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- EMDB-6168: Structure of Enteric Pathogen Bovine Parvovirus -

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Basic information

Entry
Database: EMDB / ID: EMD-6168
TitleStructure of Enteric Pathogen Bovine Parvovirus
Map dataReconstruction of Bovine Parvovirus VP2 capsid
Sample
  • Sample: Bovine Parvovirus VP2 Virus-like particle
  • Virus: Bovine parvovirus-1
KeywordsBPV / parvovirus / bocavirus capsid / vp2
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 VP2 / VP2
Function and homology information
Biological speciesBovine parvovirus-1
Methodsingle particle reconstruction / cryo EM / Resolution: 8.8 Å
AuthorsKailasan S / Halder S / Gurda B / Bladek H / Chipman PR / McKenna R / Brown K / Agbandje-McKenna M
CitationJournal: J Virol / Year: 2015
Title: Structure of an enteric pathogen, bovine parvovirus.
Authors: Shweta Kailasan / Sujata Halder / Brittney Gurda / Heather Bladek / Paul R Chipman / Robert McKenna / Kevin Brown / Mavis Agbandje-McKenna /
Abstract: Bovine parvovirus (BPV), the causative agent of respiratory and gastrointestinal disease in cows, is the type member of the Bocaparvovirus genus of the Parvoviridae family. Toward efforts to obtain a ...Bovine parvovirus (BPV), the causative agent of respiratory and gastrointestinal disease in cows, is the type member of the Bocaparvovirus genus of the Parvoviridae family. Toward efforts to obtain a template for the development of vaccines and small-molecule inhibitors for this pathogen, the structure of the BPV capsid, assembled from the major capsid viral protein 2 (VP2), was determined using X-ray crystallography as well as cryo-electron microscopy and three-dimensional image reconstruction (cryo-reconstruction) to 3.2- and 8.8-Å resolutions, respectively. The VP2 region ordered in the crystal structure, from residues 39 to 536, conserves the parvoviral eight-stranded jellyroll motif and an αA helix. The BPV capsid displays common parvovirus features: a channel at and depressions surrounding the 5-fold axes and protrusions surrounding the 3-fold axes. However, rather than a depression centered at the 2-fold axes, a raised surface loop divides this feature in BPV. Additional observed density in the capsid interior in the cryo-reconstructed map, compared to the crystal structure, is interpreted as 10 additional N-terminal residues, residues 29 to 38, that radially extend the channel under the 5-fold axis, as observed for human bocavirus 1 (HBoV1). Surface loops of various lengths and conformations extend from the core jellyroll motif of VP2. These loops confer the unique surface topology of the BPV capsid, making it strikingly different from HBoV1 as well as the type members of other Parvovirinae genera for which structures have been determined. For the type members, regions structurally analogous to those decorating the BPV capsid surface serve as determinants of receptor recognition, tissue and host tropism, pathogenicity, and antigenicity.
IMPORTANCE: Bovine parvovirus (BPV), identified in the 1960s in diarrheic calves, is the type member of the Bocaparvovirus genus of the nonenveloped, single-stranded DNA (ssDNA) Parvoviridae family. ...IMPORTANCE: Bovine parvovirus (BPV), identified in the 1960s in diarrheic calves, is the type member of the Bocaparvovirus genus of the nonenveloped, single-stranded DNA (ssDNA) Parvoviridae family. The recent isolation of human bocaparvoviruses from children with severe respiratory and gastrointestinal infections has generated interest in understanding the life cycle and pathogenesis of these emerging viruses. We have determined the high-resolution structure of the BPV capsid assembled from its predominant capsid protein VP2, known to be involved in a myriad of functions during host cell entry, pathogenesis, and antigenicity for other members of the Parvovirinae. Our results show the conservation of the core secondary structural elements and the location of the N-terminal residues for the known bocaparvovirus capsid structures. However, surface loops with high variability in sequence and conformation give BPV a unique capsid surface topology. Similar analogous regions in other Parvovirinae type members are important as determinants of receptor recognition, tissue and host tropism, pathogenicity, and antigenicity.
History
DepositionOct 28, 2014-
Header (metadata) releaseNov 5, 2014-
Map releaseDec 31, 2014-
UpdateMay 27, 2015-
Current statusMay 27, 2015Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 1
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 1
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

