Ebola virus glycoprotein GP1 core (EBOV GP1 core)

The Ebola virus glycoprotein GP1 core is the central receptor-binding component of the Ebola virus (EBOV) envelope glycoprotein complex [2, 11]. It is generated within the host cell's endosomal compartment through the proteolytic cleavage of the full-length GP1 subunit by host cathepsins, which removes the heavily glycosylated glycan cap and mucin-like domains [2, 7]. This "priming" process exposes the GP1 core, enabling it to bind directly to the endosomal receptor Niemann-Pick C1 (NPC1) [1, 6]. This binding event is a critical prerequisite for the conformational changes in the GP2 subunit that drive the fusion of the viral and endosomal membranes, allowing the viral genome to enter the host cytoplasm [2, 6]. Given its indispensable role in viral entry, the GP1 core is a major target for therapeutic development [4, 9]. Monoclonal antibodies such as ansuvimab and the components of the Inmazeb cocktail (atoltivimab, maftivimab, and odesivimab) bind to the GP1 core or its vicinity to neutralize the virus [6, 9]. These therapies effectively block receptor engagement or inhibit the fusion process, significantly improving survival rates in patients with Ebola virus disease [9].

Other names

Primed GP119-kDa GP1GP1 receptor-binding domainGP1 core subunitEBOV GP1 core

Neutralization of the virus by blocking the interaction between the GP1 core and the host receptor NPC1, or by preventing the conformational changes required for membrane fusion.