Japanese encephalitis virus membrane glycoprotein precursor (prM) (prM)

The Japanese encephalitis virus membrane glycoprotein precursor (prM) is a structural protein essential for the assembly and maturation of the Japanese encephalitis virus (JEV) (UniProt P27395). It acts as a chaperone for the envelope (E) protein, forming a prM-E heterodimer that prevents the E protein from undergoing premature fusion in the acidic environment of the secretory pathway (PubMed: 12134023). During viral egress, prM is cleaved by the host cell protease furin into the mature M protein and a pr peptide, a step necessary for the virus to become infectious (PubMed: 25100874). This protein is a primary component in several JEV vaccines, such as Ixiaro and IMOJEV, which aim to induce neutralizing antibodies against the viral surface (CDC, 2023). While prM itself is not typically the sole target of small-molecule antivirals, its role in maturation makes it a focal point for research into furin inhibitors and therapeutic antibodies (PubMed: 31235547). Understanding prM's function is vital for addressing Japanese encephalitis, a leading cause of viral encephalitis in Asia (WHO, 2022). The transition from prM to M is a hallmark of flavivirus maturation and represents a vulnerable stage in the viral life cycle. Therapeutic strategies often focus on the prM-E complex because it is the most exposed and immunologically relevant structure on the immature virion.

Other names

Pre-membrane proteinprM proteinMembrane protein precursorJEV prM

Vaccine-induced neutralizing antibodies target the prM/E complex to prevent viral entry; experimental furin inhibitors block the cleavage of prM into mature M protein to prevent viral infectivity.