Target intelligence / Profile preview

Nipah virus surface glycoproteins (G and F) (NiV G and F)

Target
NiV G and F
Molecular classification
Viral surface protein, Glycoprotein, Viral attachment protein, Viral fusion protein, Type II transmembrane protein (G), Type I transmembrane protein (F)
01

Overview

The Nipah virus surface glycoproteins, comprising the attachment protein (G) and the fusion protein (F), are the essential molecular machinery for viral entry into host cells (UniProt Q9IK92, Q9IK91). The G protein initiates infection by binding to host cell receptors, primarily Ephrin-B2 and Ephrin-B3, which are widely expressed in the vascular endothelium and central nervous system (Nature, 2005). This binding event triggers a conformational change in the F protein, which then mediates the fusion of the viral envelope with the host cell plasma membrane (Journal of Virology, 2011). As the primary targets for the host's neutralizing antibody response, these glycoproteins are the focus of intensive vaccine and therapeutic development (NIH, 2023). For instance, the monoclonal antibody m102.4 targets the receptor-binding domain of the G protein to prevent viral attachment (Science Translational Medicine, 2011). Additionally, vaccine candidates like mRNA-1215 utilize the G protein sequence to elicit protective immunity (Moderna, 2024). Given the high case fatality rate of Nipah virus infection, which can reach 75%, these proteins represent critical targets for preventing fatal encephalitis and severe respiratory distress (WHO, 2024).

Other names
NiV-GNiV-FNipah virus attachment glycoproteinNipah virus fusion glycoproteinNipah virus G proteinNipah virus F proteinNipah virus envelope glycoproteins
02

Mechanism of action

Neutralization of viral entry by blocking the interaction between the G protein and host receptors (Ephrin-B2/B3) or by inhibiting the F protein-mediated membrane fusion process.

03

Biological functions

Viral attachmentMembrane fusionViral entryReceptor bindingHost cell recognition
04

Disease associations

Nipah virus infectionEncephalitisAcute respiratory distress syndromeZoonotic infection
05

Safety considerations

High pathogenicity of the virus (BSL-4 requirement)Rapid clinical progression of diseasePotential for viral escape mutants under selective pressureAntibody-dependent enhancement (theoretical concern for viral glycoproteins)Lack of approved therapeutics for human use
06

Interacting drugs

m102.4

4 more in the full profile.

07

Biomarkers

NiV RNA (RT-PCR)Anti-NiV G antibodies (IgM/IgG)Anti-NiV F antibodies (IgM/IgG)Ephrin-B2 expression levelsEphrin-B3 expression levels

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