Filovirus glycoprotein (GP) (GP)

The filovirus glycoprotein (GP) is the primary surface protein of viruses in the Filoviridae family, including Ebola (EBOV), Sudan (SUDV), Bundibugyo (BDBV), and Marburg (MARV) viruses [13, 16]. It is a class I viral fusion protein synthesized as a precursor that is cleaved into two subunits, GP1 and GP2, which form a disulfide-linked heterodimer; these heterodimers then assemble into homotrimers on the viral surface [13, 16]. GP1 is responsible for host cell attachment and binding to the essential endosomal receptor Niemann-Pick C1 (NPC1) after proteolytic processing by host cathepsins [2, 18]. GP2 contains the fusion machinery required to merge the viral envelope with the host endosomal membrane, allowing the viral ribonucleoprotein to enter the cytoplasm [2, 13]. As the only protein exposed on the virion surface, GP is the critical target for the host immune response and the primary focus for the development of vaccines and therapeutic monoclonal antibodies [13, 18]. Current treatments, such as Inmazeb and Ebanga, utilize monoclonal antibodies to neutralize the virus by blocking these entry steps, though the high genetic diversity between filovirus species often necessitates the use of antibody cocktails or the development of pan-filovirus agents [4, 8, 17].

Other names

Envelope glycoproteinGP1,2Spike proteinSurface glycoproteinGP1/GP2 complex

Neutralization of viral particles, inhibition of viral attachment to host cells, blocking of endosomal receptor (NPC1) binding, inhibition of cathepsin-mediated proteolytic cleavage, and prevention of GP2-mediated membrane fusion [2, 8, 13, 18].