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- EMDB-19396: FAdV-C4 Aviadenovirus structure, strain AG234 -

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Basic information

Entry
Database: EMDB / ID: EMD-19396
TitleFAdV-C4 Aviadenovirus structure, strain AG234
Map data
Sample
  • Virus: Fowl aviadenovirus 4
Keywordsadenovirus / fowl / highly thermostable / VIRUS
Biological speciesFowl aviadenovirus 4
Methodsingle particle reconstruction / cryo EM / Resolution: 3.2 Å
AuthorsPerez-Illana MP / Schachnner A / Condezo GN / Hernando-Perez M / Martinez M / Marabini R / Hess M / San Martin C
Funding support2 items
OrganizationGrant numberCountry
Other privateLa Caixa Foundation (ID 100010434),La Caixa Foundation (ID 100010434),LCF/BQ/SO16/52270032)
Other governmentco-funded by the Spanish State Research Agency and the European Regional Development Fund, PID2022-136456NB-I00/ AEI/10.13039/501100011033/FEDER,UE
CitationJournal: PLoS Pathog / Year: 2025
Title: Aviadenovirus structure: A highly thermostable capsid in the absence of stabilizing proteins.
Authors: Marta Pérez-Illana / Anna Schachner / Mercedes Hernando-Pérez / Gabriela N Condezo / Alberto Paradela / Marta Martínez / Roberto Marabini / Michael Hess / Carmen San Martín /
Abstract: High-resolution structural studies have mainly focused on two out of the six adenovirus genera: mastadenoviruses and atadenoviruses. Here we report the high-resolution structure of an aviadenovirus, ...High-resolution structural studies have mainly focused on two out of the six adenovirus genera: mastadenoviruses and atadenoviruses. Here we report the high-resolution structure of an aviadenovirus, the poultry pathogen fowl adenovirus serotype 4 (FAdV-C4). FAdV-C4 virions are highly thermostable, despite lacking minor coat and core proteins shown to stabilize the mast- and atadenovirus particles, having no genus-specific cementing proteins, and packaging a 25% longer genome. Unique structural features of the FAdV-C4 hexon include a large insertion at the trimer equatorial region, and a long N-terminal tail. Protein IIIa conformation is closer to atadenoviruses than to mastadenoviruses, while protein VIII diverges from all previously reported structures. We interpret these differences in light of adenovirus evolution. Finally, we discuss the possible role of core composition in determining capsid stability properties. These results enlarge our view on the structural diversity of adenoviruses, and provide useful information to counteract fowl pathogens or use non-human adenoviruses as vectors.
History
DepositionJan 11, 2024-
Header (metadata) releaseJan 29, 2025-
Map releaseJan 29, 2025-
UpdateOct 22, 2025-
Current statusOct 22, 2025Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_19396.png

Downloads & links

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Map

FileDownload / File: emd_19396.map.gz / Format: CCP4 / Size: 1.6 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
1.38 Å/pix.
x 752 pix.
= 1034. Å		1.38 Å/pix.
x 752 pix.
= 1034. Å		1.38 Å/pix.
x 752 pix.
= 1034. Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.375 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.055
Minimum - Maximum-0.12381991 - 0.21060576
Average (Standard dev.)0.00063285825 (±0.016218984)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-376-376-376
Dimensions752752752
Spacing752752752
CellA=B=C: 1034.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_19396_half_map_1.map
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram

Histogram (log scale)

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Half map: #1

Fileemd_19396_half_map_2.map
Projections & Slices
AxesZYX

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Histogram

Histogram (log scale)

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Sample components

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Entire : Fowl aviadenovirus 4

EntireName: Fowl aviadenovirus 4
Components
  • Virus: Fowl aviadenovirus 4

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Supramolecule #1: Fowl aviadenovirus 4

SupramoleculeName: Fowl aviadenovirus 4 / type: virus / ID: 1 / Parent: 0 / NCBI-ID: 130663 / Sci species name: Fowl aviadenovirus 4 / Virus type: VIRION / Virus isolate: SPECIES / Virus enveloped: No / Virus empty: Yes
Host (natural)Organism: Gallus gallus (chicken)

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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

BufferpH: 7.8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Average electron dose: 40.5 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsCalibrated magnification: 97902 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING ONLY
Startup modelType of model: OTHER
Final reconstructionApplied symmetry - Point group: I (icosahedral) / Resolution.type: BY AUTHOR / Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 40383
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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