Human metapneumovirus fusion protein (prefusion conformation) (hMPV F protein)

The human metapneumovirus fusion protein (prefusion conformation) is a trimeric, class I viral fusion glycoprotein essential for mediating viral entry through membrane fusion. It is synthesized as an inactive precursor (F0), requiring proteolytic cleavage into F1 and F2 subunits which remain covalently linked. The prefusion conformation is the native state presented on viral particles prior to cell entry, and is the main target of potently neutralizing antibodies. Structural studies have shown the prefusion F exposes multiple key neutralizing epitopes, some conserved with related viruses such as respiratory syncytial virus (RSV). Its central role in infection, accessibility on the virus surface, and ability to elicit strong neutralizing immune responses make it the primary candidate for structure-based vaccine design and therapeutic antibody development against human metapneumovirus

Other names

hMPV F proteinHuman metapneumovirus F glycoproteinMetapneumovirus fusion glycoprotein

Neutralizing antibodies prevent membrane fusion and viral entry by binding to functional or antigenic sites on the prefusion F protein, stabilizing it, or preventing its conformational change required for fusion