West Nile virus envelope protein precursor membrane and envelope protein (WNV prM and E proteins)

The West Nile virus envelope protein precursor membrane and envelope protein (abbreviated "prM and E proteins") are the two main structural glycoproteins forming the viral surface and driving the infectivity and assembly of West Nile virus (WNV), a pathogenic Flavivirus. The *prM* protein acts as a chaperone for proper folding and protection of the *E* protein during virus assembly. During virion maturation, prM is cleaved by the host protease furin to produce the mature membrane (M) protein, enabling viral infectivity[6][4]. The *E* protein is an approximately 53–60 kDa glycoprotein with three domains: DI (central β-barrel), DII (fusion loop), and DIII (immunoglobulin-like, receptor-binding domain)[1][4][7]. *E* is responsible for binding to host cell surface receptors and mediating subsequent membrane fusion, making it the dominant antigenic determinant and principal target of host neutralizing antibodies[1][4][7]. Both prM and E are N-glycosylated, a modification that influences viral infectivity, host tropism, viral particle release, and neuroinvasiveness[2][3][4]. The glycosylation of E at N154 is particularly important for virulence and infection in vertebrates, and varies between strains[2][3][4][7]. Recombinant expression of prM and E leads to secretion of subviral particles (SVPs) that are antigenically and morphologically similar to infectious WNV, providing the basis for vaccine design and serodiagnosis[7]. Mutations affecting glycosylation or domain structure of these proteins can modulate pathogenicity and immune recognition[4][7]. Overall, WNV prM and E proteins are critical therapeutic and vaccine targets due to their essential roles in viral entry, infectivity, and the elicitation of protective immune responses[7][4][6].

Other names

prM proteinprecursor membrane proteinpremembrane proteinE proteinenvelope glycoprotein

Neutralizing antibodies block E protein fusion or receptor binding Entry inhibitors (experimental) may block E-mediated membrane fusion