In today's eLife, Hui and colleagues published a paper on MAVS filaments.
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. 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.
Structural basis for the prion-like MAVS filaments in antiviral innate immunity.