Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Published Erratum
. 2015 Aug 28:4:e07546.
doi: 10.7554/eLife.07546.

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

Hui Xu  1 , Xiaojing He  2 , Hui Zheng  1 , Lily J Huang  1 , Fajian Hou  3 , Zhiheng Yu  4 , Michael Jason de la Cruz  4 , Brian Borkowski  1 , Xuewu Zhang  2 , Zhijian J Chen  3 , Qiu-Xing Jiang  1
Affiliations
Published Erratum

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

Hui Xu et al. Elife. .
No abstract available

Keywords: MAVS; biophysics; cryoEM reconstruction; human; immunology; innate immunity; prion-like filaments; structural biology; viruses.

PubMed Disclaimer

Conflict of interest statement

ZJC: Reviewing editor, eLife.

The other authors declare that no competing interests exist.

Figures

Figure 1.
Figure 1.. Analyses of high-resolution cryoEM images of MAVS CARD filaments.
(A) A representative EM image after motion correction. (B) The power spectrum of a motion-corrected image showing Thon rings up to ∼3 Å (bottom arrow), with the CTF fittings (white concentric rings) exhibited as white flat annuli over the power spectrum. The CTF fitting was done with CTFFIND4. (C) The quality of the CTF fitting was evaluated by comparing the rotationally averaged amplitudes from the Thon rings (green trace) with the averaged amplitudes of the fitted CTF function (dashed yellow trace). The Thon rings are visible to ∼3 Å, and the fitting is good to at least ∼4 Å (top arrow in B). (D) Representative class averages of the new dataset showing some fine structural features. The classification was done with Relion 2D classification. (E) Summed power spectra of filaments with less than 5° of out-of-plane tilt in the last step of refinement. Layer lines 9 and 32 (meridional) are labeled (yellow arrows). The contrast is enhanced to show layer line 32. The middle portion of the power spectrum is shown as a zoomed-in view to the top with layer lines 4 and 9 labeled. (F) Summed power of projections from the C1 map along 360 different directions normal to its helical axis. DOI: http://dx.doi.org/10.7554/eLife.07546.001
Figure 2.
Figure 2.. Molecular modeling based on the near-atomic resolution cryoEM map.
(A) A side view of the cryoEM map with an atomic model of human MAVS CARD docked as a rigid body (blue: atomic model of residues 1–97, PDB: 3J6J). The N- and C- termini face the periphery of the filament. (B) Gold-standard Fourier Shell Correlation (FSC) curve between maps calculated from the top and bottom two halves of the selected data. The dashed line points to the estimated resolution of 4.18 Å at FSC = 0.143. (C) FSC between the segmented cryoEM map of one CARD and the map calculated from the atomic model (PDB: 3J6J, residues 1–97). The 0.5 thresholding yielded an estimated resolution of 4.25 Å. (D) Zoomed-in views of the six α-helices with side chains shown as stick models and superimposed with the EM density (grey mesh). DOI: http://dx.doi.org/10.7554/eLife.07546.002
Figure 3.
Figure 3.. Molecular interfaces of the pseudoatomic model based on the C1 map.
(A) A model of the MAVS CARD filament based on the cryoEM map, showing three helical turns. Each MAVS CARD interacts with six nearest neighbors: two neighbors along the helical trajectory (grey and yellow), and four neighbors between helical turns (grey and cyan, grey and orange). (B, C) Details of interactions at type I and II interfaces. Residues at the interfaces are shown as stick models. (D) The segmented cryoEM map with two MAVS CARD molecules and a magnified view of type II interface with clear EM density for W56 and R43. (E) Important residues at type III interface shown as stick models. DOI: http://dx.doi.org/10.7554/eLife.07546.004
See this image and copyright information in PMC

Erratum for

References

    1. Clemens DL, Ge P, Lee BY, Horwitz MA, Zhou ZH. Atomic structure of T6SS reveals interlaced array essential to function. Cell. 2015;160:940–951. doi: 10.1016/j.cell.2015.02.005. - DOI - PMC - PubMed
    1. Egelman EH. Reconstruction of helical filaments and tubes. Methods in Enzymology. 2010;482:167–183. doi: 10.1016/S0076-6879(10)82006-3. - DOI - PMC - PubMed
    1. Egelman EH. Ambiguities in helical reconstruction. eLife. 2014;3:04969. doi: 10.7554/eLife.04969. - DOI - PMC - PubMed
    1. Emsley P, Lohkamp B, Scott WG, Cowtan K. Features and development of Coot. Acta Crystallographica. Section D, Biological Crystallography. 2010;66:486–501. doi: 10.1107/S0907444910007493. - DOI - PMC - PubMed
    1. Li X, Mooney P, Zheng S, Booth C, Braunfeld MB, Gubbens S, Agard DA, Cheng Y. Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nature Methods. 2013;10:584–590. doi: 10.1038/nmeth.2472. - DOI - PMC - PubMed

Publication types

LinkOut - more resources