Preference of RIG-I for short viral RNA molecules in infected cells revealed by next-generation sequencing

By A. Baum, Ravi Sachidanandam, A. García‐Sastre. 2010

438 citations recorded by the source corpus.

Subfields: Immunology, Molecular Biology

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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): “Years of work by many labs has shown that the most potent triggers of the RIG-I response in biochemical experiments, in cells, and in living animals are double-stranded RNAs (dsRNAs), containing a blunt, base-paired terminus that is decorated with a 50-triphosphate (p3dsRNA) or 50-diphosphate (p2dsR”
A structure-based model of RIG-I activation. (2012, background): “Nevertheless, panhandle structures corresponding to the blunt-ended 59pppbpRNAs that act as RIG-I PAMPs in vitro occur in many ssRNA virus systems and have been implicated (Strahle et al. 2007; Schlee et al. 2009; Baum et al. 2010; Rehwinkel et al. 2010).”
Establishing the role of ATP for the function of the RIG-I innate immune sensor (2015, background): “, 2015), yet these RNAs do not induce immune signaling by RIGI, even at saturating concentrations (Schlee et al., 2009; Baum et al., 2010; Goubau et al., 2014).”
Influenza A Virus Panhandle Structure Is Directly Involved in RIG-I Activation and Interferon Induction (2015, background): “Two recent studies characterizing physiological RIG-I agonists during IAV infection demonstrated that RIG-I associates with both full-length viral genomes (preferentially shorter genome segments) and DI genomes (15, 18).”
Cytosolic Sensing of Viruses (2013, background): “Consistent with these two features, viral genomic RNA was identified as the physiological RIG-I agonist in cells infected with influenza and Sendai virus (Baum et al., 2010; Rehwinkel et al., 2010; Weber et al., 2013).”
The RIG-I ATPase core has evolved a functional requirement for allosteric stabilization by the Pincer domain (2014, background): “In addition to the ATPase core, RIG-I also contains a C-terminal domain (CTD) that enhances specificity for pathogenic RNA by recognizing the terminal 5′ triphosphate moiety (18–20) on genomic RNA (21,22) or replicative intermediates (23) of numerous RNA viruses such as influenza, flaviviruses, hepa”
Immune signaling by RIG-I-like receptors (2011, background): “Next-generation sequencing of RNA derived from RIG-I-bound RNA complexes isolated from influenza virus-infected cells confirm that RIG-I associates preferentially with short 50ppp-RNA sequence motifs along RNA containing some dsRNA regions (Baum et al., 2010).”
An evolving arsenal: viral RNA detection by RIG-I-like receptors (2014, background): “In RIG-I, the CTD has evolved to engage in a high affinity interaction with a triphosphate group [13,17,18 ] present at the dsRNA termini of deposited genomic RNA [19,20] or replicative intermediates [21] of target viruses (Figure 1 Detection).”