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- EMDB-9635: The structure of Enterovirus D68 A-particle triggered by an unkno... -

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Basic information

Entry
Database: EMDB / ID: EMD-9635
TitleThe structure of Enterovirus D68 A-particle triggered by an unknown stimulus
Map dataNone
Sample
  • Virus: Enterovirus D68
    • Other: VP1
    • Other: VP2
    • Other: VP3
Biological speciesEnterovirus D68
Methodsingle particle reconstruction / cryo EM / Resolution: 4.4 Å
AuthorsZheng QB / Zhu R / Xu LF / He MZ / Yan XD / Cheng T / Li SW
CitationJournal: Nat Microbiol / Year: 2019
Title: Atomic structures of enterovirus D68 in complex with two monoclonal antibodies define distinct mechanisms of viral neutralization.
Authors: Qingbing Zheng / Rui Zhu / Longfa Xu / Maozhou He / Xiaodong Yan / Dongxiao Liu / Zhichao Yin / Yangtao Wu / Yongchao Li / Lisheng Yang / Wangheng Hou / Shuxuan Li / Zizhen Li / Zhenqin Chen ...Authors: Qingbing Zheng / Rui Zhu / Longfa Xu / Maozhou He / Xiaodong Yan / Dongxiao Liu / Zhichao Yin / Yangtao Wu / Yongchao Li / Lisheng Yang / Wangheng Hou / Shuxuan Li / Zizhen Li / Zhenqin Chen / Zhihai Li / Hai Yu / Ying Gu / Jun Zhang / Timothy S Baker / Z Hong Zhou / Barney S Graham / Tong Cheng / Shaowei Li / Ningshao Xia /
Abstract: Enterovirus D68 (EV-D68) undergoes structural transformation between mature, cell-entry intermediate (A-particle) and empty forms throughout its life cycle. Structural information for the various ...Enterovirus D68 (EV-D68) undergoes structural transformation between mature, cell-entry intermediate (A-particle) and empty forms throughout its life cycle. Structural information for the various forms and antibody-bound capsids will facilitate the development of effective vaccines and therapeutics against EV-D68 infection, which causes childhood respiratory and paralytic diseases worldwide. Here, we report the structures of three EV-D68 capsid states representing the virus at major phases. We further describe two original monoclonal antibodies (15C5 and 11G1) with distinct structurally defined mechanisms for virus neutralization. 15C5 and 11G1 engage the capsid loci at icosahedral three-fold and five-fold axes, respectively. To block viral attachment, 15C5 binds three forms of capsids, and triggers mature virions to transform into A-particles, mimicking engagement by the functional receptor ICAM-5, whereas 11G1 exclusively recognizes the A-particle. Our data provide a structural and molecular explanation for the transition of picornavirus capsid conformations and demonstrate distinct mechanisms for antibody-mediated neutralization.
History
DepositionAug 27, 2018-
Header (metadata) releaseNov 7, 2018-
Map releaseNov 7, 2018-
UpdateDec 26, 2018-
Current statusDec 26, 2018Processing site: PDBj / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.048
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 0.048
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_9635.png

Downloads & links

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Map

FileDownload / File: emd_9635.map.gz / Format: CCP4 / Size: 347.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationNone
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.13 Å/pix.
x 450 pix.
= 507.6 Å		1.13 Å/pix.
x 450 pix.
= 507.6 Å		1.13 Å/pix.
x 450 pix.
= 507.6 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.128 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.048 / Movie #1: 0.048
Minimum - Maximum-0.10020681 - 0.13266715
Average (Standard dev.)0.001057365 (±0.01054751)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions450450450
Spacing450450450
CellA=B=C: 507.6 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.1281.1281.128
M x/y/z450450450
origin x/y/z0.0000.0000.000
length x/y/z507.600507.600507.600
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS450450450
D min/max/mean-0.1000.1330.001

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Supplemental data

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Sample components

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Entire : Enterovirus D68

EntireName: Enterovirus D68
Components
  • Virus: Enterovirus D68
    • Other: VP1
    • Other: VP2
    • Other: VP3

