Ebola virus glycoprotein GP1 receptor binding domain (EBOV GP1 RBD)

The Ebola virus glycoprotein GP1 receptor binding domain (RBD) is a critical structural component of the EBOV surface spikes, which are responsible for mediating viral entry into host cells (UniProt, 2023). As part of the GP1 subunit, the RBD is initially shielded by a glycan cap and a mucin-like domain to evade the host immune system during the early stages of infection (Misasi et al., 2016). Upon internalization into the host cell endosome, these protective layers are cleaved by host cathepsins, exposing the RBD (Carette et al., 2011). The exposed RBD then binds to its primary intracellular receptor, Niemann-Pick C1 (NPC1), which is essential for the subsequent GP2-mediated membrane fusion (Carette et al., 2011). This binding event triggers the release of the viral nucleocapsid into the cytoplasm, initiating viral replication. Because of its indispensable role in viral entry, the GP1 RBD is a major target for therapeutic monoclonal antibodies and vaccine design (FDA, 2020). Drugs such as ansuvimab (Ebanga) specifically target this domain to block the NPC1 interaction and neutralize the virus (Misasi et al., 2016). Targeting the RBD is a proven strategy for reducing mortality in patients with Ebola virus disease.

Other names

GP1 RBDEbola virus GP1 subunitEbola virus surface glycoprotein receptor binding domainEBOV GP1 receptor binding domain

Neutralization of viral infectivity by blocking the interaction between the GP1 receptor binding domain and the host endosomal receptor Niemann-Pick C1 (NPC1), thereby preventing membrane fusion and viral entry (Misasi et al., 2016; Carette et al., 2011).