Human metapneumovirus fusion glycoprotein (hMPV F protein)

Human metapneumovirus fusion glycoprotein (hMPV F protein) is a trimeric viral surface protein essential for mediating the merger of the viral and host cell membranes[1][5][4][8]. It is first synthesized as an inactive precursor (F0), which undergoes proteolytic cleavage to generate disulfide-bonded F1 and F2 subunits; three such heterodimers assemble into a metastable prefusion trimeric complex[3][4]. During infection, the F protein triggers fusion of viral and cellular membranes, initiating entry and an infectious cycle[1][3][7][4]. This glycoprotein is densely glycosylated and contains conserved motifs (such as RGD) that enable interactions with host cell surface factors (proteoglycans, integrins)[1][7]. The F protein is the primary target of neutralizing antibodies and a key antigen for vaccine design[1][5][4][8]. Highly conserved among viral subgroups, its structure resembles those of related paramyxovirus fusion proteins, such as RSV F[1][5][4]. Antigenic epitopes differ between pre-fusion and post-fusion conformations, and only certain conformations have optimal immunogenicity for vaccine purposes[4][8].

Other names

hMPV F proteinMetapneumovirus F proteinFusion (F) glycoprotein

Neutralization by antibodies: antibodies bind key epitopes on F protein, preventing fusion and viral entry[1][3][4][5] Vaccine antigens: recombinant or stabilized F protein used to elicit protective immune response[1][4][8]