RIG-I Selectively Discriminates against 5'-Monophosphate RNA.
By Xiaoming Ren, Melissa M. Linehan, A. Iwasaki, Anna Marie Pyle. 2019
54 citations recorded by the source corpus.
The innate immune sensor RIG-I must sensitively detect and respond to viral RNAs that enter the cytoplasm, while remaining unresponsive to the abundance of structurally similar RNAs that are the products of host metabolism. In the case of RIG-I, these viral and host targets differ by only a few atoms, and a molecular mechanism for such selective differentiation has remained elusive. Using a combination of quantitative biophysical and immunological studies, we show that RIG-I, which is normally activated by duplex RNAs containing a 5'-tri- or diphosphate (5'-ppp or 5'-pp RNAs), is actively antagonized by RNAs containing 5'-monophosphates (5'-p RNAs). This is accomplished by a gating mechanism in which an alternative RIG-I conformation blocks the C-terminal domain (CTD) upon 5'-p RNA binding, thereby short circuiting the activation of signaling.
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, methodology): “HF complexes form a reduced network of interactions with dsRNA, which is consistent with their fast off rates (Devarkar et al., 2018;Rawling et al., 2015) and lowbinding affinity (Ren et al., 2019; Vela et al., 2012).”