Structural polyprotein (Western equine encephalitis virus) (WEEV Structural Polyprotein)

The Western equine encephalitis virus (WEEV) structural polyprotein is a large precursor molecule that is enzymatically processed into the essential components of the viral particle, including the capsid protein and the envelope glycoproteins E1 and E2 [1, 15]. The E2 glycoprotein is primarily responsible for viral attachment to target host cells by binding to receptors such as PCDH10, while the E1 glycoprotein acts as a class II fusion protein that mediates the entry of the viral genome into the cytoplasm following endocytosis [1, 4]. WEEV is a highly infectious alphavirus that causes Western equine encephalitis, a disease characterized by fever, headache, and potentially fatal central nervous system inflammation in both humans and horses [3, 9, 16]. The envelope proteins are the primary targets for the host's immune response, making them the focus of vaccine design, including DNA-based and recombinant subunit vaccines [2, 11]. Currently, there are no approved antiviral therapies specifically for WEEV, though research into small molecules like Nitazoxanide has shown that inhibiting host protein disulfide isomerases can prevent the proper folding of the E1 glycoprotein, thereby reducing viral infectivity [12]. Neutralizing monoclonal antibodies targeting specific epitopes on the E2 protein are also being developed as potential prophylactic and therapeutic agents [5].

Other names

Western equine encephalitis virus envelope polyproteinWEEV structural polyproteinWEEV envelope glycoproteinsp130 structural polyproteinE1-E2-E3-6K-Capsid polyproteinWEEV spike protein complex

Neutralization of viral entry, inhibition of membrane fusion, inhibition of protein disulfide isomerase (PDI)-mediated protein folding, and prevention of viral assembly.