Expression, purification, crystallization and preliminary X-ray studies of the Ebola VP35 interferon inhibitory domain
- 31 January 2009
- journal article
- research article
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section F Structural Biology and Crystallization Communications
- Vol. 65 (2) , 163-165
- https://doi.org/10.1107/s1744309108044187
Abstract
Ebola VP35 is a multifunctional protein that is important for host immune suppression and pathogenesis. VP35 contains an N-terminal oligomerization domain and a C-terminal interferon inhibitory domain (IID). Mutations within the VP35 IID result in loss of host immune suppression. Here, efforts to crystallize recombinantly overexpressed VP35 IID that was purified from Escherichia coli are described. Native and selenomethionine-labeled crystals belonging to the orthorhombic space group P212121 were obtained by the hanging-drop vapor-diffusion method and diffraction data were collected at the ALS synchrotron.Keywords
This publication has 16 references indexed in Scilit:
- Structure of the Ebola VP35 interferon inhibitory domainProceedings of the National Academy of Sciences, 2009
- Inhibition of IRF-3 Activation by VP35 Is Critical for the High Level of Virulence of Ebola VirusJournal of Virology, 2008
- The VP35 Protein of Ebola Virus Inhibits the Antiviral Effect Mediated by Double-Stranded RNA-Dependent Protein Kinase PKRJournal of Virology, 2007
- Solvent content of protein crystalsPublished by Elsevier ,2006
- Reverse Genetic Generation of Recombinant Zaire Ebola Viruses Containing Disrupted IRF-3 Inhibitory Domains Results in Attenuated Virus Growth In Vitro and Higher Levels of IRF-3 Activation without Inhibiting Viral Transcription or ReplicationJournal of Virology, 2006
- VP35 Knockdown Inhibits Ebola Virus Amplification and Protects against Lethal Infection in MiceAntimicrobial Agents and Chemotherapy, 2006
- Homo-Oligomerization of Marburgvirus VP35 Is Essential for Its Function in Replication and TranscriptionJournal of Virology, 2005
- Homo-oligomerization facilitates the interferon-antagonist activity of the ebolavirus VP35 proteinVirology, 2005
- A C-terminal basic amino acid motif of Zaire ebolavirus VP35 is essential for type I interferon antagonism and displays high identity with the RNA-binding domain of another interferon antagonist, the NS1 protein of influenza A virusVirology, 2004
- The Ebola Virus VP35 Protein Inhibits Activation of Interferon Regulatory Factor 3Journal of Virology, 2003