|Entry||Database: EMDB / ID: EMD-8605|
|Title||Human bocavirus 4Bocaparvovirus|
|Sample||Human bocavirus 4:|
virus / Capsid protein VP2
|Function / homology|
Function and homology information
T=1 icosahedral viral capsid / phospholipase A2 / phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine) / phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine) / phospholipase A2 activity / lipid catabolic process / host cell cytoplasm / host cell nucleus / structural molecule activity
Parvovirus coat protein VP2 / Parvovirus coat protein VP1 / Parvovirus coat protein VP2 / Parvovirus coat protein VP1/VP2 / Capsid/spike protein, ssDNA virus / Parvovirus coat protein VP1, N-terminal
Minor capsid protein VP1 / Minor capsid protein VP1
|Biological species||Human bocavirus 4|
|Method||single particle reconstruction / cryo EM / Resolution: 3 Å|
|Authors||Mietzsch M / Agbandje-McKenna M|
|Citation||Journal: J. Virol. / Year: 2017|
Title: Structural Insights into Human Bocaparvoviruses.
Authors: Mario Mietzsch / Shweta Kailasan / Jamie Garrison / Maria Ilyas / Paul Chipman / Kalle Kantola / Mandy E Janssen / John Spear / Duncan Sousa / Robert McKenna / Kevin Brown / Maria Söderlund-Venermo / Timothy Baker / Mavis Agbandje-McKenna /
Abstract: Bocaparvoviruses are emerging pathogens of the family. Human bocavirus 1 (HBoV1) causes severe respiratory infections and HBoV2 to HBoV4 cause gastrointestinal infections in young children. Recent ...Bocaparvoviruses are emerging pathogens of the family. Human bocavirus 1 (HBoV1) causes severe respiratory infections and HBoV2 to HBoV4 cause gastrointestinal infections in young children. Recent reports of life-threatening cases, lack of direct treatment or vaccination, and a limited understanding of their disease mechanisms highlight the need to study these pathogens on a molecular and structural level for the development of therapeutics. Toward this end, the capsid structures of HBoV1, HBoV3, and HBoV4 were determined to a resolution of 2.8 to 3.0 Å by cryo-electron microscopy and three-dimensional image reconstruction. The bocaparvovirus capsids, which display different tissue tropisms, have features in common with other parvoviruses, such as depressions at the icosahedral 2-fold symmetry axis and surrounding the 5-fold symmetry axis, protrusions surrounding the 3-fold symmetry axis, and a channel at the 5-fold symmetry axis. However, unlike other parvoviruses, densities extending the 5-fold channel into the capsid interior are conserved among the bocaparvoviruses and are suggestive of a genus-specific function. Additionally, their major viral protein 3 contains loops with variable regions at their apexes conferring capsid surface topologies different from those of other parvoviruses. Structural comparisons at the strain (HBoV) and genus (bovine parvovirus and HBoV) levels identified differences in surface loops that are functionally important in host/tissue tropism, pathogenicity, and antigenicity in other parvoviruses and likely play similar roles in these viruses. This study thus provides a structural framework to characterize determinants of host/tissue tropism, pathogenicity, and antigenicity for the development of antiviral strategies to control human bocavirus infections. Human bocaviruses are one of only a few members of the family pathogenic to humans, especially young children and immunocompromised adults. There are currently no treatments or vaccines for these viruses or the related enteric bocaviruses. This study obtained the first high-resolution structures of three human bocaparvoviruses determined by cryo-reconstruction. HBoV1 infects the respiratory tract, and HBoV3 and HBoV4 infect the gastrointestinal tract, tissues that are likely targeted by the capsid. Comparison of these viruses provides information on conserved bocaparvovirus-specific features and variable regions resulting in unique surface topologies that can serve as guides to characterize HBoV determinants of tissue tropism and antigenicity in future experiments. Based on the comparison to other existing parvovirus capsid structures, this study suggests capsid regions that likely control successful infection, including determinants of receptor attachment, host cell trafficking, and antigenic reactivity. Overall, these observations could impact efforts to design antiviral strategies and vaccines for HBoVs.
|Validation Report||PDB-ID: 5us9|
SummaryFull reportAbout validation report
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_8605.map.gz / Format: CCP4 / Size: 242.3 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 0.95 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Entire Human bocavirus 4
|Entire||Name: Human bocavirus 4 / Number of components: 2|
-Component #1: virus, Human bocavirus 4
|Virus||Name: Human bocavirus 4Bocaparvovirus / Class: VIRUS-LIKE PARTICLE / Empty: Yes / Enveloped: No / Isolate: SEROTYPE|
|Species||Species: Human bocavirus 4|
|Source (engineered)||Expression System: Spodoptera frugiperda (fall armyworm)|
-Component #2: protein, Capsid protein VP2
|Protein||Name: Capsid protein VP2 / Number of Copies: 60 / Recombinant expression: No|
|Mass||Theoretical: 61.033809 kDa|
|Source||Species: Human bocavirus 4|
|Source (engineered)||Expression System: Spodoptera frugiperda (fall armyworm)|
|Specimen||Specimen state: Particle / Method: cryo EM|
|Sample solution||pH: 7.4|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 60 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Camera||Detector: DIRECT ELECTRON DE-20 (5k x 3k)|
|Processing||Method: single particle reconstruction / Number of projections: 13394|
|3D reconstruction||Resolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF|
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