Journal
IMMUNITY
Volume 31, Issue 1, Pages 25-34Publisher
CELL PRESS
DOI: 10.1016/j.immuni.2009.05.008
Keywords
-
Categories
Funding
- BMBF Biofuture [0311896, SFB 670, SFB 704, KFO115, KFO 177]
- German Research Foundation DFG [BA3544/1-1]
- National Institutes of Health [Al-065483, Al-067497]
- Memorial Sloan-Kettering Cancer Center (MSKCC)
Ask authors/readers for more resources
Antiviral immunity is triggered by immunorecognition of viral nucleic acids. The cytosolic helicase RIG-I is a key sensor of viral infections and is activated by RNA containing a triphosphate at the 5' end. The exact structure of RNA activating RIG-I remains controversial. Here, we established a chemical approach for 5' triphosphate oligoribonucleotide synthesis and found that synthetic single-stranded 5' triphosphate oligoribonucleotides were unable to bind and activate RIG-I. Conversely, the addition of the synthetic complementary strand resulted in optimal binding and activation of RIG-I. Short double-strand conformation with base pairing of the nucleoside carrying the 5' triphosphate was required. RIG-I activation was impaired by a 3' overhang at the 5' triphosphate end. These results define the structure of RNA for full RIG-I activation and explain how RIG-I detects negative-strand RNA viruses that lack long double-stranded RNA but do contain blunt short double-stranded 5' triphosphate RNA in the panhandle region of their single-stranded genome.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available