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The **Japanese encephalitis virus envelope glycoprotein** is the principal structural protein on the surface of the Japanese encephalitis virus (JEV), a flavivirus. This ~53-60 kDa glycoprotein, commonly known as the E protein, mediates viral attachment, membrane fusion, and entry into host cells through three functional domains (EDI, EDII, and EDIII)[1][2][4][6]. Domain I stabilizes the overall E protein structure; Domain II contains the fusion loop necessary for membrane fusion under acidic endosomal conditions; and Domain III is immunoglobulin-like, involved in receptor binding and a key target for neutralizing antibodies[1][2][3][6]. The E protein is critical for viral infectivity, tissue tropism, neurovirulence, and is a major target for therapeutic vaccine and antibody development. The E protein’s structural features, glycosylation, and conserved motifs determine its role in pathogenesis, especially neuroinvasion and neurovirulence, and it is utilized as a biomarker for infection and for monitoring immune responses to vaccination[1][2][3].
Inhibition of viral entry (by preventing attachment or fusion, e.g., neutralizing antibodies). Immune blockade of critical epitopes to prevent neuroinvasion and cell infection.
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