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Structural basis for a novel interaction between the NS1 protein derived from the 1918 influenza virus and RIG-I #MMPMID26365801
Jureka AS; Kleinpeter AB; Cornilescu G; Cornilescu CC; Petit CM
Structure 2015[Nov]; 23 (11): 2001-10 PMID26365801show ga
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.