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Ebola virus secreted glycoprotein (sGP) is the primary protein product of the Ebola virus GP gene, produced via transcriptional editing and secreted in large quantities into the blood of infected patients. It exists as a disulfide-linked homodimer and shares the first 295 amino acids of its N-terminus with the virion-attached surface glycoprotein (GP), while possessing a unique C-terminal tail. The primary biological role of sGP is to act as an "antigenic decoy," subverting the host's immune response by binding to and sequestering antibodies that would otherwise target the virus, a process known as antigenic subversion. Additionally, sGP has been shown to inhibit neutrophil activation, suppress pro-inflammatory cytokine production, and potentially enhance viral replication through the activation of the MAPK signaling pathway. Because sGP is detectable in the serum shortly after infection, it serves as a critical biomarker for the early diagnosis of Ebola virus disease. However, its high concentration in the blood presents a therapeutic challenge, as it can "soak up" monoclonal antibody treatments like those found in the Inmazeb or ZMapp cocktails, necessitating higher doses to achieve clinical efficacy.
Decoy neutralization and inhibition of sGP-mediated immune suppression to enhance viral clearance.
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