West Nile virus pre-membrane protein (prM protein)

The **West Nile virus pre-membrane protein (prM)** is a key structural protein of the West Nile virus, a member of the *Flaviviridae* family. The prM protein functions as a chaperone for the viral envelope (E) protein, ensuring its correct folding and protecting the fusion domain from premature activation during passage through the secretory pathway. During virion maturation, prM is cleaved by the host protease furin in response to acidic pH, releasing the ‘pr’ peptide and allowing the virus to become infectious. Mutations in specific prM residues affect viral particle secretion and virulence, highlighting prM’s critical role in the West Nile virus life cycle and pathogenicity[1][2]. While not a classical drug target like a human receptor or enzyme, prM is considered a potential **therapeutic target** to block viral maturation and infectivity. Notably, prM protein acts with the envelope (E) protein in immature virions and is crucial for protecting the E protein’s fusion peptide until the correct maturation stage[2]. The cleavage of prM by furin in the trans-Golgi network is required for production of mature, infectious West Nile virus[2]. Residue changes in prM can modulate virus secretion and virulence, as shown in strain comparisons[1].

Other names

prM proteinWNV prMWest Nile virus prMpreM protein

Acidotropic agents (like ammonium chloride) prevent maturation by blocking furin-mediated cleavage of prM, resulting in noninfectious viral particles