Ebola virus glycoprotein GP2 fusion loop (EBOV GP2 FL)

The Ebola virus glycoprotein (GP) is the sole protein on the viral surface, existing as a trimer of GP1-GP2 heterodimers that mediates attachment and entry into host cells (UniProt P87666). The GP2 subunit contains a highly conserved hydrophobic region known as the fusion loop (FL), which is essential for the fusion of the viral envelope with the host endosomal membrane (Misasi & Sullivan, 2021). During the infection process, the GP1 subunit is cleaved by host endosomal proteases (cathepsins), exposing the GP2 fusion loop. This exposure allows the loop to insert into the host membrane, triggering a conformational change that facilitates viral entry into the cytoplasm. Because the fusion loop sequence is highly conserved across different ebolavirus species, it is a primary target for broadly neutralizing antibodies (bNAbs) such as ADI-15878 and CA45, which can neutralize multiple strains of the virus (Wec et al., 2017; Zhao et al., 2017). These antibodies typically function by preventing the structural transitions of GP2 required for membrane fusion.

Other names

Ebola virus GP2 fusion peptideGP2 internal fusion loopEBOV GP2 IFLEbolavirus GP2 fusion loop epitopeGP2-FL

Neutralization of viral infectivity by binding to the conserved fusion loop, thereby preventing the conformational transition of GP2 and the subsequent fusion of the viral envelope with the host endosomal membrane (Wec et al., 2017; Zhao et al., 2017).