elifesciences.org CORRECTION Correction: Structural basis for the prion-like MAVS filaments in antiviral innate immunity Hui Xu 1,2 , Xiaojing He 3 , Hui Zheng 1 , Lily J Huang 1 , Fajian Hou 2† , Zhiheng Yu 4 , Michael Jason de la Cruz 4 , Brian Borkowski 1 , Xuewu Zhang 3 *, Zhijian J Chen 2,5 *, Qiu-Xing Jiang 1 * 1 Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, United States; 2 Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, United States; 3 Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, United States; 4 CryoEM Shared Resources, Janelia Farm Research Campus, Howard Hughes Medical Institute, Ashburn, United States; 5 Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, United States Xu H, He X, Zheng H, Huang LJ, Hou F, Yu Z, de la Cruz MJ, Borkowski B, Zhang X, Chen ZJ, Jiang Q-X. 2014. Structural basis for the prion-like MAVS filaments in antiviral innate immunity. eLife 3:e01489. doi: 10.7554/eLife.01489. Published 25 February 2014 Introduction 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). Results and discussion CryoEM images of Flag-tagged MAVS CARD (residues 1–100) protein, which was expressed in HEK293T cells and purified as described previously (Xu et al., 2014), were collected using automated data acquisition in a Titan Krios with a Falcon II direct electron detector (Figure 1A; see ‘Materials and methods’ section for detail). Fourier transforms of motion-corrected raw images showed Thon rings up to ∼3 ˚ A(Figure 1B–C). After CTF fitting, the selected raw images were phase-flipped, and Reviewing editor: Wesley I Sundquist, University of Utah School of Medicine, United States *For correspondence: xuewu. zhang@utsouthwestern.edu (XZ); zhijian.chen@utsouthwestern.edu (ZJC); qiu-xing.jiang@ utsouthwestern.edu (QXJ) Present address: † State Key Laboratory of Cell Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China Competing interests: See page 7 Published: 28 August 2015 Copyright Xu et al. This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited. Xu et al. eLife 2015;4:e07546. DOI: 10.7554/eLife.07546 1 of 7