Master of Science in Biochemistry, Department of Biology, Faculty of Science, Shahid Chamran University of Ahvaz, Ahvaz, Iran.
Abstract: (2685 Views)
The Filoviridae family within the order Mononegavirales consists of two genera, Ebolaviruses and Marburgviruses. Zaire strain of ebolavirus as one of the most lethal viruses ever isolated, with nearly a 90% fatality rate that causes severe hemorrhagic fever in humans and nonhuman primates. Of the seven proteins encoded by ebolavirus, VP24, Glycoprotein and VP35 are virulence factors. Viral protein 35 (VP35) is a multifunctional protein that functions at several stages in the viral replication cycle. VP35 is known to antagonize numerous components in the Interferon induction and signaling pathway including RLR receptors, especially RIG-1, IRF-3 and IRF-7 kinases, protein kinase R, and protein kinase R-activator (PACT) are known. VP35 also functions as an RNAi silencing suppressor, a co-factor for the viral polymerase and a structural component of the viral nucleocapsid. Therefore VP35 is required for efficient viral replication and pathogenesis. Studies revealed that there are two highly conserved basic patches termed the first basic patch (FBP) and the central basic patch (CBP) located within the C-terminal interferon inhibitory domain (IID) of VP35. Given the importance of this protein in the pathogenesis of the Ebola virus, VP35 is a potential target for antiviral development. In this regard, we describe the important parts of this protein from Structural and functional aspects.