tetano
Editor, Senior Moderator
Structure. 2015 Sep 9. pii: S0969-2126(15)00334-2. doi: 10.1016/j.str.2015.08.007. [Epub ahead of print]
[h=1]Structural Basis for a Novel Interaction between the NS1 Protein Derived from the 1918 Influenza Virus and RIG-I.[/h] Jureka AS[SUP]1[/SUP], Kleinpeter AB[SUP]1[/SUP], Cornilescu G[SUP]2[/SUP], Cornilescu CC[SUP]2[/SUP], Petit CM[SUP]3[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] The influenza non-structural protein 1 (NS1) plays a critical role in antagonizing the innate immune response to infection. One interaction that facilitates this function is between NS1 and RIG-I, one of the main sensors of influenza virus infection. While NS1 and RIG-I are known to interact, it is currently unclear whether this interaction is direct or if it is mediated by other biomolecules. Here we demonstrate a direct, strain-dependent interaction between the NS1 RNA binding domain (NS1[SUP]RBD[/SUP]) of the influenza A/Brevig Mission/1918 H1N1 (1918[SUP]H1N1[/SUP]) virus and the second caspase activation and recruitment domain of RIG-I. Solving the solution structure of the 1918[SUP]H1N1[/SUP] NS1[SUP]RBD[/SUP] revealed features in a functionally novel region that may facilitate the observed interaction. The biophysical and structural data herein suggest a possible mechanism by which strain-specific differences in NS1 modulate influenza virulence.
Copyright ? 2015 Elsevier Ltd. All rights reserved.
PMID: 26365801 [PubMed - as supplied by publisher]
[h=1]Structural Basis for a Novel Interaction between the NS1 Protein Derived from the 1918 Influenza Virus and RIG-I.[/h] Jureka AS[SUP]1[/SUP], Kleinpeter AB[SUP]1[/SUP], Cornilescu G[SUP]2[/SUP], Cornilescu CC[SUP]2[/SUP], Petit CM[SUP]3[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] The influenza non-structural protein 1 (NS1) plays a critical role in antagonizing the innate immune response to infection. One interaction that facilitates this function is between NS1 and RIG-I, one of the main sensors of influenza virus infection. While NS1 and RIG-I are known to interact, it is currently unclear whether this interaction is direct or if it is mediated by other biomolecules. Here we demonstrate a direct, strain-dependent interaction between the NS1 RNA binding domain (NS1[SUP]RBD[/SUP]) of the influenza A/Brevig Mission/1918 H1N1 (1918[SUP]H1N1[/SUP]) virus and the second caspase activation and recruitment domain of RIG-I. Solving the solution structure of the 1918[SUP]H1N1[/SUP] NS1[SUP]RBD[/SUP] revealed features in a functionally novel region that may facilitate the observed interaction. The biophysical and structural data herein suggest a possible mechanism by which strain-specific differences in NS1 modulate influenza virulence.
Copyright ? 2015 Elsevier Ltd. All rights reserved.
PMID: 26365801 [PubMed - as supplied by publisher]