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RIG-I from waterfowl and mammals have different abilities to induce antiviral responses against influenza A viruses

tetano

Editor, Senior Moderator
J Gen Virol. 2014 Nov 4. pii: vir.0.069914-0. doi: 10.1099/vir.0.069914-0. [Epub ahead of print]
RIG-I from waterfowl and mammals have different abilities to induce antiviral responses against influenza A viruses.
Shao Q1, Xu W1, Guo Q1, Yan L1, Rui L1, Liu J1, Zhao Y1, Li Z2.
Author information
Abstract

Retinoic acid-induced gene I (RIG-I), plays a crucial role in sensing viral RNA and facilitating the production of IFN-β. It varies in length and sequence among different species. The present study assessed the functional differences among RIG-I proteins derived from mammals and birds. The transfection of duck caspase recruitment domains (CARDs) and RIG-I (dCARDs and dRIG-I) and goose CARDs and RIG-I (gCARDs and gRIG-I) into DF-1 cells increased the production of IFN-β mRNA and IFN-stimulated genes and decreased influenza A virus (IAV) replication, whereas, human CARDs and RIG-I (hCARDs and hRIG-I) and mouse CARDs and RIG-I (mCARDs and mRIG-I) had no effect. In 293T and A549 cells, hCARDs had the strongest IFN-inducing activity, followed by mCARDs, dCARDs, and gCARDs. The IFN-inducing activity of hRIG-I was stronger than that of mRIG-I, dRIG-I, and gRIG-I, in that order. The results also showed that although the ability dCARDs to activate IFN was stronger than that of gCARDs in DF-1, 293T, and A549 cells, dRIG-I had a weaker ability to activate IFN than gRIG-I in DF-1 with or without IAV infection. Taken together, these data suggest that RIG-I protein has different amino acid sequences and functions among species. This genetic and functional diversity renders it flexible, adaptable, and capable of recognizing many viruses in different species.

Copyright ? 2014, the Society for General Microbiology.
KEYWORDS:

H1N1; H9N2; IFN; RIG-I; influenza

PMID:
25371516
[PubMed - as supplied by publisher]

http://www.ncbi.nlm.nih.gov/pubmed/25371516
 
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