EBOV encodes seven structural proteins: nucleoprotein (NP), polymerase cofactor (VP35), (VP40), GP, transcription activator (VP30), VP24, and RNA polymerase (L). GP protein contains 160-kDa envelope-attached glycoprotein (GP) and a 110 kDa secreted glycoprotein (sGP). GP is a class I fusion protein which assembles as trimers on viral surface and plays an important role in virus entry and attachment. Mature GP is a disulfide-linked heterodimer formed by two subunits, GP1 and GP2, which are generated from the proteolytical process of GP precursor (pre-GP) by cellular furin during virus assembly . GP1 is responsible for binding to the receptor(s) on target cells. Interacts with CD209/DC-SIGN and CLEC4M/DC-SIGNR which act as cofactors for virus entry into the host cell. GP2 acts as a class I viral fusion protein. GP1,2 mediates endothelial cell activation and decreases endothelial barrier function. sGP seems to possess an anti-inflammatory activity as it can reverse the barrier-decreasing effects of TNF alpha.