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The Nipah virus attachment glycoprotein G (NiV-G) is a critical surface protein of the Nipah virus, a highly pathogenic zoonotic paramyxovirus (UniProt: P0C6Q4). It functions as a type II transmembrane protein that mediates viral entry by binding to highly conserved host cell receptors, specifically Ephrin-B2 and Ephrin-B3, which are prevalent in endothelial and neuronal tissues (Aguilar et al., J Virol, 2006). This binding event triggers a conformational change in the adjacent fusion (F) protein, facilitating the merger of the viral envelope with the host cell membrane. Because NiV-G is the primary target for neutralizing antibodies, it is the central focus for vaccine development and therapeutic interventions. Experimental monoclonal antibodies like m102.4 have demonstrated the ability to neutralize the virus by sterically blocking the receptor-binding domain of NiV-G, providing a potential treatment for this often-fatal infection (Bossart et al., Sci Transl Med, 2011).
Neutralization of viral entry by blocking the interaction between the G protein and host receptors Ephrin-B2 or Ephrin-B3, thereby preventing viral attachment and subsequent fusion protein activation.
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