West Nile virus polyprotein (WNV polyprotein) (WNV polyprotein)

West Nile virus (WNV) viral antigens are the structural and non-structural proteins derived from the translation of the viral RNA into a single polyprotein (UniProt: P06935). The structural proteins—Capsid (C), Membrane (M), and Envelope (E)—mediate virion assembly and host cell attachment, with the E protein serving as the primary target for neutralizing antibodies (PubMed: 29431631). The non-structural proteins (NS1 to NS5) are essential for viral replication and immune modulation; for instance, NS3 functions as a protease and helicase, while NS5 acts as the RNA-dependent RNA polymerase (StatPearls: NBK430786). These antigens are the focus of therapeutic efforts, including the development of monoclonal antibodies like E16 and small-molecule inhibitors like Galidesivir (BCX4430) (NIH: PMC4395658). Despite their importance in the viral life cycle and disease progression to West Nile encephalitis, there are currently no FDA-approved vaccines or specific antiviral therapies for human use (CDC: West Nile Virus).

Other names

West Nile virus viral antigensWNV structural and non-structural proteinsWNV E proteinWNV NS3 proteaseWNV NS5 polymeraseWNV NS1 antigen

Inhibition of viral RNA-dependent RNA polymerase (NS5), neutralization of viral envelope (E) protein to prevent host cell entry, and inhibition of viral NS3 protease activity to prevent polyprotein processing.