Structural Basis for a Novel Interaction between the NS1 Protein Derived from the 1918 Influenza Virus and RIG-I.
Structural Basis for a Novel Interaction between the NS1 Protein Derived from the 1918 Influenza Virus and RIG-I.
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DOI：
10.1016/j.str.2015.08.007
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发表时间：
2015-11-03
期刊：
影响因子：
--
通讯作者：
Petit CM
中科院分区：
文献类型：
--
作者：
Jureka AS;Kleinpeter AB;Cornilescu G;Cornilescu CC;Petit CM
The influenza nonstructural 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. In the present study, we demonstrate a direct, strain dependent interaction between the NS1 RNA binding domain (NS1RBD) of the influenza A/Brevig Mission/1918 H1N1 (1918H1N1) virus and the second CARD domain of RIG-I. Solving the solution structure of the 1918H1N1 NS1RBD 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.
