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Ebola virus VP35 protein is a highly multifunctional structural protein encoded by the Ebola virus, critical for viral replication, transcription, and assembly. It acts as an essential cofactor of the viral RNA-dependent RNA polymerase complex (L protein), facilitates immune evasion by binding double-stranded RNA and antagonizing receptor-mediated interferon signaling, and is indispensable for virulence and pathogenesis in host cells. The VP35 protein contains an N-terminal coiled-coil oligomerization domain and a C-terminal interferon inhibitory (dsRNA-binding) domain, both essential for its function. Disruption of VP35 function attenuates viral replication and pathogenicity, making it a promising—but not yet clinically validated—antiviral drug target.
Drugs or molecules targeting VP35 generally inhibit its dsRNA binding, disrupt its interaction with polymerase (L protein), and/or block its interferon antagonist function.
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