Crystallization and preliminary X-ray analysis of Ebola VP35 interferon inhibitory domain mutant proteins

Daisy W. Leung, Dominika Borek, Mina Farahbakhsh, Parameshwaran Ramanan, Jay C. Nix, Tianjiao Wang, Kathleen C. Prins, Zbyszek Otwinowski, Richard B. Honzatko, Luke A. Helgeson, Christopher F. Basler, Gaya K. Amarasinghe

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

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 P6122, P212121 and P21, respectively, are described. Diffraction data were collected using synchrotron sources at the Advanced Light Source and the Advanced Photon Source.

Original languageEnglish (US)
Pages (from-to)689-692
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume66
Issue number6
DOIs
StatePublished - 2010

Keywords

  • Ebola virus
  • Interferon inhibitory domain
  • VP35

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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