The glycoprotein (GP) encoded by the Ebola virus genome is a critical determinant of the pathogenicity of Ebolavirus hemorrhagic fever viruses. It is processed into distinct forms for incorporation into the virus envelope, presentation on the cell surface, or release from infected cells. GP is a class I fusion protein that assembles as trimers on the viral surface, playing a crucial role in virus attachment and entry. The mature GP is a disulfide-linked heterodimer composed of two subunits, GP1 and GP2, generated from the proteolytic processing of the GP precursor (pre-GP) by cellular furin during virus assembly.
GP1 binds to receptors on target cells, interacting with CD209/DC-SIGN and CLEC4M/DC-SIGNR, which serve as cofactors for virus entry into host cells. GP2 functions as a class I viral fusion protein. The GP1,2 heterodimer mediates endothelial cell activation and reduces endothelial barrier function. Soluble GP (sGP) appears to have anti-inflammatory activity, as it can reverse the barrier-disrupting effects of TNF-alpha.
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