Bundibugyo ebolavirus glycoprotein (BDBV GP)

The Bundibugyo ebolavirus glycoprotein (BDBV GP) is a trimeric viral envelope protein composed of GP1 and GP2 subunits, cleaved from a GP0 precursor by furin and linked by a disulfide bond. GP1 forms a chalice-shaped bowl for host cell attachment via a recessed receptor-binding site masked by a glycan cap and mucin-like domain, while GP2 mediates membrane fusion through an internal fusion loop and heptad repeats that undergo pH-triggered conformational changes in the endosome. Heavily glycosylated, BDBV GP features a thick glycocalyx that shields conserved epitopes from immune detection, contributing to viral evasion. In Bundibugyo ebolavirus infection, endemic to Uganda, GP drives pathogenesis by facilitating entry into host cells, with its structure closely resembling Zaire ebolavirus GP but showing sequence divergence over 30%. Therapeutic antibodies like ADI-15878 target the conserved GP2 fusion loop and adjacent pocket for pan-ebolavirus neutralization, blocking fusion, while challenges include glycan barriers and escape variants. No small-molecule drugs are approved, but GP remains a key target for vaccines and monoclonal therapies due to its essential role in infection.

Other names

BDBV glycoproteinBundibugyo virus GPBDBV GP1,2BDBV envelope glycoprotein

Neutralization by binding to GP fusion loop and GP2 pocket, preventing conformational changes for membrane fusion; Blocking receptor-binding site (RBS) in GP1 chalice bowl; Inhibition of cathepsin-mediated priming and viral entry