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Papers In Press, published online ahead of print November 23, 2005
Medicine Dept., Lady Davis Institute/McGill University, Montreal, Quebec H3T 1E2
Corresponding Author: rongtuan.lin{at}mcgill.ca
Activation of the IRF-3 and IRF-7 transcription factors is essential for the induction of type I interferon and development of the innate antiviral response. Retinoic acid inducible gene I has been shown to contribute to virus-induced IFN production independent of the Toll-like receptor pathways in response to a variety of RNA viruses and double stranded RNA. In the present study, we demonstrate that the NF-kB inducible, anti-apoptotic protein A20 efficiently blocks RIG-I-mediated activation of NF-kB-, IRF-3- and IRF-7-dependent promoters, but only weakly interferes with TRIF-TLR-3 mediated IFN activation. Expression of A20 completely blocked CARD domain containing DRIG-I-induced IRF-3 Ser396 phosphorylation, homodimerization and DNA binding. The level of A20 inhibition was upstream of the TBK1/IKKe kinases that phosphorylate IRF3 and IRF7 and paradoxically, A20 selectively degraded the TRIF protein but not RIG-I. A20 possesses two ubiquitin-editing domains, an amino-terminal de-ubiquitination domain and a carboxyl-terminal ubiquitin ligase domain consisting of seven zinc finger domains. Deletion of the N-terminal de-ubiquitination domain had no significant effect on the inhibitory effect of A20, while deletion or mutation of zinc finger motif 7 ablated the inhibitory function of A20 on IRF- or NF-kB-mediated gene expression. Furthermore, cells stably expressing the active form of RIG-I induced an antiviral state that interfered with replication of VSV, an effect that was reversed by stable co-expression of A20. These results suggest that the virus inducible, NF-kB-dependent activation of A20 functions as a negative regulator of RIG-I mediated induction of the antiviral state.
J. Biol. Chem, 10.1074/jbc.M510326200
Submitted on September 20, 2005
Accepted on November 23, 2005
Negative regulation of the RIG-I-induced antiviral state by the ubiquitin-editing protein A20
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