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The glycoprotein (GP) from Zaire ebolavirus is the sole surface protein on Ebola virions and is critical for viral attachment to host cell receptors and subsequent fusion of viral and host membranes[1][3][4][7]. The mature GP exists as a trimer of GP1/GP2 heterodimers: GP1 mediates receptor binding and has a glycan cap and mucin-like domain that confer immune evasion, while GP2 is responsible for fusion and entry, featuring a fusion peptide and heptad repeat regions[4][6]. The GP gene also encodes a soluble glycoprotein isoform (sGP) released during infection, which may modulate host responses and act as a decoy for antibodies[2]. GP is the principal target for neutralizing antibody therapies and vaccine strategies, but structural variability and immune evasion mechanisms present ongoing therapeutic challenges[1][2][3][7].
Neutralizing antibodies block GP-mediated attachment or fusion by binding GP1/GP2 epitope (e.g., KZ52). Entry inhibitors bind GP, preventing fusion of viral and cellular membranes (e.g., toremifene). Soluble glycoprotein (sGP) may sponge immune response.
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