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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.).
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.).
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