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The **Japanese encephalitis virus precursor membrane (prM) and envelope (E) protein antigens** are key structural proteins of JEV, a flavivirus. The **E protein** facilitates viral attachment, entry, and membrane fusion with the host cell, and is the principal target for neutralizing antibodies, making it the main antigen for vaccine design[2][4][6]. The **prM protein** acts as a chaperone that protects E during assembly and prevents premature fusion; it is cleaved by host furin to form the mature membrane (M) protein, a critical step for the production of infectious viral particles[3][5][7]. Together, prM and E mediate critical functions in viral replication, assembly, maturation, host immune recognition, and pathogenesis, including neurovirulence—the ability to invade and damage neuronal tissue, the hallmark of Japanese encephalitis disease[1][4][5]. These antigens are essential targets for vaccine development, diagnostic assays, and potential antiviral intervention strategies.
Inhibition of prM cleavage by furin disrupts production of mature, infectious virus[1][3]; Neutralizing antibodies block E-mediated viral entry and fusion[2][4]; Mutations or genetic engineering of prM/E can attenuate neurovirulence for vaccine development[4][5]
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