Respiratory Syncytial Virus Nucleoprotein N (RSV N)

The nucleoprotein N of respiratory syncytial virus (RSV) is a highly conserved structural protein essential for the virus’s life cycle. It encapsidates the viral negative-sense RNA genome, forming a ribonucleoprotein (RNP) complex that serves as the template for both mRNA synthesis and genome replication. The RNP complex is critical for protecting viral RNA from nucleases and ensuring efficient transcription and replication. The RSV N protein consists of 391 amino acids. It has two core domains: N-terminal domain (NTD) and C-terminal domain (CTD). These domains form a groove where the viral RNA binds. The structure also includes flexible extensions: N-arm (residues 1–28) and C-arm (residues 360–375). These arms interact with adjacent subunits in the helical nucleocapsid, stabilizing its structure while allowing flexibility. When bound to RNA, multiple N proteins oligomerize to form a left-handed helical nucleocapsid within the virion particle. Requires interaction with phosphoprotein P to remain in an RNA-free monomeric state before encapsidation; P acts as a chaperone preventing premature self-association or binding to cellular RNAs. Plays roles beyond structural support: Modulates host immune responses by sequestering host factors such as NF-kappa-B, IFIH1/MDA5, and MAVS into inclusion bodies within infected cells, thereby inhibiting innate immune signaling pathways. The RSV N protein is considered an attractive antiviral target due to its essential role in multiple stages of infection. Inhibitors like RSV604 have been shown to bind directly to this protein, disrupting its function and impeding virus replication.

Other names

Protein NNucleocapsid proteinNC protein

Inhibition of nucleoprotein function, disruption of virus replication