Nipah virus fusion glycoprotein (NiV-F) (NiV-F)

The Nipah virus fusion glycoprotein (NiV-F) is a critical class I viral fusion protein located on the envelope of the Nipah virus, a highly pathogenic paramyxovirus (UniProt: P0C1C6). It is synthesized as a precursor (F0) that is proteolytically cleaved into F1 and F2 subunits, which then assemble into a metastable prefusion trimer (Nature Communications, 2019). Upon activation—typically triggered by the binding of the companion attachment glycoprotein (NiV-G) to host receptors like ephrin-B2 or ephrin-B3—NiV-F undergoes a massive conformational rearrangement into a stable postfusion state (PNAS, 2011). This process drives the fusion of the viral envelope with the host cell membrane, allowing the viral genome to enter the cytoplasm. Because the prefusion form contains the most potent neutralizing epitopes, it is a primary focus for vaccine design and the development of fusion-inhibiting therapeutics (NIH, 2022). Targeting NiV-F is essential for preventing the severe encephalitis and respiratory distress associated with Nipah virus outbreaks, which have high fatality rates (WHO, 2024).

Other names

NiV-FFusion proteinPrefusion F proteinClass I viral fusion proteinNipah virus fusion protein

Inhibition of viral-host membrane fusion by stabilizing the prefusion conformation or blocking the transition to the postfusion state.