Taï Forest virus glycoprotein (TAFV GP)

The Taï Forest virus glycoprotein (TAFV GP) is the primary surface protein of the Taï Forest ebolavirus, a member of the Filoviridae family. It is a type I transmembrane glycoprotein that exists as a trimer of GP1 and GP2 heterodimers, which are produced by the proteolytic cleavage of a precursor protein by host furin (UniProt P31288). The GP1 subunit facilitates initial attachment to host cells and subsequent binding to the endosomal receptor Niemann-Pick C1 (NPC1) after the glycan cap is removed by host cathepsins (Carette et al., Nature 2011). The GP2 subunit contains the hydrophobic fusion peptide that mediates the merger of the viral and endosomal membranes, allowing the viral genome to enter the cytoplasm (UniProt P31288). Because it is the only protein on the virion surface, TAFV GP is the critical target for neutralizing antibodies and vaccine design (Wec et al., Science 2017). Although Taï Forest virus is rare, with only one recorded human case, its glycoprotein is a key component in the development of pan-ebolavirus therapeutics intended to provide broad protection against multiple species within the Ebolavirus genus (Bornholdt et al., Science 2016).

Other names

Côte d'Ivoire ebolavirus glycoproteinCIEV GPGP1,2Envelope glycoproteinEbolavirus glycoprotein – TAFV species

Neutralization of viral entry by blocking attachment to host cell receptors or preventing pH-dependent membrane fusion within the endosome.