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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).
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.
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