埃博拉病毒VP35干扰素抑制结构域突变蛋白的结晶及初步X射线分析
Crystallization and preliminary X-ray analysis of Ebola VP35 interferon inhibitory domain mutant proteins.
作者信息
Leung Daisy W, Borek Dominika, Farahbakhsh Mina, Ramanan Parameshwaran, Nix Jay C, Wang Tianjiao, Prins Kathleen C, Otwinowski Zbyszek, Honzatko Richard B, Helgeson Luke A, Basler Christopher F, Amarasinghe Gaya K
机构信息
Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, USA.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jun 1;66(Pt 6):689-92. doi: 10.1107/S1744309110013266. Epub 2010 May 27.
Abstract
VP35 is one of seven structural proteins encoded by the Ebola viral genome and mediates viral replication, nucleocapsid formation and host immune suppression. The C-terminal interferon inhibitory domain (IID) of VP35 is critical for dsRNA binding and interferon inhibition. The wild-type VP35 IID structure revealed several conserved residues that are important for dsRNA binding and interferon antagonism. Here, the expression, purification and crystallization of recombinant Zaire Ebola VP35 IID mutants R312A, K319A/R322A and K339A in space groups P6(1)22, P2(1)2(1)2(1) and P2(1), respectively, are described. Diffraction data were collected using synchrotron sources at the Advanced Light Source and the Advanced Photon Source.
摘要
VP35是埃博拉病毒基因组编码的七种结构蛋白之一，介导病毒复制、核衣壳形成和宿主免疫抑制。VP35的C末端干扰素抑制结构域（IID）对于双链RNA结合和干扰素抑制至关重要。野生型VP35 IID结构揭示了几个对双链RNA结合和干扰素拮抗作用很重要的保守残基。本文描述了重组扎伊尔埃博拉病毒VP35 IID突变体R312A、K319A/R322A和K339A分别在空间群P6(1)22、P2(1)2(1)2(1)和P2(1)中的表达、纯化和结晶。使用先进光源和先进光子源的同步加速器源收集衍射数据。
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2
Mutations abrogating VP35 interaction with double-stranded RNA render Ebola virus avirulent in guinea pigs.突变使埃博拉病毒的 VP35 蛋白与双链 RNA 的相互作用失效，从而使病毒丧失毒力。
J Virol. 2010 Mar;84(6):3004-15. doi: 10.1128/JVI.02459-09. Epub 2010 Jan 13.
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