Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA.

By E. Kowalinski, T. Lunardi, A. McCarthy, Jade Louber, J. Brunel, B. Grigorov, D. Gerlier, Stephen Cusack. 2011

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Citations in the corpus

The RIG-I receptor adopts two different conformations for distinguishing host from viral RNA ligands (2022, neutral): “Until now, our existing knowledge of RIG-I conformational states and RNA interactions has stemmed from a small set of crystal structures that were obtained under diverse conditions, using RIG-I truncation constructs employed in different laboratories, which makes it difficult to compare features tha”
Molecular mechanisms of RNA interference (2013, positive): “Data interpretation was bolstered by structure determination of the helicase RIG-I, which provided a model that was readily positioned into the EM density for the related helicase domain of human Dicer (43).”
Unified mechanisms for self-RNA recognition by RIG-I Singleton-Merten syndrome variants (2018, background): “SF2 and RD are crucial for RNA-recognition of RLRs, whereas 2CARD communicates successful RNA-binding events to downstream signaling factors (Jiang et al., 2011; Kowalinski et al., 2011; Luo et al., 2011).”
Cytosolic Sensing of Viruses (2013, background): “Thus, the CTD provides the basis for recognition of distinct RNA structures by RIG-I and MDA5.”
RNA binding activates RIG-I by releasing an autorepressed signaling domain (2019, background): “Therefore, it was predicted that the 2CARD/hel2i contact is broken upon RIG-I activation and that 2CARD is flipped into solution, making it sterically accessible for interaction with other proteins (12).”
The Thermodynamic Basis for Viral RNA Detection by the RIG-I Innate Immune Sensor (2012, background): “Despite its decoupling from theCTD, the isolatedHD retains affinity for dsRNA ligands, as suggested by crystallographic studies on the duck RIG-I helicase complex, which lacks the CTD (14).”
RIG-I uses an ATPase-powered translocation-throttling mechanism for kinetic proofreading of RNAs and oligomerization (2018, background): “5’ppp dsRNA binding disrupts CARD2:Hel2i interactions, aiding in CARDs release, and ATP binding facilitates this process (Zheng et al., 2015).”
Establishing the role of ATP for the function of the RIG-I innate immune sensor (2015, background): “DOI: 10.7554/eLife.09391 11 of 21 derives from a complex network of specific interactions with the 5′ triphosphate moiety and stacking interactions with the terminal base pair of an RNA duplex (Lu et al., 2010; Jiang et al., 2011; Kowalinski et al., 2011; Luo et al., 2011, 2012b).”
A structure-based model of RIG-I activation. (2012, methodology): “4C) and the absence of significant interaction between the isolated CTD and the complementary part of RIG-I in vitro (Kowalinski et al. 2011).”
Immune sensing of DNA (2013, neutral): “The RNA PRRs RIG-I and MDA5 have a defined signaling domain (CARD) as well as a nucleic acid binding DDX domain, and crystal structures for both receptors have revealed how they engage RNA and subsequently signal (Kowalinski et al., 2011; Luo et al., 2011; Wu et al., 2013a).”
Structure and Degradation of Circular RNAs Regulate PKR Activation in Innate Immunity. (2019, positive): “, 2008), and RIG-I binds to intracellular 50-triphosphate single-stranded RNA and panhandle-like blunt-end 50-triphosphate dsRNA (Kowalinski et al., 2011; Pichlmair et al., 2006).”
ATP hydrolysis by the viral RNA sensor RIG-I prevents unintentional recognition of self-RNA (2015, background): “…approximately matches the footprint of dsRNA across the two SF2 RecA domains in the crystal structure of ADP BeFx-bound RIG-I (Jiang et al., 2011; Kohlway et al., 2013; Kowalinski et al., 2011; Luo et al., 2011) and also meets the requirements for activation of RIG-I’s ATPase Figure supplement 1.”
Sequence-Specific Modifications Enhance the Broad-Spectrum Antiviral Response Activated by RIG-I Agonists (2015, background): “The elucidation of the crystal structure of RIG-I highlighted the molecular interactions between RIG-I and 5=ppp dsRNA (45–48) and provided a structural basis for the conformational changes involved in exposing the CARD domain for effective downstream signaling (49).”
An evolving arsenal: viral RNA detection by RIG-I-like receptors (2014, positive): “While this has been attributed to a potential interaction interface between Hel2i and other proteins, the same amino acids are actually located at the intramolecular interface between Hel2i and CARD2, which has been crystallographically visualized in truncated versions of the RIG-I protein [10 ] .”
Structural basis for m7G recognition and 2′-O-methyl discrimination in capped RNAs by the innate immune receptor RIG-I (2016, positive): “Interestingly, comparing the helicase domain from our Helicase-RD–5′ppp HP RNA complex with the previously reported structures of Helicase-RD bound to 5′ppp 8-bp HP RNA [Protein Data Bank (PDB) ID 4AY2] (16) and the unliganded duck RIG-I (PDB ID 4A2W) (5) yielded rmsds of 3.”