tetano
Editor, Senior Moderator
Nucleic Acids Res. 2016 Jun 10. pii: gkw525. [Epub ahead of print]
[h=1]Structural features of influenza A virus panhandle RNA enabling the activation of RIG-I independently of 5'-triphosphate.[/h] Lee MK[SUP]1[/SUP], Kim HE[SUP]2[/SUP], Park EB[SUP]3[/SUP], Lee J[SUP]4[/SUP], Kim KH[SUP]4[/SUP], Lim K[SUP]4[/SUP], Yum S[SUP]3[/SUP], Lee YH[SUP]4[/SUP], Kang SJ[SUP]5[/SUP], Lee JH[SUP]6[/SUP], Choi BS[SUP]7[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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.
? The Author(s) 2016. Published by Oxford University Press on behalf of Nucleic Acids Research.
PMID: 27288441 [PubMed - as supplied by publisher] Free full text
[h=1]Structural features of influenza A virus panhandle RNA enabling the activation of RIG-I independently of 5'-triphosphate.[/h] Lee MK[SUP]1[/SUP], Kim HE[SUP]2[/SUP], Park EB[SUP]3[/SUP], Lee J[SUP]4[/SUP], Kim KH[SUP]4[/SUP], Lim K[SUP]4[/SUP], Yum S[SUP]3[/SUP], Lee YH[SUP]4[/SUP], Kang SJ[SUP]5[/SUP], Lee JH[SUP]6[/SUP], Choi BS[SUP]7[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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.
? The Author(s) 2016. Published by Oxford University Press on behalf of Nucleic Acids Research.
PMID: 27288441 [PubMed - as supplied by publisher] Free full text