4lg2
Crystal structure of Reston Ebola virus VP35 RNA binding domain bound to 12-bp dsRNACrystal structure of Reston Ebola virus VP35 RNA binding domain bound to 12-bp dsRNA
Structural highlights
FunctionVP35_EBORR Acts as a polymerase cofactor in the RNA polymerase transcription and replication complex. Prevents establishment of cellular antiviral state by blocking virus-induced phosphorylation and activation of interferon regulatory factor 3 (IRF3), a transcription factor critical for the induction of interferons alpha and beta. The mechanism by which this blockage occurs remains incompletely defined, a hypothesis suggests that VP35 dsRNA-binding activity prevents activation of IRF3 by sequestering dsRNA. Also inhibits the antiviral effect mediated by the interferon-induced, double-stranded RNA-activated protein kinase EIF2AK2/PKR (By similarity). Publication Abstract from PubMedRecognition of viral double-stranded RNA (dsRNA) activates interferon production and immune signaling in host cells. Crystal structures of ebolavirus VP35 show that it caps dsRNA ends to prevent sensing by pattern recognition receptors such as RIG-I. By contrast, structures of marburgvirus VP35 show that it primarily coats the dsRNA backbone. Here, we demonstrate that ebolavirus VP35 also coats the dsRNA backbone in solution, although binding to the dsRNA ends probably constitutes the initial binding event. Ebolavirus VP35 also coats the backbone of dsRNA for interferon antagonism.,Bale S, Julien JP, Bornholdt ZA, Krois AS, Wilson IA, Saphire EO J Virol. 2013 Jul 3. PMID:23824825[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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