Zaire ebolavirus glycoprotein - glycan cap region (EBOV GP glycan cap)

The glycan cap is a critical structural domain of the Zaire ebolavirus glycoprotein (GP), specifically located within the GP1 subunit. It is characterized by dense N-linked glycosylation that forms a 'glycan shield,' protecting the underlying receptor-binding domain (RBD) from host immune detection (PubMed: 29434354, UniProt: P87666). During the viral entry process, the virus is internalized into host endosomes where the glycan cap and the adjacent mucin-like domain must be proteolytically removed by host cathepsins B and L. This cleavage exposes the RBD, allowing it to bind to the endosomal receptor Niemann-Pick C1 (NPC1), which is essential for membrane fusion and viral escape into the cytoplasm (PubMed: 30531979). Due to its prominent position on the viral surface and its role in regulating entry, the glycan cap is a primary target for therapeutic monoclonal antibodies. Drugs such as Odesivimab (a component of Inmazeb) and 13C6 (a component of ZMapp) bind to this region to neutralize the virus or prevent the necessary enzymatic processing, thereby halting the infection cycle (FDA: Inmazeb Label, Science 2016).

Other names

Ebola virus glycoprotein glycan capGP1 glycan capEBOV GP1 glycan cap domainZaire ebolavirus GP glycan cap

Neutralization of viral particles and inhibition of cathepsin-mediated proteolytic cleavage required for receptor binding domain exposure.