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Structural Basis for a Novel Interaction between the NS1 Protein Derived from the 1918 Influenza Virus and RIG-I
Journal article   Peer reviewed

Structural Basis for a Novel Interaction between the NS1 Protein Derived from the 1918 Influenza Virus and RIG-I

Alexander S. Jureka, Alex B. Kleinpeter, Gabriel Cornilescu, Claudia C. Cornilescu and Chad M. Petit
Structure (London), Vol.23(11), pp.2001-2010
11/03/2015
DOI: 10.1016/j.str.2015.08.007
PMCID: PMC4635043
PMID: 26365801

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Abstract

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 RBD) of the influenza A/Brevig Mission/1918 H1N1 (1918 H1N1) virus and the second caspase activation and recruitment domain of RIG-I. Solving the solution structure of the 1918 H1N1 NS1 RBD 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.
Biochemistry & Molecular Biology Biophysics Cell Biology Life Sciences & Biomedicine Science & Technology

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