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The Japanese encephalitis virus (JEV) envelope glycoprotein E is the major structural protein on the surface of the JEV virion and serves as the primary target for the host immune response (UniProt P27395). It mediates critical steps in the viral life cycle, including attachment to host cell receptors and subsequent membrane fusion within the endosome (PubMed: 23152523). The protein is organized into three distinct structural domains (DI, DII, and DIII), with DIII being particularly important for receptor binding and containing many potent neutralizing epitopes (PubMed: 22438551). As the principal antigen for all currently licensed Japanese encephalitis vaccines, such as IXIARO and IMOJEV, the E protein is essential for inducing protective neutralizing antibodies (CDC, 2023). Therapeutic strategies targeting the E protein include the development of monoclonal antibodies that block viral entry and small-molecule inhibitors designed to prevent the conformational changes necessary for fusion (PubMed: 25855244). Understanding the specific epitopes on the virion surface is crucial for designing next-generation vaccines and diagnostic tools to combat Japanese encephalitis.
Neutralization of viral infectivity by blocking receptor binding or preventing the pH-dependent conformational change required for membrane fusion.
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