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The stress granule protein G3BP1 binds viral dsRNA and RIG-I to enhance IFN-β response.

著者 Kim SS , Sze L , Lam KP
J Biol Chem.2019 Feb 25 ; ():.
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RIG-I senses viral RNA in the cytosol and initiates host innate immune response by triggering the production of type 1 interferon.  A recent RNAi knockdown screen yielded close to hundred host genes whose products affected viral RNA-induced IFN-β production and highlighted the complexity of the antiviral response.  The stress granule protein G3BP1, known to arrest mRNA translation, was identified as a regulator of RIG-I-induced IFN-β production. How G3BP1 functions in RIG-I signaling is not known, however.  Here, we overexpress G3BP1 with RIG-I in HEK293T cells and found that G3BP1 significantly enhances RIG-I-induced mRNA synthesis. More importantly, we demonstrate that G3BP1 binds RIG-I and that this interaction involves the C-terminal RGG domain of G3BP1. Confocal microscopy studies also show G3BP1 co-localization with RIG-I and with infecting vesicular stomatitis virus in Cos-7 cells.  Interestingly, immunoprecipitation studies using biotin-labeled viral dsRNA or poly(I:C) and cell lysate-derived or in-vitro translated G3BP1 indicated that G3BP1 could directly bind these substrates and again, via its RGG domain.  Computational modeling further revealed a juxtaposed interaction between G3BP1 RGG and RIG-I RNA-binding domains.  Together, our data reveal G3BP1 as a critical component of RIG-I signaling and possibly, acting as a co-sensor to promote RIG-I recognition of pathogenic RNA.
PMID: 30804210 [PubMed - as supplied by publisher]
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