Bombali virus glycoprotein (BOMV GP)

Bombali virus glycoprotein (BOMV GP) is the primary surface protein of the Bombali ebolavirus, a species within the Ebolavirus genus first identified in bats in West Africa (Source 1.3.2, 1.3.5). As a Class I viral fusion protein, it is synthesized as a precursor that is cleaved into GP1 and GP2 subunits, which form a trimeric spike on the viral envelope (Source 1.3.1, 1.5.1). The GP1 subunit is responsible for attachment to host cell surface factors and binding to the endosomal receptor Niemann-Pick C1 (NPC1), while the GP2 subunit mediates the fusion of viral and host membranes (Source 1.1.1, 1.3.1). Although no human infections have been reported to date, BOMV GP has been shown to facilitate entry into human cells in vitro, suggesting a potential risk for zoonotic spillover (Source 1.3.4, 1.4.1). This glycoprotein is a major target for the development of vaccines and therapeutic antibodies aimed at providing broad protection against multiple ebolavirus species (Source 1.3.2, 1.4.4). While many monoclonal antibodies specific to the Zaire ebolavirus, such as those in the REGN-EB3 cocktail or mAb114, do not neutralize BOMV GP, broadly reactive antibodies like CA45 and P6 have demonstrated efficacy in inhibiting its function (Source 1.1.3, 1.3.2). Additionally, certain small molecule drugs, including toremifene and sertraline, have been found to bind and destabilize the glycoprotein's prefusion structure, offering a potential pathway for antiviral intervention (Source 1.5.1).

Other names

Bombali ebolavirus glycoproteinBOMV glycoproteinGP1,2Envelope glycoprotein

Neutralization of viral particles, inhibition of viral entry and membrane fusion, and destabilization of the prefusion glycoprotein conformation.