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- EMDB-51321: Structure of IPNV L5 capsid -

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Basic information

Entry
Database: EMDB / ID: EMD-51321
TitleStructure of IPNV L5 capsid
Map data
Sample
  • Virus: Infectious pancreatic necrosis virus
    • Protein or peptide: Structural polyprotein
KeywordsSalmoid / Capsid / Birnavirus / Infectious pancreatic necrosis virus / IPNV / VIRUS
Function / homology
Function and homology information


Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases / serine-type peptidase activity / viral capsid / host cell cytoplasm / structural molecule activity / proteolysis / metal ion binding
Similarity search - Function
Birnavirus VP3, domain 2 / Birnavirus VP3, domain 1 / Birnavirus VP2 protein / Birnavirus VP3 protein / Birnavirus VP4 protease domain / Birnavirus VP2 protein / Birnavirus VP3 protein / Birnavirus VP4 protein / Birnavirus VP4 protease domain profile. / Viral coat protein subunit
Similarity search - Domain/homology
Structural polyprotein
Similarity search - Component
Biological speciesInfectious pancreatic necrosis virus
Methodsingle particle reconstruction / cryo EM / Resolution: 2.75 Å
AuthorsMunke A / Gamil A / Mikalsen A / Wang H / Evensen O / Okamoto K
Funding support Sweden, Norway, 6 items
OrganizationGrant numberCountry
Swedish Research Council2018-03387 Sweden
Swedish Research Council2023-01857 Sweden
Swedish Research Council2022-00236 Sweden
Swedish Research Council2018-00421 Sweden
Swedish Research Council2022-02347 Sweden
Norwegian Research Council324266 Norway
CitationJournal: J Virol / Year: 2025
Title: Structure of the T=13 capsid of infectious pancreatic necrosis virus (IPNV)-a salmonid birnavirus.
Authors: Anna Munke / Amr Ahmed Abdelrahim Gamil / Aase B Mikalsen / Han Wang / Øystein Evensen / Kenta Okamoto /
Abstract: Birnaviruses infect a broad range of vertebrate hosts, including fish and birds, and cause substantial economic losses in the fishery and livestock industries. The infectious pancreatic necrosis ...Birnaviruses infect a broad range of vertebrate hosts, including fish and birds, and cause substantial economic losses in the fishery and livestock industries. The infectious pancreatic necrosis virus (IPNV), an aquabirnavirus, specifically infects salmonids. While structures on T=1 subviral particles of the birnaviruses, including IPNV, have been studied, structural insights into the infectious T=13 particles have been limited to the infectious bursal disease virus (IBDV), an avibirnavirus. Determining the capsid structure of the T=13 particle of IPNV is crucial for advancing knowledge of its antigenicity, capsid assembly, and possible functional structures. Here, the capsid structure of the IPNV L5 strain has been determined at a resolution of 2.75 Å. The overall structure resembles the T=13 IBDV structure, with notable differences in the surface loops on the P domain of the VP2 capsid protein essential for antigenicity and virulence. Additionally, previously undescribed structural features have been identified, including the C-terminal regions of the VP2 subunits within the pentagonal assembly unit at each 5-fold axis, which interlock with adjacent VP2 subunits. This interlocking, together with class-averaged projections of triangular and pentagonal units, suggests that the pentagonal unit formation could be important for a correct T=13 particle assembly, preventing the formation of T=1 subviral particles. Furthermore, positively charged residues in obstructed capsid pores at each 5-fold axis are speculated to facilitate intraparticle genome synthesis of IPNV.IMPORTANCEAquabirnaviruses cause deadly infectious diseases in salmonid fish, posing significant challenges for both wild and farmed fish populations. The most prevalent aquabirnavirus worldwide is the infectious pancreatic necrosis virus, whose multifunctional capsid is critical to its infection, replication, and maturation. Previously, research has focused on the structure of the virus' non-infectious subviral capsid. In this study, however, the first structure of the large, infectious, and functional form of the capsid has been determined. This new capsid structure reveals functional motifs that were previously unclear in the non-infectious capsid. These motifs are believed to be essential for the virus' replication and particle assembly, making them promising targets for developing strategies to control virus proliferation.
History
DepositionAug 13, 2024-
Header (metadata) releaseJan 8, 2025-
Map releaseJan 8, 2025-
UpdateJul 23, 2025-
Current statusJul 23, 2025Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

