Japanese encephalitis virus envelope protein and premembrane protein (JEV E and prM proteins)

The **Japanese encephalitis virus envelope protein (E) and premembrane protein (prM)** are two essential surface glycoproteins of the Japanese encephalitis virus (JEV), a member of the Flaviviridae family. The E protein (~500 amino acids) is responsible for viral **attachment to cellular receptors, membrane fusion, hemagglutination, receptor binding, and induction of neutralizing immune responses**[1][2][5]. It possesses three functional domains and forms homodimers on the virion surface, directly mediating both cell entry and the major antigenic responses generated during infection[2][3]. The **prM protein** acts as a chaperone for proper folding of E during virion assembly and is cleaved to membrane (M) protein on maturation[6][5]. Both proteins are principal targets for vaccine and therapeutic antibody development[1][2][3]. Mutations in domain III of the E protein can affect neutralization and neurovirulence, and targeting E with monoclonal antibodies is a central strategy for passive immunotherapy and vaccine development[1][2]. The JEV E protein is also used as a biomarker for diagnosing infection and immunity.

Other names

Japanese encephalitis virus E proteinJapanese encephalitis virus prM proteinJEV E proteinJEV premembrane proteinJEV prM

Inhibition of viral entry by blocking E protein-mediated attachment and membrane fusion; Neutralization of virus via epitope targeting on E protein