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- EMDB-11813: Structure of the SARS-CoV spike glycoprotein in complex with the ... -

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Basic information

Entry
Database: EMDB / ID: EMD-11813
TitleStructure of the SARS-CoV spike glycoprotein in complex with the 47D11 neutralizing antibody Fab fragment
Map dataComplex of the SARS-CoV spike glycoprotein with the neutralizing antibody Fab fragment 47D11
Sample
  • Complex: Complex of the SARS-CoV-2 spike glycoprotein with the 47D11 neutralizing antibody Fab fragment
    • Protein or peptide: Spike glycoprotein
    • Protein or peptide: 47D11 neutralizing antibody heavy chain
    • Protein or peptide: 47D11 neutralizing antibody light chain
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
Function / homology
Function and homology information


: / endocytosis involved in viral entry into host cell / host cell endoplasmic reticulum-Golgi intermediate compartment membrane / membrane => GO:0016020 / receptor-mediated virion attachment to host cell / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / host cell plasma membrane / virion membrane
Similarity search - Function
: / Spike (S) protein S1 subunit, receptor-binding domain, SARS-CoV / Spike (S) protein S1 subunit, N-terminal domain, SARS-CoV-like / Spike glycoprotein, betacoronavirus / Spike (S) protein S1 subunit, receptor-binding domain, betacoronavirus / Spike S1 subunit, receptor binding domain superfamily, betacoronavirus / Betacoronavirus spike glycoprotein S1, receptor binding / Spike glycoprotein S1, N-terminal domain, betacoronavirus-like / Betacoronavirus-like spike glycoprotein S1, N-terminal / Spike glycoprotein S2 superfamily, coronavirus ...: / Spike (S) protein S1 subunit, receptor-binding domain, SARS-CoV / Spike (S) protein S1 subunit, N-terminal domain, SARS-CoV-like / Spike glycoprotein, betacoronavirus / Spike (S) protein S1 subunit, receptor-binding domain, betacoronavirus / Spike S1 subunit, receptor binding domain superfamily, betacoronavirus / Betacoronavirus spike glycoprotein S1, receptor binding / Spike glycoprotein S1, N-terminal domain, betacoronavirus-like / Betacoronavirus-like spike glycoprotein S1, N-terminal / Spike glycoprotein S2 superfamily, coronavirus / Spike glycoprotein S2, coronavirus / Coronavirus spike glycoprotein S2 / Coronavirus spike glycoprotein S1, C-terminal / Coronavirus spike glycoprotein S1, C-terminal
Similarity search - Domain/homology
Biological speciesSevere acute respiratory syndrome coronavirus 2 / SARS coronavirus WH20 / Homo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.8 Å
AuthorsFedry J / Hurdiss DL / Wang C / Li W / Obal G / Drulyte I / Howes SC / van Kuppeveld FJM / Foerster F / Bosch BJ
Funding support Netherlands, 5 items
OrganizationGrant numberCountry
European Research Council (ERC)724425-BENDER Netherlands
H2020 Marie Curie Actions of the European Commission792575 Netherlands
H2020 Marie Curie Actions of the European Commission842333 Netherlands
European Molecular Biology Organization (EMBO)ALTF-948-2017 Netherlands
European Molecular Biology Organization (EMBO)ALTF-1172-2018 Netherlands
CitationJournal: Sci Adv / Year: 2021
Title: Structural insights into the cross-neutralization of SARS-CoV and SARS-CoV-2 by the human monoclonal antibody 47D11.
Authors: Juliette Fedry / Daniel L Hurdiss / Chunyan Wang / Wentao Li / Gonzalo Obal / Ieva Drulyte / Wenjuan Du / Stuart C Howes / Frank J M van Kuppeveld / Friedrich Förster / Berend-Jan Bosch /
Abstract: The emergence of SARS-CoV-2 antibody escape mutations highlights the urgent need for broadly neutralizing therapeutics. We previously identified a human monoclonal antibody, 47D11, capable of cross- ...The emergence of SARS-CoV-2 antibody escape mutations highlights the urgent need for broadly neutralizing therapeutics. We previously identified a human monoclonal antibody, 47D11, capable of cross-neutralizing SARS-CoV-2 and SARS-CoV and protecting against the associated respiratory disease in an animal model. Here, we report cryo-EM structures of both trimeric spike ectodomains in complex with the 47D11 Fab. 47D11 binds to the closed receptor-binding domain, distal to the ACE2 binding site. The CDRL3 stabilizes the N343 glycan in an upright conformation, exposing a mutationally constrained hydrophobic pocket, into which the CDRH3 loop inserts two aromatic residues. 47D11 stabilizes a partially open conformation of the SARS-CoV-2 spike, suggesting that it could be used effectively in combination with other antibodies targeting the exposed receptor-binding motif. Together, these results reveal a cross-protective epitope on the SARS-CoV-2 spike and provide a structural roadmap for the development of 47D11 as a prophylactic or postexposure therapy for COVID-19.
History
DepositionOct 1, 2020-
Header (metadata) releaseMay 19, 2021-
Map releaseMay 19, 2021-
UpdateJun 16, 2021-
Current statusJun 16, 2021Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.016
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.016
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7akj
  • Surface level: 0.016
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_11813.png

