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The Sudan ebolavirus glycoprotein (SUDV GP) is the sole protein expressed on the surface of the Sudan virus virion and is the primary mediator of host cell entry (UniProt P31769). It is synthesized as a precursor (GP0) that is post-translationally cleaved into two subunits, GP1 and GP2, which remain linked by a disulfide bond to form a heteromeric trimer. GP1 is responsible for attachment to host cell surface receptors, such as C-type lectins, and binding to the endosomal receptor Niemann-Pick C1 (NPC1), while GP2 contains the fusion machinery required for the merger of the viral envelope with the host endosomal membrane (PMID: 36417483). As the only surface-exposed viral protein, SUDV GP is the critical target for the host's neutralizing antibody response and is the central component of most vaccine candidates. In the context of Sudan virus disease (SVD), GP facilitates infection and can also contribute to immune evasion through the production of a secreted form (sGP). Therapeutic strategies focusing on SUDV GP include the development of viral-vectored vaccines, such as rVSV-SUDV and ChAd3-SUDV, which aim to induce robust antibody and T-cell responses (WHO, 2022). Additionally, monoclonal antibody cocktails like MBP134 have been developed to target conserved epitopes on the glycoprotein to provide passive immunity and improve survival rates in infected individuals (PMID: 30643246).
Induction of neutralizing antibodies and T-cell responses to prevent viral entry and clear infected cells.
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