Nipah virus fusion glycoprotein (NiV-F)

The Nipah virus fusion glycoprotein (NiV-F) is a critical Class I viral fusion protein located on the surface of the Nipah virus envelope. It functions in tandem with the attachment glycoprotein (G) to facilitate the merger of the viral and host cell membranes, a process essential for viral entry and infection. Upon the binding of the G protein to host receptors like ephrin-B2 or ephrin-B3, NiV-F undergoes a dramatic conformational change from a metastable prefusion state to a stable postfusion state, which drives the fusion of the lipid bilayers. Beyond its role in entry, NiV-F is responsible for cell-to-cell fusion, resulting in pathognomonic multinucleated syncytia that contribute to extensive vascular and neuronal damage. As a surface-exposed protein, NiV-F is a primary target for the development of vaccines and therapeutic countermeasures. Neutralizing monoclonal antibodies such as 5B3, 1F5, and mAb92 specifically target epitopes on NiV-F to lock it in its prefusion conformation and prevent infection. Additionally, fusion-inhibitory lipopeptides derived from the heptad repeat regions of the protein are under investigation for their ability to block the formation of the six-helix bundle required for membrane fusion. Given the high fatality rate of Nipah virus and its potential for person-to-person transmission, NiV-F remains a focal point for structural biology and drug discovery efforts aimed at pandemic preparedness.

Other names

Protein FFusion proteinNiV fusion proteinF glycoproteinHNV-F

Inhibition of viral-host membrane fusion, stabilization of the prefusion conformation, and blockade of six-helix bundle (6HB) formation.