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Western equine encephalitis virus (WEEV) glycoproteins, primarily E1 and E2, are essential structural proteins located on the surface of the viral envelope [1]. The E2 glycoprotein is responsible for mediating attachment to host cell receptors, while the E1 glycoprotein facilitates pH-dependent membrane fusion within the endosome to release the viral genome into the cytoplasm [2]. As the most exposed components of the virion, these glycoproteins are the primary targets for neutralizing antibodies and are the focus of vaccine design, including DNA, subunit, and viral-like particle (VLP) platforms [3]. WEEV is an alphavirus that can cause severe neurological disease and encephalitis in humans and horses, primarily transmitted by mosquitoes [4]. While no specific antiviral drugs or human vaccines are currently FDA-approved, research into monoclonal antibodies targeting specific epitopes on the E2/E1 heterodimer shows promise for post-exposure prophylaxis and treatment [5]. (Sources: [1] UniProt P03316; [2] PMID: 25122783; [3] PMID: 19128758; [4] CDC; [5] PMID: 24501067)
Neutralization of viral entry by blocking receptor binding or inhibiting pH-dependent membrane fusion.
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