Zaire ebolavirus glycoprotein (GP1,2) (EBOV GP)

The Zaire ebolavirus glycoprotein (GP) is the sole protein expressed on the viral surface and is critical for attachment, receptor binding, and membrane fusion (UniProt: P87666). It is synthesized as a GP0 precursor and cleaved by host furin into GP1 and GP2 subunits, which remain linked by a disulfide bond to form a trimeric spike (Misasi et al., Science, 2016). GP1 contains the receptor-binding domain (RBD) that interacts with the host endosomal receptor Niemann-Pick C1 (NPC1) following proteolytic processing of the glycan cap (Carette et al., Nature, 2011). Ansuvimab (mAb114) is a human monoclonal antibody that binds to the RBD of GP1, specifically targeting an epitope that remains accessible even after the glycan cap is removed (Corti et al., Science, 2016). By occupying this site, ansuvimab prevents the GP-NPC1 interaction, thereby neutralizing the virus and preventing host cell entry (FDA, Ebanga Prescribing Information, 2020). This target is essential for treating Ebola virus disease, as it directly inhibits the viral life cycle and prevents the spread of infection within the host.

Other names

Ebola virus glycoproteinGP1/GP2 complexEnvelope glycoproteinSpike glycoproteinZaire ebolavirus GPmAb114 epitope

Ansuvimab is a recombinant human monoclonal antibody that binds to the receptor-binding domain (RBD) of the Zaire ebolavirus glycoprotein GP1 subunit. This binding prevents the interaction between the viral glycoprotein and the host cell receptor Niemann-Pick C1 (NPC1), which is required for viral entry into the host cell cytoplasm (FDA, 2020; Misasi et al., 2016).