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- EMDB-45136: Infectious B19V capsid -

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Basic information

Entry
Database: EMDB / ID: EMD-45136
TitleInfectious B19V capsid
Map data
Sample
  • Virus: Human parvovirus B19
    • Protein or peptide: Capsid protein 2
KeywordsB19 / Virion / Capsid / VIRUS
Function / homologyParvovirus coat protein VP2 / Parvovirus coat protein VP1/VP2 / Parvovirus coat protein VP2 / Capsid/spike protein, ssDNA virus / T=1 icosahedral viral capsid / structural molecule activity / Capsid protein 2
Function and homology information
Biological speciesHuman parvovirus B19
Methodsingle particle reconstruction / cryo EM / Resolution: 2.2 Å
AuthorsLee H / Hafenstein S
Funding support1 items
OrganizationGrant numberCountry
Not funded
CitationJournal: Nat Commun / Year: 2024
Title: Infectious parvovirus B19 circulates in the blood coated with active host protease inhibitors.
Authors: Hyunwook Lee / Ruben Assaraf / Suriyasri Subramanian / Dan Goetschius / Jan Bieri / Nadia M DiNunno / Remo Leisi / Carol M Bator / Susan L Hafenstein / Carlos Ros /
Abstract: The lack of a permissive cell culture system has limited high-resolution structures of parvovirus B19 (B19V) to virus-like particles (VLPs). In this study, we present the atomic resolution structure ...The lack of a permissive cell culture system has limited high-resolution structures of parvovirus B19 (B19V) to virus-like particles (VLPs). In this study, we present the atomic resolution structure (2.2 Å) of authentic B19V purified from a patient blood sample. There are significant differences compared to non-infectious VLPs. Most strikingly, two host protease inhibitors (PIs), inter-alpha-trypsin inhibitor heavy chain 4 (ITIH4) and serpinA3, were identified in complex with the capsids in all patient samples tested. The ITIH4 binds specifically to the icosahedral fivefold axis and serpinA3 occupies the twofold axis. The protein-coated virions remain infectious, and the capsid-associated PIs retain activity; however, upon virion interaction with target cells, the PIs dissociate from the capsid prior to viral entry. Our finding of an infectious virion shielded by bound host serum proteins suggests an evolutionarily favored phenomenon to evade immune surveillance and escape host protease activity.
History
DepositionMay 30, 2024-
Header (metadata) releaseOct 16, 2024-
Map releaseOct 16, 2024-
UpdateMay 21, 2025-
Current statusMay 21, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_45136.png

Downloads & links

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Map

FileDownload / File: emd_45136.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.08 Å/pix.
x 512 pix.
= 552.96 Å		1.08 Å/pix.
x 512 pix.
= 552.96 Å		1.08 Å/pix.
x 512 pix.
= 552.96 Å

Surface

Projections

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Slices (1/2)

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.08 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy EMDB: 0.3
Minimum - Maximum-0.9227395 - 1.8158062
Average (Standard dev.)0.002447608 (±0.07573635)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-256-256-256
Dimensions512512512
Spacing512512512
CellA=B=C: 552.96 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_45136_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: #2

Fileemd_45136_half_map_2.map
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Sample components

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Entire : Human parvovirus B19

EntireName: Human parvovirus B19
Components
  • Virus: Human parvovirus B19
    • Protein or peptide: Capsid protein 2

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Supramolecule #1: Human parvovirus B19

SupramoleculeName: Human parvovirus B19 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 10798 / Sci species name: Human parvovirus B19 / Virus type: VIRION / Virus isolate: SEROTYPE / Virus enveloped: No / Virus empty: No

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Macromolecule #1: Capsid protein 2

MacromoleculeName: Capsid protein 2 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human parvovirus B19
Molecular weightTheoretical: 60.916016 KDa
SequenceString: MTSVNSAEAS TGAGGGGSNP VKSMWSEGAT FSANSVTCTF SRQFLIPYDP EHHYKVFSPA ASSCHNASGK EAKVCTISPI MGYSTPWRY LDFNALNLFF SPLEFQHLIE NYGSIAPDAL TVTISEIAVK DVTDKTGGGV QVTDSTTGRL CMLVDHEYKY P YVLGQGQD ...String:
MTSVNSAEAS TGAGGGGSNP VKSMWSEGAT FSANSVTCTF SRQFLIPYDP EHHYKVFSPA ASSCHNASGK EAKVCTISPI MGYSTPWRY LDFNALNLFF SPLEFQHLIE NYGSIAPDAL TVTISEIAVK DVTDKTGGGV QVTDSTTGRL CMLVDHEYKY P YVLGQGQD TLAPELPIWV YFPPQYAYLT VGDVNTQGIS GDSKKLASEE SAFYVLEHSS FQLLGTGGTA TMSYKFPPVP PE NLEGCSQ HFYEMYNPLY GSRLGVPDTL GGDPKFRSLT HEDHAIQPQN FMPGPLVNSV STKEGDSSNT GAGKALTGLS TGT SQNTRI SLRPGPVSQP YHHWDTDKYV TGINAISHGQ TTYGNAEDKE YQQGVGRFPN EKEQLKQLQG LNMHTYFPNK GTQQ YTDQI ERPLMVGSVW NRRALHYESQ LWSKIPNLDD SFKTQFAALG GWGLHQPPPQ IFLKILPQSG PIGGIKSMGI TTLVQ YAVG IMTVTMTFKL GPRKATGRWN PQPGVYPPHA AGHLPYVLYD PTATDAKQHH RHGYEKPEEL WTAKSRVHPL

UniProtKB: Capsid protein 2

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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
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Detector mode: INTEGRATING / Average electron dose: 100.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 0.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 16458
Initial angle assignmentType: RANDOM ASSIGNMENT
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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