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

doi:10.1107/S1744309110013266

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

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12 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 language	English (US)
Pages (from-to)	689-692
Number of pages	4
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	66
Issue number	6
DOIs	https://doi.org/10.1107/S1744309110013266
State	Published - 2010

Keywords

Ebola virus
Interferon inhibitory domain
VP35

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

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Leung, D. W., Borek, D., Farahbakhsh, M., Ramanan, P., Nix, J. C., Wang, T., Prins, K. C., Otwinowski, Z., Honzatko, R. B., Helgeson, L. A., Basler, C. F., & Amarasinghe, G. K. (2010). Crystallization and preliminary X-ray analysis of Ebola VP35 interferon inhibitory domain mutant proteins. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66(6), 689-692. https://doi.org/10.1107/S1744309110013266

Leung, DW, Borek, D, Farahbakhsh, M, Ramanan, P, Nix, JC, Wang, T, Prins, KC, Otwinowski, Z, Honzatko, RB, Helgeson, LA, Basler, CF & Amarasinghe, GK 2010, 'Crystallization and preliminary X-ray analysis of Ebola VP35 interferon inhibitory domain mutant proteins', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 66, no. 6, pp. 689-692. https://doi.org/10.1107/S1744309110013266

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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.",

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AU - Borek, Dominika

AU - Farahbakhsh, Mina

AU - Ramanan, Parameshwaran

AU - Nix, Jay C.

AU - Wang, Tianjiao

AU - Prins, Kathleen C.

AU - Otwinowski, Zbyszek

AU - Honzatko, Richard B.

AU - Helgeson, Luke A.

AU - Basler, Christopher F.

AU - Amarasinghe, Gaya K.

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AB - 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.

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

Abstract

Keywords

ASJC Scopus subject areas

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