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 virus
- 1 October 2004
- Vol. 328 (2) , 177-184
- https://doi.org/10.1016/j.virol.2004.07.006
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- A Recombinant Influenza A Virus Expressing anRNA-Binding-Defective NS1 Protein Induces High Levels of BetaInterferon and Is Attenuated inMiceJournal of Virology, 2003
- Pathogenesis of Ebola Hemorrhagic Fever in Cynomolgus MacaquesThe American Journal of Pathology, 2003
- Ebola and Marburg Viruses Replicate in Monocyte‐Derived Dendritic Cells without Inducing the Production of Cytokines and Full MaturationThe Journal of Infectious Diseases, 2003
- The Ebola Virus VP35 Protein Inhibits Activation of Interferon Regulatory Factor 3Journal of Virology, 2003
- IKKε and TBK1 are essential components of the IRF3 signaling pathwayNature Immunology, 2003
- The interferon antiviral response: from viral invasion to evasionCurrent Opinion in Infectious Diseases, 2002
- Monocyte-Derived Human Macrophages and Peripheral Blood Mononuclear Cells Infected with Ebola Virus Secrete MIP-1α and TNF-α and Inhibit Poly-IC-Induced IFN-α in VitroVirology, 2001
- Inhibition of Interferon-Mediated Antiviral Responses by Influenza A Viruses and Other Negative-Strand RNA VirusesVirology, 2001
- The Ebola virus VP35 protein functions as a type I IFN antagonistProceedings of the National Academy of Sciences, 2000
- The VP35 and VP40 proteins of filovirusesFEBS Letters, 1993