[PDF][PDF] Nonself RNA-sensing mechanism of RIG-I helicase and activation of antiviral immune responses
K Takahasi, M Yoneyama, T Nishihori, R Hirai… - Molecular cell, 2008 - cell.com
K Takahasi, M Yoneyama, T Nishihori, R Hirai, H Kumeta, R Narita, M Gale, F Inagaki…
Molecular cell, 2008•cell.comSummary A DExD/H protein, RIG-I, is critical in innate antiviral responses by sensing viral
RNA. Here we show that RIG-I recognizes two distinct viral RNA patterns: double-stranded
(ds) and 5′ ppp single-stranded (ss) RNA. The binding of RIG-I with dsRNA or 5′ ppp
ssRNA in the presence of ATP produces a common structure, as suggested by protease
digestion. Further analyses demonstrated that the C-terminal domain of RIG-I (CTD)
recognizes these RNA patterns and CTD coincides with the autorepression domain …
RNA. Here we show that RIG-I recognizes two distinct viral RNA patterns: double-stranded
(ds) and 5′ ppp single-stranded (ss) RNA. The binding of RIG-I with dsRNA or 5′ ppp
ssRNA in the presence of ATP produces a common structure, as suggested by protease
digestion. Further analyses demonstrated that the C-terminal domain of RIG-I (CTD)
recognizes these RNA patterns and CTD coincides with the autorepression domain …
Summary
A DExD/H protein, RIG-I, is critical in innate antiviral responses by sensing viral RNA. Here we show that RIG-I recognizes two distinct viral RNA patterns: double-stranded (ds) and 5′ppp single-stranded (ss) RNA. The binding of RIG-I with dsRNA or 5′ppp ssRNA in the presence of ATP produces a common structure, as suggested by protease digestion. Further analyses demonstrated that the C-terminal domain of RIG-I (CTD) recognizes these RNA patterns and CTD coincides with the autorepression domain. Structural analysis of CTD by NMR spectroscopy in conjunction with mutagenesis revealed that the basic surface of CTD with a characteristic cleft interacts with RIG-I ligands. Our results suggest that the bipartite structure of CTD regulates RIG-I on encountering viral RNA patterns.
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