the RNA helicase and 5′ triphosphatase. Nsps14 is a N7 MTase and 3′-5′ exoribonuclease. ExoN of Nsap14 acts as an N7 MTase and attaches the 5′ cap to viral RNAs. Viral exoribonuclease enzyme proofreads the viral RNA genome, where Nsp15 is a viral endoribonuclease (PDB: 6VWW). 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