Eastern equine encephalitis virus E2 envelope glycoprotein (EEEV E2) (EEEV E2)

The Eastern equine encephalitis virus (EEEV) E2 envelope glycoprotein is a major surface component of the EEEV virion, organized into 80 trimeric spikes consisting of E1-E2 heterodimers (UniProt: P0E9L5). It is primarily responsible for mediating viral attachment to host cell receptors, such as the very-low-density lipoprotein receptor (VLDLR), and initiating the process of receptor-mediated endocytosis (Hundhausen et al., 2023). Once inside the endosome, the acidic environment triggers a dissociation of the E1-E2 complex, allowing the E1 protein to facilitate membrane fusion and release the viral genome into the cytoplasm (Voss et al., 2010). As the most prominent surface antigen, E2 is the principal target for the host's neutralizing antibody response and is the primary focus for the development of vaccines and therapeutic monoclonal antibodies like EEEV-33 and EEEV-143 (Adams et al., 2021). Given that EEEV is a highly pathogenic alphavirus with a mortality rate of up to 70% in humans, targeting the E2 protein to prevent neuroinvasion and systemic infection is a critical area of biodefense and public health research (CDC, 2024).

Other names

E2 glycoproteinSpike glycoprotein E2EEEV E2 proteinEnvelope protein E2

Neutralization of viral entry by blocking receptor binding sites on the E2 protein or stabilizing the E1-E2 heterodimer to prevent the pH-induced conformational changes necessary for membrane fusion (Adams et al., 2021; Voss et al., 2010).