Ebola virus glycoprotein (EBOV GP) (EBOV GP)

The Ebola virus glycoprotein (EBOV GP) is the primary surface protein of the Ebola virus and serves as the essential mediator for viral attachment, fusion, and entry into host cells (UniProt P87666). It is a class I fusion protein synthesized as a GP0 precursor, which is subsequently cleaved by furin into GP1 and GP2 subunits that remain disulfide-linked. GP1 facilitates binding to host cell surface lectins and, following endosomal proteolysis, to the intracellular receptor Niemann-Pick C1 (NPC1), while GP2 mediates the fusion of viral and host membranes (PubMed: 21866102). As the only protein on the virion surface, it is the sole target for neutralizing antibodies and the primary antigen used in vaccine development, such as the Ervebo vaccine (PubMed: 30531979). Therapeutic monoclonal antibodies, including those in the Inmazeb cocktail and Ansuvimab, target specific conserved epitopes on GP to block viral entry or recruit immune effector cells (FDA, 2020). Understanding the interaction between B-cell receptors and GP is crucial for developing long-lasting immunity and broad-spectrum therapeutics against various Ebolavirus species.

Other names

Envelope glycoproteinGPGP1/GP2 subunitEbola virus surface glycoprotein

Neutralization of viral entry by blocking attachment to host receptors (e.g., NPC1) or preventing membrane fusion; induction of antibody-dependent cellular cytotoxicity (ADCC).