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The Nipah virus attachment glycoprotein G (NiV-G) is a critical type II transmembrane protein located on the surface of the Nipah virus envelope (UniProt: P0C1C7). It mediates viral pathogenesis by facilitating the attachment of the virus to host cells through high-affinity interactions with the receptors Ephrin-B2 and Ephrin-B3, which are prevalent in endothelial and neuronal tissues (PubMed: 16007097). This binding event is the essential first step of the viral entry process, as it triggers a conformational change in the associated fusion (F) protein to merge the viral and host membranes (PubMed: 21715493). Due to its accessibility and indispensable role in infection, NiV-G is the primary target for the development of neutralizing monoclonal antibodies and vaccine candidates (PubMed: 23115215). For example, the monoclonal antibody m102.4 specifically targets the receptor-binding domain of NiV-G to block viral entry. Therapeutic interventions targeting NiV-G are vital for addressing the high mortality rates associated with Nipah virus-induced encephalitis and severe respiratory distress (WHO, 2024).
Neutralization of viral entry by binding to the receptor-binding domain (RBD) of the G protein, thereby preventing its interaction with host Ephrin-B2 and Ephrin-B3 receptors (PubMed: 23115215).
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