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Venezuelan equine encephalitis virus (VEEV) glycoproteins, specifically E1 and E2, are the major structural proteins forming the spikes on the viral envelope (Voss et al., Nature 2010). The E2 glycoprotein is primarily responsible for receptor binding, including the host receptor LDLRAD3, while the E1 glycoprotein facilitates pH-triggered membrane fusion within host endosomes (Ma et al., Nature 2020). These proteins are the principal targets for neutralizing antibodies and are the focus of vaccine development efforts to prevent VEEV infection, which can lead to severe neurological disease and death in humans and equines (Pittman et al., Vaccine 1996). Therapeutic strategies often involve monoclonal antibodies that bind to specific epitopes on E2 to block viral attachment or entry (Hunt et al., Journal of Virology 2006). The E1 and E2 proteins are synthesized as a polyprotein precursor that is cleaved by host proteases during maturation (UniProt P03316). Understanding the structural biology of these glycoproteins is essential for designing effective countermeasures against this highly infectious alphavirus.
Neutralization of viral particles by blocking receptor binding or preventing pH-dependent membrane fusion.
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