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J Biol Chem. 2012 Dec 14;287(51):42564-73. doi: 10.1074/jbc.M112.385146. Epub 2012 Oct 10.

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

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Department of Molecular Biophysics, Yale University, New Haven, Connecticut 06520, USA.


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.

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