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Supramolecule #1: Enterovirus D68

SupramoleculeName: Enterovirus D68 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 42789 / Sci species name: Enterovirus D68 / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: No

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Macromolecule #1: VP1

MacromoleculeName: VP1 / type: other / ID: 1 / Classification: other
Source (natural)Organism: Enterovirus D68
SequenceString: IESIIKTATD TVKSEINAEL GVVPSLNAVE TGATSNTEPE EAIQTRTVIN QHGVSETLVE NFLSRAALVS KRSFEYKDHT SSAAQADKNF FKWTINTRSF VQLRRKLELF TYLRFDAEIT ILTTVAVNGS GNNTYVGLPD LTLQAMFVPT GALTPEKQDS FHWQSGSNAS ...String:
IESIIKTATD TVKSEINAEL GVVPSLNAVE TGATSNTEPE EAIQTRTVIN QHGVSETLVE NFLSRAALVS KRSFEYKDHT SSAAQADKNF FKWTINTRSF VQLRRKLELF TYLRFDAEIT ILTTVAVNGS GNNTYVGLPD LTLQAMFVPT GALTPEKQDS FHWQSGSNAS VFFKISDPPA RITIPFMCIN SAYSVFYDGF AGFEKNGLYG INPADTIGNL CVRIVNEHQP VGFTVTVRVY MKPKHIKAWA PRPPRTLPYM SIANANYKGK ERAPNALNAI IGNRDSVKTM PHNIV

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Macromolecule #2: VP2

MacromoleculeName: VP2 / type: other / ID: 2 / Classification: other
Source (natural)Organism: Enterovirus D68
SequenceString: SPSAEACGYS DRVLQLKLGN SAIVTQEAAN YCCAYGEWPN YLPDHEAVAI DKPTQPETAT DRFYTLKSVK WETGSTGWWW KLPDALNNIG MFGQNVQHHY LYRSGFLIHV QCNATKFHQG ALLVVAIPEH QRGAHNTNTS PGFDDIMKGE EGGTFNHPYV LDDGTSLACA ...String:
SPSAEACGYS DRVLQLKLGN SAIVTQEAAN YCCAYGEWPN YLPDHEAVAI DKPTQPETAT DRFYTLKSVK WETGSTGWWW KLPDALNNIG MFGQNVQHHY LYRSGFLIHV QCNATKFHQG ALLVVAIPEH QRGAHNTNTS PGFDDIMKGE EGGTFNHPYV LDDGTSLACA TIFPHQWINL RTNNSATIVL PWMNAAPMDF PLRHNQWTLA IIPVVPLGTR TTSSMVPITV SIAPMCCEFN GLRHAITQ

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Macromolecule #3: VP3

MacromoleculeName: VP3 / type: other / ID: 3 / Classification: other
Source (natural)Organism: Enterovirus D68
SequenceString: GVPTYLLPGS GQFLTTDDHS SAPALPCFNP TPEMHIPGQV RNMLEVVQVE SMMEINNTES AVGMERLKVD ISALTDVDQL LFNIPLDIQL DGPLRNTLVG NISRYYTHWS GSLEMTFMFC GSFMATGKLI LCYTPPGGSC PTTRETAMLG THIVWDFGLQ SSVTLIIPWI ...String:
GVPTYLLPGS GQFLTTDDHS SAPALPCFNP TPEMHIPGQV RNMLEVVQVE SMMEINNTES AVGMERLKVD ISALTDVDQL LFNIPLDIQL DGPLRNTLVG NISRYYTHWS GSLEMTFMFC GSFMATGKLI LCYTPPGGSC PTTRETAMLG THIVWDFGLQ SSVTLIIPWI SGSHYRMFNN DAKSTNANVG YVTCFMQTNL IVPSESSDTC SLIGFIAAKD DFSLRLMRDS PDIGQLDHLH AAEAAYQ

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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: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TECNAI F30
Image recordingFilm or detector model: FEI FALCON II (4k x 4k) / Average electron dose: 25.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Tecnai F30 / Image courtesy: FEI Company

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Image processing

Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.4 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 2.0) / Number images used: 2491
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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