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- EMDB-18483: Herpes simplex virus 1 nuclear C-capsid (WT) vertices determined ... -

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Basic information

Entry
Database: EMDB / ID: EMD-18483
TitleHerpes simplex virus 1 nuclear C-capsid (WT) vertices determined in situ
Map dataFiltered, unmasked
Sample
  • Virus: Human alphaherpesvirus 1 (Herpes simplex virus type 1)
KeywordsCapsid / capsid vertex specific component / in situ / virus
Biological speciesHuman alphaherpesvirus 1 (Herpes simplex virus type 1)
Methodsubtomogram averaging / cryo EM / Resolution: 32.0 Å
AuthorsMironova Y / Prazak V / Vasishtan D
Funding support United Kingdom, Germany, 5 items
OrganizationGrant numberCountry
Wellcome Trust209250/Z/17/Z United Kingdom
Wellcome Trust099683/Z/12/Z United Kingdom
Wellcome Trust090532/Z/09/Z United Kingdom
German Research Foundation (DFG)390874280 Germany
German Research Foundation (DFG)453548970 Germany
CitationJournal: Nat Microbiol / Year: 2024
Title: Molecular plasticity of herpesvirus nuclear egress analysed in situ.
Authors: Vojtěch Pražák / Yuliia Mironova / Daven Vasishtan / Christoph Hagen / Ulrike Laugks / Yannick Jensen / Saskia Sanders / John M Heumann / Jens B Bosse / Barbara G Klupp / Thomas C ...Authors: Vojtěch Pražák / Yuliia Mironova / Daven Vasishtan / Christoph Hagen / Ulrike Laugks / Yannick Jensen / Saskia Sanders / John M Heumann / Jens B Bosse / Barbara G Klupp / Thomas C Mettenleiter / Michael Grange / Kay Grünewald /
Abstract: The viral nuclear egress complex (NEC) allows herpesvirus capsids to escape from the nucleus without compromising the nuclear envelope integrity. The NEC lattice assembles on the inner nuclear ...The viral nuclear egress complex (NEC) allows herpesvirus capsids to escape from the nucleus without compromising the nuclear envelope integrity. The NEC lattice assembles on the inner nuclear membrane and mediates the budding of nascent nucleocapsids into the perinuclear space and their subsequent release into the cytosol. Its essential role makes it a potent antiviral target, necessitating structural information in the context of a cellular infection. Here we determined structures of NEC-capsid interfaces in situ using electron cryo-tomography, showing a substantial structural heterogeneity. In addition, while the capsid is associated with budding initiation, it is not required for curvature formation. By determining the NEC structure in several conformations, we show that curvature arises from an asymmetric assembly of disordered and hexagonally ordered lattice domains independent of pUL25 or other viral capsid vertex components. Our results advance our understanding of the mechanism of nuclear egress in the context of a living cell.
History
DepositionSep 19, 2023-
Header (metadata) releaseApr 17, 2024-
Map releaseApr 17, 2024-
UpdateOct 30, 2024-
Current statusOct 30, 2024Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_18483.png

Downloads & links

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Map

FileDownload / File: emd_18483.map.gz / Format: CCP4 / Size: 1.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationFiltered, unmasked
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
8.6 Å/pix.
x 92 pix.
= 791.2 Å		8.6 Å/pix.
x 60 pix.
= 516. Å		8.6 Å/pix.
x 92 pix.
= 791.2 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

generated in cubic-lattice coordinate

Voxel sizeX=Y=Z: 8.6 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.335
Minimum - Maximum-152.46884 - 89.118449999999996
Average (Standard dev.)-28.052506999999999 (±21.423432999999999)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions609292
Spacing926092
CellA: 791.2 Å / B: 516.0 Å / C: 791.2 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_18483_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Unfiltered

Fileemd_18483_half_map_2.map
AnnotationUnfiltered
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Human alphaherpesvirus 1

EntireName: Human alphaherpesvirus 1 (Herpes simplex virus type 1)
Components
  • Virus: Human alphaherpesvirus 1 (Herpes simplex virus type 1)

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Supramolecule #1: Human alphaherpesvirus 1

SupramoleculeName: Human alphaherpesvirus 1 / type: virus / ID: 1 / Parent: 0 / NCBI-ID: 10298 / Sci species name: Human alphaherpesvirus 1 / Sci species strain: 17 / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: No

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Experimental details

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Structure determination

Methodcryo EM
Processingsubtomogram averaging
Aggregation statecell

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Sample preparation

BufferpH: 7.5
GridModel: Quantifoil R2/2 / Material: GOLD / Support film - topology: HOLEY
VitrificationCryogen name: ETHANE-PROPANE / Chamber humidity: 70 % / Chamber temperature: 310.15 K
Details: Vitrified samples were milled using dual beam cryo-FIB-SEM (Aquilos).

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Electron microscopy

MicroscopeTFS KRIOS
Specialist opticsEnergy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average exposure time: 0.4 sec. / Average electron dose: 2.5 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 6.0 µm / Nominal defocus min: 5.0 µm / Nominal magnification: 26000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Final reconstructionApplied symmetry - Point group: C5 (5 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 32.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: PEET / Number subtomograms used: 1170
ExtractionNumber tomograms: 14 / Number images used: 1170 / Software - Name: IMOD
Final angle assignmentType: OTHER / Software - Name: PEET
FSC plot (resolution estimation)

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