The ～30kb positive-stranded RNA genome of coronaviruses encodes a replication/transcription machinery that is unusually complex and composed of 16 nonstructural proteins (nsps). The four proteins nsp7 to nsp10, which are conserved among all CoVs but have no functional homologs outside of the Coronaviridae, are translated as part of the viral polyproteins pp1a and pp1ab, and the mature proteins are released by the action of the SARS-CoV protease nsp5. Hexadecamer of nsp7 and nsp8 may possess dsRNA-binding activity. SARS-CoV 2 nonstructural protein 7 (nsp7) is of interest for its potential roles in the transcription and replication of the positive-stranded viral RNA genome.
Cleavage by the viral main protease, 3CLpro results in generating the nsp8 protein, The nsp8 protein has been shown to associate with several other nsps and to colocalize with these nsps in cytoplasmic complexes that are important for viral RNA synthesis. It forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. Nsp8 was shown to have RNA-dependent RNA polymerase (RdRp) activity that could be involved in producing primers utilized by nsp12 which is normally accepted to be the RdRp for SARS-CoV.
Coronavirus N protein is required for coronavirus RNA synthesis, and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is a most abundant protein of coronavirus. N protein packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. Because of the conservation of N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.
Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. Coronavirus N protein is required for coronavirus RNA synthesis, and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is a most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.
Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. The coronavirus N protein is required for coronavirus RNA synthesis and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is the most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to the formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of the N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.
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