EBOV

EBOV studies focus on viral proteins that control nucleocapsid transport, vascular injury, and interferon evasion^[1]. GP induces cytotoxicity in human endothelial cells, and this pathogenic effect maps to its mucin-like domain^[2]. Mechanistically, VP35 binds double-stranded RNA and inhibits RIG-I-induced IFN-α/β production. Structural data show that VP35 recognizes dsRNA backbone and blunt ends, preventing RIG-I-like receptor sensing^[3]. VP35 also inhibits IRF-3 activation, and the R312A mutation impaired this antagonist function in mouse-adapted EBOV^[4]. Compared with VP35, VP24 acts downstream by binding karyopherin α1 and blocking nuclear accumulation of tyrosine-phosphorylated STAT1^[5]. This distinction separates VP35 as an interferon-production antagonist from VP24 as an interferon-signaling antagonist^[5]. Compared with Bundibugyo virus VP24, EBOV VP24 binds karyopherin α proteins with higher affinity and correlates with stronger IFN-I inhibition^[6]. For inhibitor studies, myricetin inhibited recombinant VP35-dsRNA interaction in a fluorescence-based assay^[7]. - VP35 assays should measure dsRNA binding, IRF-3 activation, RIG-I signaling, and polymerase-complex activity^[3][4]. - VP24 studies should compare STAT1 transport, KPNA binding, and EBOV versus BDBV interfaces^[5][6].