Target intelligence / Profile preview

Hendra virus attachment glycoprotein (HeV-G) (HeV-G)

Target
HeV-G
Molecular classification
Viral surface protein, Type II integral membrane protein, Paramyxovirus attachment glycoprotein, Six-bladed beta-propeller protein
01

Overview

The Hendra virus attachment glycoprotein (HeV-G) is a critical type II transmembrane surface protein of the Hendra virus, a highly pathogenic zoonotic paramyxovirus (UniProt, PMC3516248). It plays a primary role in viral entry by mediating the attachment of the virion to host cell receptors, specifically ephrin-B2 and ephrin-B3 (PMC1317515). Upon receptor binding, the globular head of HeV-G undergoes a conformational change that triggers the associated fusion (F) protein to execute membrane fusion, allowing the viral genome to enter the host cell (PubMed 23115312). Because of its essential role in infection and its exposure on the viral surface, HeV-G is a major target for neutralizing antibodies and vaccine development (PMC6819283). The most notable therapeutic agent is the human monoclonal antibody m102.4, which potently neutralizes the virus by blocking the receptor-binding site on HeV-G (PLOS Pathogens 2013). Efforts to target this protein are crucial for managing outbreaks of Hendra virus, which causes severe respiratory distress and fatal encephalitis in humans and horses (Wikipedia, NIH).

Other names
Glycoprotein GHeV G proteinHendra virus attachment proteinHenipavirus attachment glycoproteinReceptor-binding proteinRBP
02

Mechanism of action

Neutralization of viral infection by blocking the receptor-binding domain of the G protein, which prevents its interaction with host ephrin-B2 and ephrin-B3 receptors and inhibits the subsequent triggering of the fusion (F) protein required for viral-cell membrane fusion and entry.

03

Biological functions

Viral attachment to host cellHost cell surface receptor bindingTriggering of viral fusion protein FSymbiont entry into host cellOligomerization
04

Disease associations

Hendra virus infectionSevere respiratory diseaseEncephalitisZoonotic infection
05

Safety considerations

High viral pathogenicity (Biosafety Level 4 agent)Potential for viral escape mutations in the G proteinLimited human clinical safety data for targeted therapeuticsSevere neurological sequelae in survivors
06

Interacting drugs

m102.4

3 more in the full profile.

07

Biomarkers

Anti-HeV-G antibodiesHendra virus RNAViral antigen presenceSyncytia formation

Beyond the preview

Go deeper on Hendra virus attachment glycoprotein (HeV-G) (HeV-G).

Explore the evidence, development activity, and competitive landscape with Gosset’s full data platform.

Drug pipeline

Full profile access

Explore the programs pursuing this target and their development progress.

  • Drug candidates
  • Developers
  • Development stage

Clinical trials

Full profile access

Follow the clinical studies evaluating therapies directed at this target.

  • Trial design
  • Status
  • Readouts

Competitive landscape

Full profile access

Compare approaches across drug candidates, modalities, and indications.

  • Programs
  • Modalities
  • Indications

Literature & evidence

Full profile access

Investigate the research and source evidence behind target biology and development.

  • Publications
  • Sources
  • Analysis

Patents

Full profile access

Explore patent activity around therapies and technologies addressing this target.

  • Patents
  • Assignees
  • Technologies

Research & analysis

Full profile access

Connect target biology, drug development, and emerging evidence in your research.

  • Biology
  • Development news
  • Analysis

Bring the full picture into focus.

See how Gosset can support your research on Hendra virus attachment glycoprotein (HeV-G) (HeV-G).

Explore the full profile

Gosset Free

Get started with Gosset.

Enter your work email and we’ll be in touch with next steps.

Work email preferred.

Book a call