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Updated: May 2, 2026

Engineering Antiviral Agents via Surface Plasmon Resonance
Published on: June 14, 2022
Three-stranded antiviral attack.
Jenish R Patel1, Adolfo García-Sastre
1Jenish R Patel is in the Department of Microbiology, and the Global Health and Emerging Pathogens Institute, Icahn School of Medicine at Mount Sinai, New York, United States jenish.patel@mssm.edu.
Mitochondrial antiviral signalling proteins assemble into a helical filament crucial for cellular antiviral defense. This structure is key to how cells detect and respond to viral infections.
Area of Science:
- Cellular biology
- Immunology
- Virology
Background:
- Mitochondrial antiviral signalling (MAVS) proteins are critical mediators of innate immunity.
- MAVS initiates signalling cascades in response to viral detection.
- The structural organization of MAVS is essential for its function.
Purpose of the Study:
- To elucidate the structural basis of MAVS filament formation.
- To understand how MAVS structure relates to its antiviral signalling function.
Main Methods:
- Cryo-electron microscopy (Cryo-EM) was used to determine the high-resolution structure of the MAVS filament.
- Biochemical assays were employed to study filament assembly and dynamics.
Main Results:
- Mitochondrial antiviral signalling proteins form a unique three-stranded helical filament.
- The helical structure reveals specific interfaces involved in protein-protein interactions and filament stabilization.
- Structural insights explain the mechanism of MAVS polymerization.
Conclusions:
- The intricate helical filament structure of MAVS is fundamental to its role in cellular antiviral responses.
- Understanding MAVS filament structure provides a basis for developing novel antiviral therapeutics.
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