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- EMDB-2076: CryoEM icosahedral reconstruction of AHSV4 -

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Basic information

Entry
Database: EMDB / ID: EMD-2076
TitleCryoEM icosahedral reconstruction of AHSV4
Map dataAHSV4 filled
Sample
  • Sample: AHSV4 filled
  • Virus: African horse sickness virus 4
KeywordsAHSV4 / cryoEM / structure
Biological speciesAfrican horse sickness virus 4
Methodsingle particle reconstruction / cryo EM / Resolution: 14.4 Å
AuthorsManole V / Laurinmaki P / Wyngaardt WV / Potgieter CA / Wright IM / Venter GJ / Dijk AAV / Sewell BT / Butcher SJ
CitationJournal: J Virol / Year: 2012
Title: Structural insight into African horsesickness virus infection.
Authors: Violeta Manole / Pasi Laurinmäki / Wouter Van Wyngaardt / Christiaan A Potgieter / Isabella M Wright / Gert J Venter / Alberdina A van Dijk / B Trevor Sewell / Sarah J Butcher /
Abstract: African horsesickness (AHS) is a devastating disease of horses. The disease is caused by the double-stranded RNA-containing African horsesickness virus (AHSV). Using electron cryomicroscopy and three- ...African horsesickness (AHS) is a devastating disease of horses. The disease is caused by the double-stranded RNA-containing African horsesickness virus (AHSV). Using electron cryomicroscopy and three-dimensional image reconstruction, we determined the architecture of an AHSV serotype 4 (AHSV-4) reference strain. The structure revealed triple-layered AHS virions enclosing the segmented genome and transcriptase complex. The innermost protein layer contains 120 copies of VP3, with the viral polymerase, capping enzyme, and helicase attached to the inner surface of the VP3 layer on the 5-fold axis, surrounded by double-stranded RNA. VP7 trimers form a second, T=13 layer on top of VP3. Comparative analyses of the structures of bluetongue virus and AHSV-4 confirmed that VP5 trimers form globular domains and VP2 trimers form triskelions, on the virion surface. We also identified an AHSV-7 strain with a truncated VP2 protein (AHSV-7 tVP2) which outgrows AHSV-4 in culture. Comparison of AHSV-7 tVP2 to bluetongue virus and AHSV-4 allowed mapping of two domains in AHSV-4 VP2, and one in bluetongue virus VP2, that are important in infection. We also revealed a protein plugging the 5-fold vertices in AHSV-4. These results shed light on virus-host interactions in an economically important orbivirus to help the informed design of new vaccines.
History
DepositionApr 18, 2012-
Header (metadata) releaseSep 26, 2012-
Map releaseSep 26, 2012-
UpdateFeb 20, 2013-
Current statusFeb 20, 2013Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 5000
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 5000
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

EMD-2076.png

Downloads & links

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Map

FileDownload / File: emd_2076.map.gz / Format: CCP4 / Size: 120.1 MB / Type: IMAGE STORED AS SIGNED INTEGER (2 BYTES)
AnnotationAHSV4 filled
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
2.8 Å/pix.
x 401 pix.
= 1122.8 Å		2.8 Å/pix.
x 401 pix.
= 1122.8 Å		2.8 Å/pix.
x 401 pix.
= 1122.8 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 2.8 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy EMDB: 3000.0 / Movie #1: 5000
Minimum - Maximum-17727.0 - 32443.0
Average (Standard dev.)1161.900146480000103 (±5294.345703130000402)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-200-200-200
Dimensions401401401
Spacing401401401
CellA=B=C: 1122.7999 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Integer*27
Å/pix. X/Y/Z2.82.82.8
M x/y/z401401401
origin x/y/z0.0000.0000.000
length x/y/z1122.8001122.8001122.800
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ128128168
MAP C/R/S123
start NC/NR/NS-200-200-200
NC/NR/NS401401401
D min/max/mean-17727.00032443.0001161.900

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Supplemental data

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Sample components

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Entire : AHSV4 filled

EntireName: AHSV4 filled
Components
  • Sample: AHSV4 filled
  • Virus: African horse sickness virus 4

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Supramolecule #1000: AHSV4 filled

SupramoleculeName: AHSV4 filled / type: sample / ID: 1000 / Number unique components: 1

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Supramolecule #1: African horse sickness virus 4

SupramoleculeName: African horse sickness virus 4 / type: virus / ID: 1 / Name.synonym: AHSV4 / NCBI-ID: 36421 / Sci species name: African horse sickness virus 4 / Virus type: VIRION / Virus isolate: SEROTYPE / Virus enveloped: No / Virus empty: No / Syn species name: AHSV4
Host (natural)Organism: Equus caballus (horse) / synonym: VERTEBRATES

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.2 mg/mL
BufferpH: 8.5 / Details: 2mM Tris-HCl, pH 8.5
GridDetails: Quantifoil 200 mesh holey carbon
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Instrument: FEI VITROBOT MARK III

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Electron microscopy

MicroscopeFEI TECNAI F20
DateFeb 1, 2009
Image recordingCategory: FILM / Film or detector model: KODAK SO-163 FILM / Digitization - Scanner: OTHER / Digitization - Sampling interval: 7 µm / Number real images: 307 / Average electron dose: 18 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsCalibrated magnification: 50000 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2 mm / Nominal defocus max: 5.0 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 50000
Sample stageSpecimen holder model: GATAN LIQUID NITROGEN
Experimental equipment
Model: Tecnai F20 / Image courtesy: FEI Company

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Image processing

CTF correctionDetails: each micrograph
Final reconstructionApplied symmetry - Point group: I (icosahedral) / Algorithm: OTHER / Resolution.type: BY AUTHOR / Resolution: 14.4 Å / Resolution method: FSC 0.5 CUT-OFF / Software - Name: AUTO3DEM / Number images used: 1633

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