West Nile virus premembrane protein and envelope glycoprotein E (WNV prM/E)

The West Nile virus (WNV) premembrane (prM) and envelope (E) proteins are essential structural components that mediate the virus's ability to infect host cells. The E protein is the primary surface protein involved in attachment to host receptors and subsequent membrane fusion, while the prM protein serves as a chaperone that protects the E protein from premature fusion during the assembly process (PMID: 18483444). Upon maturation, prM is cleaved by the host protease furin, rendering the virus infectious (UniProt: P06935). Because these proteins are exposed on the virion surface, they are the principal targets for neutralizing antibodies and are the primary antigens used in the development of WNV vaccines (PMID: 16188990). Targeting these proteins aims to prevent viral entry and dissemination, thereby reducing the risk of severe neurological complications such as encephalitis and meningitis (PMID: 15650267). Therapeutic strategies often involve monoclonal antibodies, such as E16, which bind to the E protein to block viral attachment or fusion (PMID: 16188990).

Other names

prM proteinEnvelope protein EWNV E proteinWNV prMStructural protein prM-E

Neutralization of viral infectivity by blocking receptor binding or inhibiting pH-dependent membrane fusion within the endosome.