Sudan Ebola virus glycoprotein (SUDV GP)

The Sudan Ebola virus glycoprotein (SUDV GP) is the sole protein expressed on the surface of the Sudan virus virion and is essential for the viral life cycle. It is synthesized as a precursor (GP0) that is cleaved by cellular furin into two subunits, GP1 and GP2, which remain disulfide-linked to form a trimeric spike on the viral envelope. The GP1 subunit is responsible for attachment to host cell surface receptors and subsequent binding to the intracellular receptor Niemann-Pick C1 (NPC1) within the endosome, while the GP2 subunit mediates the fusion of the viral and host endosomal membranes. Due to its critical role in viral entry and its exposure on the virion surface, SUDV GP is the primary target for the host immune response and the development of therapeutic interventions. Monoclonal antibodies and vaccines specifically target this glycoprotein to neutralize the virus and prevent infection. Because SUDV is genetically distinct from the Zaire ebolavirus (EBOV), therapeutics designed for EBOV, such as Inmazeb or Ebanga, generally do not provide cross-protection against SUDV, necessitating the development of SUDV-specific agents like Gidimatenimab. Clinical efforts continue to focus on optimizing the breadth and potency of GP-targeting molecules to combat Sudan virus outbreaks.

Other names

Sudan virus glycoproteinSUDV envelope glycoproteinSurface glycoprotein Sudan ebolavirusGPSudan virus GP

Neutralization of viral particles, inhibition of viral attachment to host cells, and blockade of endosomal membrane fusion by preventing interaction with the Niemann-Pick C1 (NPC1) receptor.