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The thermodynamic basis for viral RNA detection by the RIG-I innate immune sensor

tetano

Editor, Senior Moderator
J Biol Chem. 2012 Oct 10. [Epub ahead of print]
The thermodynamic basis for viral RNA detection by the RIG-I innate immune sensor.
Vela A, Fedorova O, Ding SC, Pyle AM.
Source

Yale University, United States;
Abstract

RIG-I is a cytoplasmic surveillance protein that contributes to the earliest stages of the vertebrate innate immune response. The protein specifically recognizes 5' triphosphorylated RNA structures that are released into the cell by viruses such as influenza and hepatitis C. To understand the energetic basis for viral RNA recognition by RIG-I, we studied the binding of RIG-I domain variants to a family of dsRNA ligands. Thermodynamic analysis revealed that the isolated RIG-I domains each make important contributions to affinity and that they interact using different strategies. Covalent linkage between the domains enhances RNA ligand specificity while reducing overall binding affinity, thereby providing a mechanism for discriminating virus from host RNA.

PMID:
23055530
[PubMed - as supplied by publisher]

Free full text

http://www.ncbi.nlm.nih.gov/pubmed/23055530
 
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