Mumps virus internal proteins (MuV internal proteins)

The internal proteins of the Mumps virus (MuV), a member of the Paramyxoviridae family, include the nucleocapsid (N), phosphoprotein (P), large (L) polymerase, matrix (M), and the non-structural V and I proteins (UniProt: P11214, P06940). These proteins are essential for the viral life cycle, facilitating genome encapsidation, RNA-dependent RNA replication, transcription, and viral assembly (PubMed: 25653450). The L and P proteins form the polymerase complex responsible for synthesizing viral mRNA and genomic RNA, while the N protein protects the RNA genome from host cell nucleases and serves as a template for replication (PubMed: 17223310). The M protein is critical for orchestrating virus assembly and budding at the host cell plasma membrane (PubMed: 22114333). Furthermore, the V protein acts as a potent interferon antagonist by targeting STAT proteins for proteasomal degradation, thereby subverting the host's innate immune response (PubMed: 11435588). While current clinical management relies on vaccination, these internal proteins are primary targets for developing direct-acting antivirals, including polymerase inhibitors like ribavirin and favipiravir, which aim to halt viral replication (PubMed: 15652225, PubMed: 24434254).

Other names

Mumps orthorubulavirus internal proteinsMuV N, P, L, M, V, and I proteinsMumps virus nucleocapsid proteinMumps virus phosphoproteinMumps virus large proteinMumps virus matrix proteinMumps virus V proteinMumps virus I protein

Inhibition of the viral RNA-dependent RNA polymerase (RdRp) complex, disruption of the interaction between the nucleocapsid and polymerase, and interference with viral assembly and budding processes.