The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase, mda-5, and inhibit its activation of the IFN -β promoter
University of London · St George's, University of London · +1 more institution
Abstract
Most paramyxoviruses circumvent the IFN response by blocking IFN signaling and limiting the production of IFN by virus-infected cells. Here we report that the highly conserved cysteine-rich C-terminal domain of the V proteins of a wide variety of paramyxoviruses binds melanoma differentiation-associated gene 5 (mda-5) product. mda-5 is an IFN-inducible host cell DExD/H box helicase that contains a caspase recruitment domain at its N terminus. Overexpression of mda-5 stimulated the basal activity of the IFN-beta promoter in reporter gene assays and significantly enhanced the activation of the IFN-beta promoter by intracellular dsRNA. Both these activities were repressed by coexpression of the V proteins of…
Citation impact
- FWCI
- 46.93
- Percentile
- 100%
- References
- 30
Authors
7- JAJ. AndrejevaCorresponding
University of London, St George's, University of London, University of St Andrews
- KCKay Childs
University of London, St George's, University of London, University of St Andrews
- DFD. F. Young
University of London, St George's, University of London, University of St Andrews
- TST. S. Carlos
University of London, St George's, University of London, University of St Andrews
- NSNicola Stock
University of London, St George's, University of London, University of St Andrews
Topics & keywords
- Sendai virus
- Biology
- Molecular biology
- Interferon
- Reporter gene
- RNA silencing
- RIG-I
- Virus