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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).
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.
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