Ebola virus glycoprotein GP2 stalk-membrane proximal external region (EBOV GP2 stalk-MPER)

The Ebola virus glycoprotein (GP) is a class I fusion protein that mediates viral entry into host cells. It exists as a trimer of GP1 and GP2 heterodimers, where GP1 is responsible for receptor binding and GP2 facilitates membrane fusion (Bornholdt et al., 2016, Science 351:1078). The stalk and membrane proximal external region (MPER) of GP2 are located near the viral membrane and play a crucial role in the conformational changes that drive the fusion of the viral envelope with the host endosomal membrane (Wec et al., 2017, Science 357:1034). This region is highly conserved among various ebolaviruses, making it an attractive target for the development of broadly neutralizing antibodies (bnAbs) and universal vaccines (King et al., 2019, Nature Microbiology 4:1304). Drugs or antibodies targeting the GP2 stalk-MPER typically function by sterically hindering the transition from the pre-fusion to the post-fusion state, thereby blocking viral infection (UniProtKB - P87666). Because of its conservation, targeting this site may provide protection against multiple species within the Ebolavirus genus.

Other names

Ebola virus GP2 stalkEbola virus GP2 MPEREBOV GP2 membrane proximal external regionGP2 stalk-MPER domain

Inhibition of the conformational transition from pre-fusion to post-fusion states of the GP2 subunit, thereby blocking the fusion of the viral envelope with the host endosomal membrane.