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The Venezuelan equine encephalitis virus envelope glycoprotein E1 is a transmembrane glycoprotein that forms heterodimers with E2 on the viral surface, organized into icosahedral spikes on the lipid envelope. E1 mediates low-pH-induced membrane fusion in endosomes by dissociating from E2, exposing its fusion loop, and forming homotrimers that drive viral-endosomal membrane merger for nucleocapsid release. It features a surface-exposed N-linked glycan at Asn134, a buried E2-associated glycan site, and interacts with entry receptors like LDLRAD3 via E1-E2 clefts. E1 contributes to assembly by linking the envelope to the nucleocapsid via transmembrane helices and cytoplasmic tails, with structures resolved by cryo-EM at 4.4 Å for strains like TC-83.
Neutralizing antibodies bind E1 fusion loop or E1-E2 interfaces to block attachment and fusion
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