Nucleoprotein of human respiratory syncytial virus (N protein (RSV N))

The nucleoprotein of human respiratory syncytial virus (RSV N) is a 391-residue structural protein that encapsidates the viral negative-sense single-stranded RNA genome, forming the nucleocapsid that serves as both the template for the viral RNA-dependent RNA polymerase and a scaffold for virion assembly[2][3][5]. The N protein consists of a core with N-terminal and C-terminal domains, as well as flexible N- and C-terminal arms that stabilize inter-protein interactions within the nucleocapsid[1][2][3]. N protein’s primary functions are to protect the viral RNA from degradation, facilitate efficient replication and transcription by providing the proper template structure, and participate in evasion of the innate immune response by shielding the RNA genome from detection[3][5]. The protein interacts closely with other viral proteins—including the phosphoprotein (P), the large polymerase protein (L), and the processivity factor M2-1—and is highly conserved and abundant, making it a promising antiviral drug target[2][3][5][7]. At present, N protein is mainly of interest for therapeutics and diagnostics: it is a distinguishing biomarker for active RSV infection[3][5], and ongoing research continues to explore its viability as a drug target for direct-acting antivirals.

Other names

nucleocapsid proteinN proteinNucleoprotein (N)RSV NHRSV N protein

Inhibition of nucleoprotein–RNA binding (experimental/under investigation): Small molecules may disrupt the interaction between the N protein and viral RNA, thus blocking replication and transcription[3][5]. Inhibition of nucleocapsid assembly (experimental/under investigation): Potential inhibitors may prevent the assembly of the N protein into nucleocapsids, disrupting the viral life cycle[3].