Prefusion fusion protein of human metapneumovirus (hMPV F protein)

The **prefusion fusion (F) protein of human metapneumovirus** is a trimeric, class I viral fusion glycoprotein present on the surface of HMPV virions[5][7]. It mediates fusion of the viral and host cell membranes, which is essential for viral entry into respiratory epithelial cells[1][6]. The prefusion conformation of the F protein is metastable and undergoes irreversible structural transition to a stable postfusion state upon activation, a process required for membrane fusion[7]. This protein is the primary target of neutralizing antibodies and is a leading vaccine antigen candidate[1][4][5][7]. The F protein binds to host cell-surface molecules such as **heparan sulfate** and possesses an **RGD motif** that mediates interaction with integrins (notably α5β1)[1][3][4]. Proteolytic cleavage by trypsin-like serine proteases (e.g., TMPRSS2) is required for activation[5]. Stabilization of the prefusion conformation has enabled improved immunogen design for next-generation vaccines[5][7]. It plays a central role in the pathogenesis of HMPV respiratory infections and is considered an essential therapeutic target for both antibodies and candidate vaccines[1][4][5][6][7].

Other names

human metapneumovirus F proteinhMPV fusion glycoproteinfusion (F) glycoprotein of HMPV

Neutralizing antibodies prevent conformational transition from prefusion to postfusion state, thus blocking viral membrane fusion and entry[4][5][7]