Downloads & links

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Map

FileDownload / File: emd_51321.map.gz / Format: CCP4 / Size: 1.3 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.28 Å/pix.
x 700 pix.
= 898.8 Å
1.28 Å/pix.
x 700 pix.
= 898.8 Å
1.28 Å/pix.
x 700 pix.
= 898.8 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.284 Å
Density
Contour LevelBy AUTHOR: 0.92
Minimum - Maximum-1.9112991 - 3.982858
Average (Standard dev.)0.03813521 (±0.23051384)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-350-350-350
Dimensions700700700
Spacing700700700
CellA=B=C: 898.80005 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_51321_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #2

Fileemd_51321_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Sample components

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Entire : Infectious pancreatic necrosis virus

EntireName: Infectious pancreatic necrosis virus
Components
  • Virus: Infectious pancreatic necrosis virus
    • Protein or peptide: Structural polyprotein

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Supramolecule #1: Infectious pancreatic necrosis virus

SupramoleculeName: Infectious pancreatic necrosis virus / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / Details: Purified from infected cell culture fluid / NCBI-ID: 11002 / Sci species name: Infectious pancreatic necrosis virus / Sci species strain: L5 / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: No
Virus shellShell ID: 1 / T number (triangulation number): 13

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Macromolecule #1: Structural polyprotein

MacromoleculeName: Structural polyprotein / type: protein_or_peptide / ID: 1 / Number of copies: 13 / Enantiomer: LEVO
EC number: Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases
Source (natural)Organism: Infectious pancreatic necrosis virus / Strain: L5
Molecular weightTheoretical: 55.724777 KDa
SequenceString: MNTNKATATY LKSIMLPETG PASIPDDITE RHILKQETSS YNLEVSESGS GILVCFPGAP GSRIGAHYRW NANQTGLEFD QWLETSQDL KKAFNYGRLI SRKYDIQSST LPAGLYALNG TLNAATFEGS LSEVESLTYN SLMSLTTNPQ DKVNNQLVTK G VTVLNLPT ...String:
MNTNKATATY LKSIMLPETG PASIPDDITE RHILKQETSS YNLEVSESGS GILVCFPGAP GSRIGAHYRW NANQTGLEFD QWLETSQDL KKAFNYGRLI SRKYDIQSST LPAGLYALNG TLNAATFEGS LSEVESLTYN SLMSLTTNPQ DKVNNQLVTK G VTVLNLPT GFDKPYVRLE DETPQGLQSM NGAKMRCTAA IAPRRYEIDL PSQRLPPVPA TGTLTTLYEG NADIVNSTTV TG DINFGLA RQPADETTFH FQLDFMGLDN DVPVVTVVSS ALATTDNHRG VSAKMTQSIP TENITKPITR VKLSYKINQQ TAI DNVATL GTMGPASVSF SSGNGNVPGV LRPITLVAYE KMTPLSILTV AGVSNYELIP NPELLKNMVT RYGKYDPEGL NYAK MILSH REELDIRTVW RTEEYKERTR VFNEITDFSS DLPTSKAWGW RDIVRGIRKV AAPVLSTLFP MAAPLIGMAD QFIGD LTKT NAAGGRYHSM AAGGRYKDVL ESWA

UniProtKB: Structural polyprotein

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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

Concentration1.08 mg/mL
BufferpH: 7.4 / Details: PBS (-)
GridModel: Quantifoil R2/2 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Number grids imaged: 2 / Number real images: 27945 / Average electron dose: 26.8 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.7 µm / Nominal defocus min: 0.5 µm / Nominal magnification: 81000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: HELIUM
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 35498 / Details: including 12,898 dsRNA-genome filled particles
CTF correctionSoftware - Name: cryoSPARC (ver. 4.3.1) / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionApplied symmetry - Point group: I (icosahedral) / Resolution.type: BY AUTHOR / Resolution: 2.75 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.3.1) / Number images used: 35498
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.3.1)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.3.1)
Final 3D classificationSoftware - Name: cryoSPARC (ver. 4.3.1)

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Atomic model buiding 1

Initial modelChain - Source name: AlphaFold / Chain - Initial model type: in silico model / Details: Predicted from sequence
RefinementSpace: REAL / Protocol: AB INITIO MODEL
Output model

PDB-9gg2:
Structure of IPNV L5 capsid

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