1. mda-5, but not RIG-I, is a common target for paramyxovirus V proteins
- Author
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Michael A. Skinner, Stephen Goodbourn, Craig Ross, Kay Childs, Nicola Stock, Louise Hilton, J. Andrejeva, and Richard E. Randall
- Subjects
Immunoprecipitation ,viruses ,Molecular Sequence Data ,Plasma protein binding ,Cell Line ,Birds ,DEAD-box RNA Helicases ,RIG-I ,03 medical and health sciences ,0302 clinical medicine ,Protein structure ,Interferon ,Two-Hybrid System Techniques ,Virology ,Chlorocebus aethiops ,Protein Interaction Mapping ,PIV5 ,medicine ,Animals ,Humans ,V proteins ,Amino Acid Sequence ,030304 developmental biology ,Viral Structural Proteins ,0303 health sciences ,biology ,Sequence Homology, Amino Acid ,Helicase ,Interferon-beta ,RNA Helicase A ,Molecular biology ,3. Good health ,Protein Structure, Tertiary ,Cell culture ,mda-5 ,Paramyxoviruses ,biology.protein ,Parainfluenza Virus 5 ,Cattle ,030215 immunology ,medicine.drug ,Protein Binding - Abstract
The induction of IFN-beta by the paramyxovirus PIV5 (formerly known as SV5) is limited by the action of the viral V protein that targets the cellular RNA helicase mda-5. Here we show that 12 other paramyxoviruses also target mda-5 by a direct interaction between the conserved cysteine-rich C-terminus of their V proteins and the helicase domain of mda-5. The inhibition of IFN-beta induction is not species-restricted, being observed in a range of mammalian cells as well as in avian cells, and we show that the inhibition of mda-5 function is also not restricted to mammalian cells. In contrast, the V proteins do not bind to the related RNA helicase RIG-I and do not inhibit its activity. The relative contributions of mda-5 and RIG-I to IFN-beta induction are discussed.
- Published
- 2007
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