Ebola virus glycoprotein (GP) (GP)

The Ebola virus glycoprotein (GP) is the primary surface protein of the Ebola virus and is essential for viral attachment, fusion, and entry into host cells (UniProt P87666). It is expressed as a trimeric spike composed of GP1 and GP2 subunits; GP1 facilitates binding to host receptors like Niemann-Pick C1 (NPC1) in the endosome, while GP2 mediates membrane fusion (PubMed PMC4392352). GP also plays a significant role in immune evasion through the production of a soluble isoform (sGP) that acts as a decoy for antibodies and a "glycan shield" that masks conserved epitopes (PubMed PMC4113787). As the only viral protein exposed on the virion surface, it is the principal target for neutralizing antibodies and vaccine development. Therapeutic monoclonal antibodies, such as those in the Inmazeb cocktail and Ebanga, specifically bind to GP to block viral entry or trigger immune-mediated clearance of infected cells (FDA.gov).

Other names

Envelope glycoproteinGP1/GP2 complexSurface glycoproteinEBOV GPSpike protein

Therapeutic agents targeting the Ebola virus glycoprotein primarily function by binding to specific epitopes on the GP1 or GP2 subunits. This binding neutralizes the virus by sterically hindering the interaction between GP1 and the host cell receptor Niemann-Pick C1 (NPC1) or by preventing the pH-dependent conformational changes in GP2 required for fusion of the viral envelope with the endosomal membrane (PubMed PMC7566845). Additionally, some antibodies may facilitate the clearance of the virus or infected cells through Fc-mediated effector functions like antibody-dependent cellular cytotoxicity (ADCC) (PubMed PMC6069510).