Japanese encephalitis virus pre-membrane protein (prM) (prM)

The Japanese encephalitis virus pre-membrane protein (prM) is a vital structural glycoprotein of the Japanese encephalitis virus, a member of the Flaviviridae family. It functions primarily as a chaperone for the envelope (E) protein, ensuring its proper folding and preventing premature fusion within the host cell's acidic secretory pathway (UniProt: P27395). During viral egress, prM is cleaved by the host cell protease furin into the pr peptide and the mature membrane (M) protein, a transition that renders the virus particle infectious (PubMed: 12134023). As a key component of the viral architecture, prM is a major target for the host immune response and is incorporated into several licensed vaccines, such as IXIARO and IMOJEV, to elicit protective neutralizing antibodies (CDC). Therapeutic strategies targeting prM often focus on inhibiting its cleavage or disrupting its interaction with the E protein to prevent the assembly of functional virions (PubMed: 25135947). Understanding the structural dynamics of prM is essential for developing next-generation countermeasures against Japanese encephalitis, a leading cause of vaccine-preventable encephalitis in Asia.

Other names

prM proteinPre-membrane proteinpMprM/M proteinJapanese encephalitis virus prM

Vaccines targeting the prM protein work by inducing neutralizing antibodies that recognize the prM-E complex, thereby preventing viral attachment and entry into host cells. Experimental therapeutic approaches involve small molecules or antibodies that inhibit the furin-mediated cleavage of prM into the mature M protein, which results in the production of non-infectious, immature viral particles.