Structural features of influenza A virus panhandle RNA enabling the activation of RIG-I independently of 5'-triphosphate

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Retinoic acid-inducible gene I (RIG-I) recognizes specific molecular patterns of viral RNAs for inducing type I interferon. The C-terminal domain (CTD) of RIG-I binds to double-stranded RNA (dsRNA) with the 5'-triphosphate (5'-PPP), which induces a conformational change in RIG-I to an active form. It has been suggested that RIG-I detects infection of influenza A virus by recognizing the 5'-triphosphorylated panhandle structure of the viral RNA genome. Influenza panhandle RNA has a unique structure with a sharp helical bending. In spite of extensive studies of how viral RNAs activate RIG-I, whether the structural elements of the influenza panhandle RNA confer the ability to activate RIG-I signaling has been poorly explored. Here, we investigated the dynamics of the influenza panhandle RNA in complex with RIG-I CTD using NMR spectroscopy and showed that the bending structure of the panhandle RNA negates the requirement of a 5'-PPP moiety for RIG-I activation.
Publisher
OXFORD UNIV PRESS
Issue Date
2016-09
Language
English
Article Type
Article
Citation

NUCLEIC ACIDS RESEARCH, v.44, no.17, pp.8407 - 8416

ISSN
0305-1048
DOI
10.1093/nar/gkw525
URI
http://hdl.handle.net/10203/214799
Appears in Collection
CH-Journal Papers(저널논문)BS-Journal Papers(저널논문)
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