Downloads & links

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Map

FileDownload / File: emd_6168.map.gz / Format: CCP4 / Size: 11.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationReconstruction of Bovine Parvovirus VP2 capsid
Voxel sizeX=Y=Z: 2.24 Å
Density
Contour LevelBy EMDB: 1.0 / Movie #1: 1
Minimum - Maximum-3.99295068 - 5.05734348
Average (Standard dev.)0.0 (±1.0)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderYXZ
Origin-72-72-72
Dimensions145145145
Spacing145145145
CellA=B=C: 324.8 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z2.242.242.24
M x/y/z145145145
origin x/y/z0.0000.0000.000
length x/y/z324.800324.800324.800
α/β/γ90.00090.00090.000
start NX/NY/NZ-72-72-72
NX/NY/NZ145145145
MAP C/R/S213
start NC/NR/NS-72-72-72
NC/NR/NS145145145
D min/max/mean-3.9935.0570.000

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Supplemental data

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Sample components

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Entire : Bovine Parvovirus VP2 Virus-like particle

EntireName: Bovine Parvovirus VP2 Virus-like particle
Components
  • Sample: Bovine Parvovirus VP2 Virus-like particle
  • Virus: Bovine parvovirus-1

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Supramolecule #1000: Bovine Parvovirus VP2 Virus-like particle

SupramoleculeName: Bovine Parvovirus VP2 Virus-like particle / type: sample / ID: 1000 / Oligomeric state: 60mer / Number unique components: 1
Molecular weightExperimental: 3.6 MDa / Theoretical: 3.6 MDa / Method: SDS PAGE, Mass Spectrometry

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Supramolecule #1: Bovine parvovirus-1

SupramoleculeName: Bovine parvovirus-1 / type: virus / ID: 1 / NCBI-ID: 365609 / Sci species name: Bovine parvovirus-1 / Sci species strain: Haden / Virus type: VIRUS-LIKE PARTICLE / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: Yes
Host (natural)Organism: Bos taurus (cattle) / synonym: VERTEBRATES
Host systemOrganism: Spodoptera frugiperda (fall armyworm) / Recombinant cell: Sf9 / Recombinant plasmid: pFastbac-1
Molecular weightExperimental: 3.6 MDa / Theoretical: 3.6 MDa
Virus shellShell ID: 1 / Name: VP2 / Diameter: 275 Å / T number (triangulation number): 1

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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

Concentration8.0 mg/mL
BufferpH: 7.4 / Details: Tris-HCl
VitrificationCryogen name: ETHANE / Chamber humidity: 90 % / Chamber temperature: 120 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TECNAI F20
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsCalibrated magnification: 67047 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.0 mm / Nominal defocus max: 3.98 µm / Nominal defocus min: 1.26 µm / Nominal magnification: 67047
Sample stageSpecimen holder: 626 / Specimen holder model: GATAN LIQUID NITROGEN
Alignment procedureLegacy - Astigmatism: Objective lens astigmatism was corrected at 92,000 times magnification.
DateFeb 5, 2013
Image recordingCategory: CCD / Film or detector model: GATAN ULTRASCAN 4000 (4k x 4k) / Digitization - Sampling interval: 15 µm / Number real images: 63 / Average electron dose: 20 e/Å2
Experimental equipment
Model: Tecnai F20 / Image courtesy: FEI Company

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Image processing

CTF correctionDetails: each particle
Final reconstructionAlgorithm: OTHER / Resolution.type: BY AUTHOR / Resolution: 8.8 Å / Resolution method: OTHER / Software - Name: Auto3DEM / Number images used: 1131
DetailsManual selection in Robem

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Atomic model buiding 1

Initial modelPDB ID:

Chain - Chain ID: A
SoftwareName: Chimera
RefinementSpace: REAL / Protocol: RIGID BODY FIT / Target criteria: correlation coefficient

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