ArticleeLife2014
Structural basis for the prion-like MAVS filaments in antiviral innate immunity.
Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 119 papers.
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Who cites it
119 citing papers in PubMed.
- Structural insights into human caspase-9 CARD assembly modes driven by conserved arginine hotspots.Journal of structural biology: X · 2026Article
- The NLRP3 inflammasome at the crossroads of innate immune signaling and cell death.Cellular & molecular immunology · 2026Review
- Chronic type II interferon promotes tumor growth through mitochondrial RNA-induced type I interferon and prostaglandin synthesis.Science (New York, N.Y.) · 2026Article
- Article
- Review
- A Multiscale Computational Architecture to Study Signaling Dynamics at Cell-Cell Interfaces.bioRxiv : the preprint server for biology · 2026Article
- C-terminal tail of MAVS dictates organelle targeting and innate immune response.Cell communication and signaling : CCS · 2026Article
- Prion-like MAVS fibrils stitch mitochondria to promote a rapid antiviral response.Cellular & molecular immunology · 2026Article
- A methylome-derived mbioRxiv : the preprint server for biology · 2026Article
- The APC/C subunit APC7 exerts antiviral effects by targeting the adaptor protein MAVS.Frontiers in immunology · 2026Article
- Negative regulators antagonizing antitumor innate immune pathways in lung cancer immune evasion.Frontiers in immunology · 2026Review
- Old dogs-new tricks: multifaceted functions of MAVS beyond antivirus activity in human health and diseases.Cell & bioscience · 2025Review
- Phytochemicals Prime RIG-I Signaling and Th1-Leaning Responses in Human Monocyte-Derived Dendritic Cells.Nutrients · 2025Article
- ARIES domains: functional signaling units of type I interferon responses.The FEBS journal · 2025Review
- Kaposi's sarcoma-associated herpesvirus induces mitochondrial fission to evade host immune responses and promote viral production.Nature microbiology · 2025Article
- Itaconate modulates immune responses via inhibition of peroxiredoxin 5.Nature metabolism · 2025Article
- ASFV pS183L protein negatively regulates RLR-mediated antiviral signalling by blocking MDA5 oligomerisation.Veterinary research · 2025Article
- Signalling by co-operative higher-order assembly formation: linking evidence at molecular and cellular levels.The Biochemical journal · 2025Review
- A structural atlas of death domain fold proteins reveals their versatile roles in biology and function.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- NOD-like receptors in fish: evolution, structure, immune signaling, and targeting for aquaculture vaccine adjuvants.Frontiers in immunology · 2025Review
59 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
- Erratum issued
Authors and funding
11 authors.
Funding
Abstract
Mitochondrial antiviral signaling (MAVS) protein is required for innate immune responses against RNA viruses. In virus-infected cells MAVS forms prion-like aggregates to activate antiviral signaling cascades, but the underlying structural mechanism is unknown. Here we report cryo-electron microscopic structures of the helical filaments formed by both the N-terminal caspase activation and recruitment domain (CARD) of MAVS and a truncated MAVS lacking part of the proline-rich region and the C-terminal transmembrane domain. Both structures are left-handed three-stranded helical filaments, revealing specific interfaces between individual CARD subunits that are dictated by electrostatic interactions between neighboring strands and hydrophobic interactions within each strand. Point mutations at multiple locations of these two interfaces impaired filament formation and antiviral signaling. Super-resolution imaging of virus-infected cells revealed rod-shaped MAVS clusters on mitochondria. These results elucidate the structural mechanism of MAVS polymerization, and explain how an α-helical domain uses distinct chemical interactions to form self-perpetuating filaments. DOI: http://dx.doi.org/10.7554/eLife.01489.001.
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