Correction: Structural basis for the prion-like MAVS filaments in antiviral innate immunity

Mitochondrial antiviral signaling (MAVS) protein forms prion-like aggregates mediated by the N-terminal caspase activation and recruitment domain (CARD) and activates antiviral signaling cascades. Purified MAVS CARD from culture cells self-assembles into filaments. Previously, we reported a low-resolution cryoEM structure of MAVS CARD filament, which exhibits a C3 symmetry with a rotation of −53.6° and an axial rise of 16.8 A for every unit in the filament (Xu et al., 2014). Recently, a cryoEM reconstruction of MAVS CARD filaments at 3.6 A resolution was reported with a C1 helical symmetry of a rotation of −101.1° and an axial rise of 5.1 A per subunit (Wu et al., 2014). The differences in these two models were carefully analyzed recently (Egelman, 2014), which suggested that the helical ambiguity in helical reconstruction was not fully resolved in our previous analysis (Xu et al., 2014). We recently collected a new dataset at higher resolutions. Using a newly developed method for analysis of helical filaments (Clemens et al., 2015), we obtained a 4.2 A resolution reconstruction of MAVS CARD filaments purified from mammalian cells under native conditions. The new model shows that the MAVS CARD filament exhibits a C1 helical symmetry in agreement with Wu et al. (2014).