Measles virus internal proteins (MeV internal proteins)

The internal proteins of the Measles virus (MeV) comprise the nucleoprotein (N), phosphoprotein (P), large protein (L), matrix protein (M), and the non-structural proteins V and C (UniProt: P03422, P03421, P08362, P06942). The N, P, and L proteins constitute the ribonucleoprotein (RNP) complex, which serves as the essential template for viral RNA transcription and replication, with the L protein acting as the catalytic RNA-dependent RNA polymerase (PubMed: 25344324). The M protein is a peripheral membrane protein that coordinates the assembly of these RNPs with the viral envelope at the host cell plasma membrane, a critical step for viral budding (PubMed: 21835787). Non-structural proteins V and C are primarily involved in antagonizing the host's innate immune response by inhibiting interferon signaling pathways (PubMed: 17110521). These proteins are key targets for antiviral development; for example, experimental inhibitors like ERDRP-0519 target the L protein to block RNA synthesis, while compounds like AS-136 aim to disrupt the N-P protein-protein interaction (PubMed: 22514371). Targeting these internal components is vital for treating severe measles cases and preventing fatal complications such as subacute sclerosing panencephalitis (SSPE).

Other names

Measles virus N, P, L, M, V, and C proteinsMeV ribonucleoprotein complexMeasles virus structural and non-structural internal proteins

Inhibition of viral RNA-dependent RNA polymerase activity, disruption of nucleocapsid assembly through N-P interaction inhibition, and interference with matrix protein-mediated viral budding.