Ebola virus envelope glycoprotein (EBOV-GP)

The Ebola virus envelope glycoprotein (GP) is the sole viral protein present on the surface of the virion and is essential for mediating entry into host cells. It plays a critical role in both attachment to host cell receptors and catalyzing membrane fusion, which allows viral RNA to enter the cytoplasm and initiate infection. The mature GP exists as a trimer of heterodimers, each composed of two subunits: GP1 and GP2. GP1 is responsible for receptor binding and contains a glycan cap and mucin-like domain that shield conserved regions from immune recognition. GP2 functions as the membrane fusion subunit. Upon activation (triggered by low pH in endosomes), it undergoes conformational changes exposing its hydrophobic fusion loop, facilitating merger with host membranes. The extensive glycosylation—especially within the mucin-like domain—shields key epitopes from neutralizing antibodies, contributing to immune evasion. It also downregulates expression of several integrins on infected cells, potentially disrupting vascular integrity and interacts with TLR4 on monocytes/macrophages stimulating inflammatory responses. Because it is exposed on virions throughout infection cycles—and due to its essential roles—the Ebola virus envelope glycoprotein is a primary target for neutralizing antibodies, central to vaccine design and a focus for small-molecule inhibitors aimed at blocking attachment or fusion steps.

Other names

Ebola GPGP1GP2

Attachment inhibition; Fusion inhibition; Neutralization