Ebolavirus glycoprotein 1 glycan cap region

The Ebolavirus glycan cap region is a distinct subdomain located within the GP1 subunit of the Ebolavirus envelope glycoprotein (GP). GP is the only surface protein of ebolaviruses, mediating both host cell attachment and entry. The glycan cap, consisting of residues approximately 227–310, forms an α/β dome-like structure on top of the GP1 head region and contains several N-linked glycosylation sites (notably N228, N238, N257, and N268 in Zaire ebolavirus). This region contributes to the extensive glycan shield that cloaks key epitopes from the host immune system, promoting immune evasion and reducing the effectiveness of neutralizing antibodies. The heavy glycosylation of the cap participates in masking conserved regions such as the receptor-binding site, modulating sensitivity to proteases and antibodies, and therefore plays a role in the regulation of viral entry and pathogenicity. During viral entry, the glycan cap is removed by host endosomal cathepsins, unmasking the receptor-binding site and allowing interaction with the Niemann-Pick C1 protein, the principal filovirus entry receptor. Monoclonal antibodies targeting the glycan cap can neutralize the virus, but therapeutic efficacy may be limited by the region's high variability and glycan heterogeneity. Consequently, the glycan cap is regarded as a relevant but challenging therapeutic target in Ebolavirus infection.

Other names

Glycan cap of Ebola virus glycoproteinEBOV GP glycan capEbolavirus GP1 glycan capGlycan cap region of filovirus GP

Antibody-mediated neutralization (by binding and blocking glycan cap epitopes, reducing viral infectivity)\nPrevention of viral entry (via interference with glycan cap structural integrity)