Marburgvirus nucleoprotein (NP)

The Marburgvirus nucleoprotein (NP) is a key viral structural protein that encapsidates the single-stranded RNA genome, forming a protective helical ribonucleoprotein (RNP) complex essential for transcription, replication, and nucleocapsid assembly during the virus life cycle. It features a conserved bilobed core domain with a positively charged RNA-binding groove between N- and C-terminal lobes, enabling oligomerization into hexameric states via hydrophobic interactions in its apo form, while VP35 chaperone binding induces a conformational shift to a monomeric open state that prevents nonspecific RNA interactions. In the nucleocapsid, thousands of NP copies spiral around the genome, each binding approximately six RNA bases, supporting genome packaging and viral particle formation from host cell membranes. NP's dynamic regulation by VP35 ensures proper RNP formation, with structural flexibility in its C-terminal helix conserved across filoviruses, highlighting its critical role in viral propagation. As a highly abundant protein in infected cells, NP represents a promising antiviral target, particularly through disruption of its VP35-binding pocket or oligomerization interfaces to block RNP assembly.

Other names

MARV nucleoproteinnucleocapsid protein