Target intelligence / Profile preview

Nipah virus fusion and attachment glycoproteins (NiV-F and NiV-G) (NiV-F/G)

Target
NiV-F/G
Molecular classification
Viral surface protein, Glycoprotein, Viral attachment protein, Viral fusion protein, Type I transmembrane protein, Type II transmembrane protein
01

Overview

The Nipah virus (NiV) glycoproteins, comprising the attachment glycoprotein (G) and the fusion glycoprotein (F), are the primary surface antigens responsible for viral entry into host cells (UniProt: P0C1C6, P0C1C7). The G protein initiates infection by binding to host cell receptors ephrin-B2 and ephrin-B3, which are expressed on endothelial cells and neurons, explaining the virus's systemic and neurotropic nature (Negrete et al., 2005, Nature). This binding triggers a cascade of conformational changes in the F protein, leading to the fusion of the viral envelope with the host cell membrane (Bossart et al., 2002, J. Virol.). Because they are essential for infectivity and are exposed on the virion surface, these glycoproteins are the primary targets for neutralizing antibodies and vaccine development (WHO, 2024). Therapeutic candidates like the monoclonal antibody m102.4 target the G protein to block receptor binding, providing a critical strategy for post-exposure treatment of this highly fatal zoonotic infection (Bossart et al., 2011, Sci. Transl. Med.).

Other names
NiV-GNiV-FNipah virus G proteinNipah virus F proteinAttachment glycoproteinFusion glycoproteinNiV glycoproteins
02

Mechanism of action

Neutralization of viral entry by blocking the interaction between the G glycoprotein and host ephrin-B2/B3 receptors, or by inhibiting the F protein-mediated membrane fusion process (Bossart et al., 2011, Sci. Transl. Med.; Aguilar et al., 2009, J. Virol.).

03

Biological functions

Viral attachmentMembrane fusionHost cell entryReceptor bindingSyncytium formation
04

Disease associations

Nipah virus infectionEncephalitisAcute respiratory distress syndromeSystemic vasculitis
05

Safety considerations

High pathogenicity and mortality rate (40-75%) (WHO, 2024)Requirement for BSL-4 containmentPotential for viral mutational escapeAntibody-dependent enhancement (theoretical risk)Limited clinical trial feasibility due to sporadic outbreaks
06

Interacting drugs

m102.4

2 more in the full profile.

07

Biomarkers

NiV-G specific antibodiesNiV-F specific antibodiesViral RNA (NiV RNA)Soluble ephrin-B2

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