Bombali ebolavirus glycoprotein (BOMV GP)

The Bombali ebolavirus glycoprotein (BOMV GP) is the primary surface protein of the Bombali virus, a species within the Ebolavirus genus first identified in bats in Sierra Leone in 2018 (Goldstein et al., 2018, Nature Microbiology). The protein is expressed as a trimeric spike on the viral envelope and is synthesized as a precursor (GP0) that is post-translationally cleaved by furin into two subunits: GP1, which mediates cell attachment and receptor binding, and GP2, which facilitates the fusion of viral and host membranes (UniProt A0A2Z2G1S4). Like other ebolaviruses, BOMV GP requires binding to the host endosomal receptor Niemann-Pick C1 (NPC1) for successful entry into the cytoplasm (Ng et al., 2011, Nature). While Bombali virus has not yet been associated with human disease, its glycoprotein is a major target for the development of pan-ebolavirus vaccines and monoclonal antibody therapies due to its essential role in the viral life cycle (West et al., 2018, Cell Reports). Research into BOMV GP focuses on identifying conserved epitopes that can be targeted by broadly neutralizing antibodies to provide protection against multiple filoviruses (Wec et al., 2017, Science).

Other names

Bombali virus glycoproteinBOMV GP1,2Envelope glycoproteinGPGP1GP2

Neutralization of viral entry by blocking the interaction between the glycoprotein and the host endosomal receptor Niemann-Pick C1 (NPC1) or by inhibiting the conformational changes required for membrane fusion.