Nucleoprotein (SARS-CoV) (N)

The Nucleoprotein (SARS-CoV) is a vital structural component that plays a central role in the packaging of the viral RNA genome into a helical ribonucleoprotein complex (McBride et al., 2014). It is a highly basic phosphoprotein that consists of three distinct domains: an N-terminal RNA-binding domain, a C-terminal dimerization domain, and a central disordered linker region (UniProt P59595). Beyond its structural duties in virion assembly, the N protein is involved in viral RNA replication and transcription by interacting with the viral replicase-transcriptase complex. It also functions as a potent suppressor of host RNA interference and interferon signaling, thereby facilitating viral pathogenesis and immune evasion (Chang et al., 2014). Due to its high abundance during infection and its relative conservation compared to the spike protein, the N protein is a primary target for rapid diagnostic tests and a promising candidate for broad-spectrum antiviral therapies. Current drug discovery efforts focus on small molecules that can disrupt N protein dimerization or its interaction with viral RNA, effectively halting the viral life cycle.

Other names

Nucleocapsid proteinProtein NSARS-CoV N proteinSARS-CoV-1 nucleocapsid protein

Inhibition of the N-terminal RNA-binding domain (NTD) or the C-terminal dimerization domain (CTD) to prevent viral genome encapsulation and assembly (Chang et al., 2014; Lin et al., 2014).