Filovirus envelope glycoprotein (GP) (GP)

The Filovirus envelope glycoprotein (GP) is the primary surface protein of viruses in the Filoviridae family, including Ebola and Marburg viruses, and functions as a homotrimeric complex (UniProt: P87666). It is synthesized as a precursor, GP0, which is cleaved by host furin into GP1 and GP2 subunits that remain disulfide-linked; GP1 mediates host cell attachment and binding to the endosomal receptor Niemann-Pick C1 (NPC1), while GP2 facilitates the fusion of viral and host membranes (Carette et al., Nature 2011). As the only viral protein exposed on the virion surface, it is the critical target for the host immune response and the development of vaccines and therapeutics (Bornholdt et al., Science 2013). Monoclonal antibody treatments, such as Inmazeb and Ebanga, work by binding to specific epitopes on the GP to neutralize the virus and prevent cellular entry (FDA, 2020). Additionally, the virus produces a secreted, dimeric form of the glycoprotein (sGP) that serves as an immune decoy, potentially subverting the host's neutralizing antibody response (Cook & Terry, Viruses 2017).

Other names

Filovirus GPGP1/GP2 complexSurface glycoproteinSpike proteinEnvelope glycoprotein trimer

Neutralization of viral infection by binding to the GP1 subunit to block interaction with the host endosomal receptor Niemann-Pick C1 (NPC1), or by binding to the GP2 subunit to inhibit the conformational changes required for viral-host membrane fusion (Carette et al., Nature 2011; Bornholdt et al., Science 2013).