Japanese encephalitis virus premembrane protein (prM) (prM)

The Japanese encephalitis virus (JEV) premembrane protein (prM) is a critical structural component of the JEV virion, belonging to the Flaviviridae family (UniProt P27395). Its primary biological role is to act as a molecular chaperone for the Envelope (E) protein, ensuring its proper folding and preventing premature, low-pH-induced fusion during the virus's transit through the host cell's secretory pathway (PubMed: 12134023). During the final stages of viral maturation, the prM protein is cleaved by the host cell protease furin into a "pr" peptide and a mature "M" protein, a step essential for the virus to become fully infectious (PubMed: 25101570). In the context of disease, JEV is a leading cause of vaccine-preventable encephalitis in Asia, and the prM protein is a major target for the host immune response. Most current JEV vaccines, including inactivated (IXIARO) and live-attenuated (IMOJEV) versions, utilize the prM and E proteins to elicit neutralizing antibodies. Therapeutic strategies targeting prM focus on inhibiting its cleavage or using it as an antigen in vaccine development to prevent viral entry and replication.

Other names

prM proteinPremembrane proteinprM/M proteinJEV prM

Induction of neutralizing antibodies that target the prM-E complex to block viral attachment and entry; inhibition of the furin-mediated cleavage of prM to M, which prevents the formation of mature, infectious virions.