Ebolavirus glycoprotein GP1-GP2 interface base epitope (EBOV GP)

The Ebolavirus glycoprotein (GP) is the primary surface protein of the virus, organized as a trimer of GP1-GP2 heterodimers that mediates host cell attachment, endosomal entry, and membrane fusion. The GP1-GP2 interface, specifically the base region encompassing the internal fusion loop (IFL), is a highly conserved and critical functional domain across various ebolavirus species, including Ebola (EBOV), Sudan (SUDV), and Bundibugyo (BDBV) (Wec et al., 2017, Science). This epitope is essential for the conformational rearrangements required to trigger the fusion of the viral envelope with the host endosomal membrane after binding to the Niemann-Pick C1 (NPC1) receptor (Bornholdt et al., 2016, Science). Because this region is structurally constrained to maintain fusion competency, it serves as a site of vulnerability for broad-spectrum neutralizing antibodies. Therapeutic agents targeting this epitope, such as the monoclonal antibodies ADI-15878 and ADI-15742, work by stabilizing the pre-fusion conformation or sterically hindering the fusion process, thereby preventing viral infection across multiple ebolavirus species (UniProt P87666).

Other names

Ebolavirus GP1-GP2 interfaceGP base epitopeInternal fusion loop (IFL) epitopeEbolavirus surface glycoproteinGP1/GP2 heterodimer interface

Neutralization of viral entry by inhibiting membrane fusion and preventing the conformational change of the GP2 subunit.