Contrasting functions of ATP hydrolysis by MDA5 and LGP2 in viral RNA sensing
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Abstract
Cytosolic long dsRNA, among the most potent proinflammatory signals, is recognized by melanoma differentiation-associated protein 5 (MDA5). MDA5 binds dsRNA cooperatively forming helical filaments. ATP hydrolysis by MDA5 fulfills a proofreading function by promoting dissociation of shorter endogenous dsRNs from MDA5 while allowing longer viral dsRNAs to remain bound leading to activation of interferon-β responses. Here, we show that adjacent MDA5 subunits in MDA5-dsRNA filaments hydrolyze ATP cooperatively, inducing cooperative filament disassembly. Consecutive rounds of ATP hydrolysis amplify the filament footprint, displacing tightly bound proteins from dsRNA. Our electron microscopy and biochemical assays show that LGP2 binds to dsRNA at internal binding sites through noncooperative ATP hydrolysis. Unlike MDA5, LGP2 has low nucleic acid selectivity and can hydrolyze GTP and CTP as well as ATP. Binding of LGP2 to dsRNA promotes nucleation of MDA5 filament assembly resulting in shorter filaments. Molecular modeling identifies an internally bound MDA5-LGP2-RNA complex, with the LGP2 C-terminal tail forming the key contacts with MDA5. These contacts are specifically required for NTP-dependent internal RNA binding. We conclude that NTPase-dependent binding of LGP2 to internal dsRNA sites complements NTPase-independent binding to dsRNA ends, via distinct binding modes, to increase the number and signaling output of MDA5-dsRNA complexes.
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- Authors
- Singh, R., Wu, Y., Herrero del Valle, A., Leigh, K. E., Mong, S., Cheng, M. T. K., Ferguson, B. J., & Modis, Y.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- University of Cambridge (GB)
- Corresponding author
- Ferguson, Brian J.
- Modis, Yorgo
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2024-03
- Volume
- 300
- Issue
- 3
- Pages
- 105711
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC10909783
- OpenAlex
- W4391424552
- Cited by
- 16
- References
- 57
- Citations by year
- 2026: 4 · 2025: 7 · 2024: 5
- FWCI
- 2.68
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Human Frontier Science Program (LT000454/2021-L)
- University of Cambridge
- Wellcome Trust (101908/Z/13/Z, 217191/Z/19/Z, 215378/Z/19/Z)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
- Keywords
- MDA5, LGP2, ATP hydrolysis, interferon-beta signaling, filament disassembly, proofreading, nucleoside triphosphatase, RNA binding, viral RNA sensing, innate immunity
- MeSH terms
- Interferon-Induced Helicase, IFIH1, Adenosine Triphosphate, Humans, Hydrolysis, Immunity, Innate, RNA, Double-Stranded, RNA, Viral, RNA Helicases, Nucleoside-Triphosphatase, DEAD-box RNA Helicases
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Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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