Respiratory syncytial virus proteins (RSV proteins)

Respiratory syncytial virus (RSV) proteins constitute the entire functional and structural machinery of the virus, a major cause of severe lower respiratory tract infections in infants and the elderly (PubMed: 31110114). The proteome includes the Large (L) protein, which acts as the RNA-dependent RNA polymerase, and the Nucleocapsid (N) and Phosphoprotein (P) which are essential for viral RNA replication and transcription (UniProt: P03418, P03422). Structural proteins such as the Fusion (F) and Attachment (G) glycoproteins are critical for viral entry into host cells and are the primary targets for neutralizing antibodies like Palivizumab and Nirsevimab (FDA). The Small Hydrophobic (SH) protein acts as a viroporin, while the Matrix (M) protein facilitates viral assembly and budding at the host cell membrane. Non-structural proteins NS1 and NS2 are vital for evading the host's innate immune response by inhibiting interferon signaling pathways. Therapeutic development focuses on inhibiting these proteins to reduce viral load and disease severity, with current research targeting the N and L proteins for small-molecule inhibition (ClinicalTrials.gov).

Other names

RSV proteomeRespiratory syncytial virus structural and non-structural proteinsRSV SH, M, N, P, L, NS1, NS2, F, G, M2 proteinsRespiratory syncytial virus SH, M, N, P, L and other structural/nonstructural proteins

Inhibition of viral RNA-dependent RNA polymerase (L protein), disruption of nucleocapsid (N protein) assembly, and blockade of viral fusion (F protein) or attachment (G protein) to host cells.