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Envelope glycoproteins Gn and Gc are surface-exposed viral proteins that, as heterodimers, form spike complexes essential for virus assembly, structure, and infectivity. The Gn protein serves mainly in receptor recognition and binding, while Gc is a class II fusion protein that undergoes conformational changes to mediate fusion between the viral and endosomal membranes. These proteins assemble into tetrameric spikes and a surface lattice on the viral envelope. Both are derived from a single polyprotein precursor encoded in the viral M segment and cleaved by host signal peptidases. Their surface-exposed regions are highly immunogenic, making them primary targets for neutralizing antibodies and candidate vaccines, but they can evade immunity via conformational shielding, glycosylation, and structural plasticity. Blocking Gn or Gc function prevents viral entry and infection.
Neutralization of viral entry via antibody binding; Inhibition of receptor binding and conformational changes necessary for membrane fusion
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