Mechanisms of length-dependent recognition of viral double-stranded RNA by RIG-I

Retinoic acid-inducible gene I (RIG-I) is the most front-line cytoplasmic viral RNA sensor and induces antiviral immune responses. RIG-I recognizes short double-stranded (dsRNA) ( 500 bp) to trigger antiviral signaling. Since RIG-I is capable of binding with dsRNA irrespective of size, length-depend...

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Bibliographic Details
Published in:Scientific reports 2023-04, Vol.13 (1), p.6318-6318, Article 6318
Main Authors: Im, Jung Hyun, Duic, Ivana, Yoshimura, Shige H., Onomoto, Koji, Yoneyama, Mitsutoshi, Kato, Hiroki, Fujita, Takashi
Format: Article
Language:English
Subjects:
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Biological activity
DEAD Box Protein 58 - metabolism
DEAD-box RNA Helicases - genetics
Double-stranded RNA
Humanities and Social Sciences
Humans
Immune response
Immunology
Interferon-Induced Helicase, IFIH1 - genetics
multidisciplinary
Oligomerization
Proteins
Retinoic acid
RNA, Double-Stranded
RNA, Viral - metabolism
Science
Science (multidisciplinary)
Signal Transduction
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Summary:Retinoic acid-inducible gene I (RIG-I) is the most front-line cytoplasmic viral RNA sensor and induces antiviral immune responses. RIG-I recognizes short double-stranded (dsRNA) ( 500 bp) to trigger antiviral signaling. Since RIG-I is capable of binding with dsRNA irrespective of size, length-dependent RIG-I signaling remains elusive. Here, we demonstrated that RIG-I bound to long dsRNA with slow kinetics. Remarkably, RIG-I/short dsRNA complex efficiently dissociated in an ATP hydrolysis-dependent manner, whereas RIG-I/long dsRNA was stable and did not dissociate. Our study suggests that the dissociation of RIG-I from RIG-I/dsRNA complex could be a step for efficient antiviral signaling. Dissociated RIG-I exhibited homo-oligomerization, acquiring ability to physically associate with MAVS, and biological activity upon introduction into living cells. We herein discuss common and unique mechanisms of viral dsRNA recognition by RIG-I and MDA5.
ISSN:2045-2322
2045-2322
DOI:10.1038/s41598-023-33208-w