|Entry||Database: EMDB / ID: 6445|
|Title||Atomic structure of a non-enveloped virus reveals pH sensors for a coordinated process of cell entry|
|Map data||The whole map of BTV virion at pH 3.4 without imposing a reverse B-factor to boost high frequency signals|
|Sample||BTV virion at pH 3.4 without imposing a reverse B-factor to boost high frequency signals|
|Keywords||Non-enveloped virus / cell entry / cryo-EM / pH sensor|
|Source||Bluetongue virus 1 / virus|
|Method||single particle reconstruction / cryo EM / 3.3 Å resolution|
|Authors||Zhang X / Patel A / Celma C / Roy P / Zhou ZH|
|Citation||Journal: Nat. Struct. Mol. Biol. / Year: 2016|
Title: Atomic model of a nonenveloped virus reveals pH sensors for a coordinated process of cell entry.
Authors: Xing Zhang / Avnish Patel / Cristina C Celma / Xuekui Yu / Polly Roy / Z Hong Zhou
Abstract: Viruses sense environmental cues such as pH to engage in membrane interactions for cell entry during infection, but how nonenveloped viruses sense pH is largely undefined. Here, we report both high- ...Viruses sense environmental cues such as pH to engage in membrane interactions for cell entry during infection, but how nonenveloped viruses sense pH is largely undefined. Here, we report both high- and low-pH structures of bluetongue virus (BTV), which enters cells via a two-stage endosomal process. The receptor-binding protein VP2 possesses a zinc finger that may function to maintain VP2 in a metastable state and a conserved His866, which senses early-endosomal pH. The membrane-penetration protein VP5 has three domains: dagger, unfurling and anchoring. Notably, the β-meander motif of the anchoring domain contains a histidine cluster that can sense late-endosomal pH and also possesses four putative membrane-interaction elements. Exposing BTV to low pH detaches VP2 and dramatically refolds the dagger and unfurling domains of VP5. Our biochemical and structure-guided-mutagenesis studies support these coordinated pH-sensing mechanisms.
|Date||Deposition: Aug 27, 2015 / Header (metadata) release: Sep 23, 2015 / Map release: Dec 9, 2015 / Last update: Jan 20, 2016|
|Structure viewer||EM map: |
Downloads & links
|File||emd_6445.map.gz (map file in CCP4 format, 524289 KB)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.89 Å|
CCP4 map header:
-Entire BTV virion at pH 3.4 without imposing a reverse B-factor to boost...
|Entire||Name: BTV virion at pH 3.4 without imposing a reverse B-factor to boost high frequency signals|
Number of components: 1
-Component #1: virus, Bluetongue virus 1
|Specimen||Specimen state: particle / Method: cryo EM|
|Sample solution||Buffer solution: citrate buffer / pH: 3.4|
|Support film||thin carbon on a lacey holey carbon support film|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Temperature: 90 K / Humidity: 100 %|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS / Date: May 11, 2011|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Camera||Detector: GATAN ULTRASCAN 4000 (4k x 4k)|
|Image acquisition||Number of digital images: 350 / Sampling size: 15 microns / Bit depth: 32|
|Processing||Method: single particle reconstruction / Applied symmetry: I (icosahedral) / Number of projections: 4503|
|3D reconstruction||Algorithm: reference match / Software: Frealign / CTF correction: each particle / Resolution: 3.3 Å / Resolution method: FSC 0.143, semi-independent|
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