Taï Forest ebolavirus glycoprotein (TAFV GP)

The Taï Forest ebolavirus glycoprotein (TAFV GP) is the primary surface protein of the Taï Forest virus, a member of the Filoviridae family (UniProt P31288). It is a class I viral fusion protein that plays a critical role in the viral life cycle by mediating attachment to host cells, endocytosis, and subsequent fusion of the viral and host membranes (PubMed: 28619716). TAFV GP is synthesized as a precursor that is cleaved into two subunits, GP1 and GP2, which remain disulfide-linked; GP1 is responsible for receptor binding (specifically to Niemann-Pick C1), while GP2 facilitates membrane fusion (PubMed: 21866102). As the sole protein on the virion surface, it is the primary target for the host immune response and a key focus for the development of vaccines and therapeutic monoclonal antibodies. While Taï Forest virus is rare compared to the Zaire ebolavirus, its glycoprotein shares structural homology with other ebolaviruses, making it a target for pan-ebolavirus therapeutic strategies. Drugs targeting this protein, such as the broadly neutralizing antibody cocktail MBP134, typically function by neutralizing the virus or blocking its entry into target cells (Cell Host Microbe: 30661663). These interventions are designed to prevent the progression of Ebola virus disease by inhibiting viral spread within the host (Science: 28619716). The glycoprotein also undergoes significant post-translational modifications, including heavy glycosylation, which helps the virus evade the host immune system through glycan shielding (PubMed: 21866102).

Other names

TAFV glycoproteinCôte d'Ivoire ebolavirus glycoproteinGPEnvelope glycoproteinTaï Forest virus glycoprotein

Neutralization of viral particles by binding to the glycoprotein, thereby preventing attachment to host receptors or inhibiting the conformational changes required for membrane fusion (PubMed: 28619716).