Scientists have discovered the Ebola virus proteins VP24 and VP35 that forms complex and coordinates the formation of nucleocapsid assembly through the polymerization of nucleoprotein (NP) along the viral RNA genome. VP35 functions as a chaperone and replication cofactor, stabilizing a newly identified outer third monomeric layer of NP, while VP24 helps stabilize and condense the nucleocapsid structure. The study also revealed that the intrinsically disordered region and C-terminal domain of the outer NP layer act as a flexible tether linking the nucleocapsid to the viral matrix. These conserved protein interfaces are promising targets for broad-spectrum antiviral therapies.