Sudan virus glycoprotein GP1,2 (SUDV GP)

Sudan virus glycoprotein GP1,2 (SUDV GP) is the sole surface protein of the Sudan virus, a member of the Filoviridae family and a causative agent of Sudan virus disease (SVD) (UniProt, 2024). It is synthesized as a precursor that is post-translationally cleaved by host furin into two subunits, GP1 and GP2, which remain linked by a disulfide bond to form a trimeric spike on the viral envelope (NIH, 2011). GP1 is responsible for host cell attachment and binding to the essential endosomal receptor Niemann-Pick C1 (NPC1), while GP2 mediates the fusion of viral and host endosomal membranes (NIH, 2025). As the only protein on the virion surface, SUDV GP is the critical target for neutralizing antibodies and the primary antigen used in vaccine development (Sabin, 2024; IAVI, 2025). Therapeutic strategies include monoclonal antibodies that block receptor binding or inhibit the conformational changes necessary for fusion, as well as vaccines designed to elicit a protective immune response against the glycoprotein (NIH, 2020; Mapp Bio, 2018). Additionally, the protein plays a role in immune evasion through the production of a secreted form (sGP) and a shed form that act as decoys for the host's immune system (UniProt, 2024). The high mortality rate of SUDV infection and the lack of cross-reactivity with treatments for other ebolaviruses make SUDV GP a high-priority target for drug discovery (WHO, 2023).

Other names

Sudan ebolavirus glycoproteinSUDV GPGP1/GP2 complexSpike glycoproteinEnvelope glycoproteinSudan virus GP1,2

Neutralization of viral entry by blocking attachment to host cells, inhibition of the conformational rearrangement of the GP1/GP2 complex required for membrane fusion, and blocking the interaction between the receptor-binding domain and the endosomal receptor Niemann-Pick C1 (NPC1) (NIH, 2011; NIH, 2020; NIH, 2025).