Measles virus structural proteins (MeV proteins)

The measles virus (MeV) structural proteins include the Hemagglutinin (H), Fusion (F), Nucleocapsid (N), Phosphoprotein (P), Matrix (M), and Large (L) proteins, which are essential for the viral life cycle [1]. The H and F glycoproteins are surface-exposed and mediate host cell entry; H binds to receptors like SLAMF1 (CD150) on immune cells and Nectin-4 on epithelial cells, while F facilitates the fusion of the viral envelope with the host cell membrane [2]. Inside the host cell, the N, P, and L proteins form the viral replication complex, with the L protein functioning as the RNA-dependent RNA polymerase to synthesize viral mRNA and replicate the RNA genome [3]. The M protein plays a critical role in viral assembly by bridging the internal ribonucleoprotein complex with the envelope glycoproteins at the plasma membrane for budding [4]. These proteins are the primary targets for the highly effective live-attenuated measles vaccine, which generates long-lasting neutralizing antibodies specifically against the H and F proteins [5]. Beyond vaccines, these proteins are targets for experimental antiviral therapies, such as small-molecule inhibitors like ERDRP-0519 that target the L protein polymerase activity [6]. Understanding the structural biology of these proteins is vital for addressing complications like subacute sclerosing panencephalitis (SSPE), where mutations in the M or F proteins can lead to persistent CNS infection [7].

Other names

Measles virus glycoproteinsMeasles virus envelope proteinsMeasles virus H, F, N, P, M, and L proteinsMeV structural proteins

Neutralization of viral attachment and fusion; Inhibition of RNA-dependent RNA polymerase; Inhibition of viral assembly