Glycoprotein/GP His Tag Protein, Ebola Virus-Q7T9D9

The fourth gene of the EBOV genome encodes a 16-kDa envelope-attached glycoprotein (GP) and an 11-kDa secreted glycoprotein (sGP), both sharing a 295-residue N-terminus but differing in C-terminal sequences. GP, a class I fusion protein forming trimers on the viral surface, is critical for virus entry and attachment. Mature GP is a disulfide-linked heterodimer of GP1 and GP2, produced by furin cleavage of the precursor (pre-GP) during assembly. GP1 contains a mucin domain and receptor-binding domain (RBD), while GP2 includes a fusion peptide, heptad-repeat region, transmembrane domain, and cytoplasmic tail. The RBD mediates interaction with cellular receptors such as DC-SIGN, TIM-1, NPC1, and others, with TIM-1 and NPC1 essential for entry. The mucin domain enhances attachment to hMGL and shields neutralization epitopes, aiding immune evasion. During membrane fusion, GP2 undergoes conformational changes that insert the fusion loop into the host membrane, facilitating release of the viral nucleocapsid into the cytoplasm.