Ebolavirus envelope glycoprotein (EBOV GP)

The Ebolavirus envelope glycoprotein (GP) is the sole protein expressed on the surface of the Ebola virus virion and is indispensable for the viral life cycle. As a class I viral fusion protein, it mediates the critical steps of host cell attachment, macropinocytosis, and the subsequent fusion of the viral envelope with the host endosomal membrane (Lee & Saphire, 2009). The protein is synthesized as a precursor that is cleaved by furin into two subunits: GP1, which handles receptor binding (including the intracellular receptor NPC1), and GP2, which facilitates membrane fusion (NIH, 2015). Beyond its structural role, GP is a major factor in pathogenesis, utilizing 'glycan shielding' to hide neutralizing epitopes and secreting a soluble isoform (sGP) that acts as an immunological decoy to subvert the host antibody response (Patsnap, 2024). Because of its essential role in infection, GP is the primary target for all currently approved Ebola countermeasures, including the Ervebo vaccine and monoclonal antibody treatments like Inmazeb and Ebanga (FDA, 2020). However, therapeutic efficacy can be challenged by the virus's ability to shed GP, which may trigger systemic inflammatory responses through TLR4 activation (Frontiers in Microbiology, 2017).

Other names

GPGP1,2EBOV GPSpike glycoproteinSurface glycoproteinEnvelope glycoproteinSoluble glycoprotein (sGP)Small soluble glycoprotein (ssGP)

Neutralization of viral particles, inhibition of host cell attachment, blocking of GP1-NPC1 receptor interaction, inhibition of GP2-mediated membrane fusion, and induction of antibody-dependent cellular cytotoxicity (ADCC).