Ebola virus Zaire species glycoprotein (EBOV GP)

The Ebola virus Zaire species glycoprotein (EBOV GP) is the sole protein expressed on the surface of the Ebola virus virion and is essential for the viral life cycle. It is synthesized as a precursor (GP0) that is cleaved by host furin into two subunits, GP1 and GP2, which remain linked by a disulfide bond to form a trimeric spike. GP1 is responsible for attachment to host cell surface receptors and binding to the endosomal receptor Niemann-Pick C1 (NPC1), while GP2 mediates the fusion of the viral and host endosomal membranes. Because it is the primary target for neutralizing antibodies, EBOV GP is the central component of current vaccines, such as Ervebo, and the target for FDA-approved monoclonal antibody therapies like Inmazeb (atoltivimab, maftivimab, and odesivimab) and Ebanga (ansuvimab). Beyond its role in entry, the virus also produces a secreted dimeric form (sGP) that may act as an immune decoy to subvert the host's antibody response.

Other names

Envelope glycoproteinGP1GP2sGPssGPGP1,2

Monoclonal antibodies bind to specific epitopes on the GP1 or GP2 subunits to neutralize the virus by blocking attachment to host receptors (like NPC1), inhibiting the conformational changes required for membrane fusion, or signaling for immune-mediated clearance of infected cells.