Downloads & links

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Map

FileDownload / File: emd_11813.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationComplex of the SARS-CoV spike glycoprotein with the neutralizing antibody Fab fragment 47D11
Voxel sizeX=Y=Z: 1.08 Å
Density
Contour LevelBy AUTHOR: 0.016 / Movie #1: 0.016
Minimum - Maximum-0.0485225 - 0.10908173
Average (Standard dev.)0.00012872726 (±0.0020619028)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 432.00003 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.081.081.08
M x/y/z400400400
origin x/y/z0.0000.0000.000
length x/y/z432.000432.000432.000
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS400400400
D min/max/mean-0.0490.1090.000

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Supplemental data

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Sample components

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Entire : Complex of the SARS-CoV-2 spike glycoprotein with the 47D11 neutr...

EntireName: Complex of the SARS-CoV-2 spike glycoprotein with the 47D11 neutralizing antibody Fab fragment
Components
  • Complex: Complex of the SARS-CoV-2 spike glycoprotein with the 47D11 neutralizing antibody Fab fragment
    • Protein or peptide: Spike glycoprotein
    • Protein or peptide: 47D11 neutralizing antibody heavy chain
    • Protein or peptide: 47D11 neutralizing antibody light chain
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose

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Supramolecule #1: Complex of the SARS-CoV-2 spike glycoprotein with the 47D11 neutr...

SupramoleculeName: Complex of the SARS-CoV-2 spike glycoprotein with the 47D11 neutralizing antibody Fab fragment
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3
Source (natural)Organism: Severe acute respiratory syndrome coronavirus 2
Molecular weightExperimental: 600 KDa

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Macromolecule #1: Spike glycoprotein

MacromoleculeName: Spike glycoprotein / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: SARS coronavirus WH20
Molecular weightTheoretical: 132.302688 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: RCTTFDDVQA PNYTQHTSSM RGVYYPDEIF RSDTLYLTQD LFLPFYSNVT GFHTINHTFD NPVIPFKDGI YFAATEKSNV VRGWVFGST MNNKSQSVII INNSTNVVIR ACNFELCDNP FFAVSKPMGT QTHTMIFDNA FNCTFEYISD AFSLDVSEKS G NFKHLREF ...String:
RCTTFDDVQA PNYTQHTSSM RGVYYPDEIF RSDTLYLTQD LFLPFYSNVT GFHTINHTFD NPVIPFKDGI YFAATEKSNV VRGWVFGST MNNKSQSVII INNSTNVVIR ACNFELCDNP FFAVSKPMGT QTHTMIFDNA FNCTFEYISD AFSLDVSEKS G NFKHLREF VFKNKDGFLY VYKGYQPIDV VRDLPSGFNT LKPIFKLPLG INITNFRAIL TAFSPAQDTW GTSAAAYFVG YL KPTTFML KYDENGTITD AVDCSQNPLA ELKCSVKSFE IDKGIYQTSN FRVVPSGDVV RFPNITNLCP FGEVFNATKF PSV YAWERK KISNCVADYS VLYNSTFFST FKCYGVSATK LNDLCFSNVY ADSFVVKGDD VRQIAPGQTG VIADYNYKLP DDFM GCVLA WNTRNIDATS TGNYNYKYRY LRHGKLRPFE RDISNVPFSP DGKPCTPPAL NCYWPLNDYG FYTTTGIGYQ PYRVV VLSF ELLNAPATVC GPKLSTDLIK NQCVNFNFNG LTGTGVLTPS SKRFQPFQQF GRDVSDFTDS VRDPKTSEIL DISPCS FGG VSVITPGTNA SSEVAVLYQD VNCTDVSTAI HADQLTPAWR IYSTGNNVFQ TQAGCLIGAE HVDTSYECDI PIGAGIC AS YHTVSLLRST SQKSIVAYTM SLGADSSIAY SNNTIAIPTN FSISITTEVM PVSMAKTSVD CNMYICGDST ECANLLLQ Y GSFCTQLNRA LSGIAAEQDR NTREVFAQVK QMYKTPTLKY FGGFNFSQIL PDPLKPTKRS FIEDLLFNKV TLADAGFMK QYGECLGDIN ARDLICAQKF NGLTVLPPLL TDDMIAAYTA ALVSGTATAG WTFGAGAALQ IPFAMQMAYR FNGIGVTQNV LYENQKQIA NQFNKAISQI QESLTTTSTA LGKLQDVVNQ NAQALNTLVK QLSSNFGAIS SVLNDILSRL DPPEAEVQID R LITGRLQS LQTYVTQQLI RAAEIRASAN LAATKMSECV LGQSKRVDFC GKGYHLMSFP QAAPHGVVFL HVTYVPSQER NF TTAPAIC HEGKAYFPRE GVFVFNGTSW FITQRNFFSP QIITTDNTFV SGNCDVVIGI INNTVYDPLQ PELDSFKEEL DKY FKNHTS PDVDLGDISG INASVVNLIK GSGYIPEAPR DGQAYVRKDG EWVLLSTFLI KLVPRGSLEW SHPQFEK

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Macromolecule #2: 47D11 neutralizing antibody heavy chain

MacromoleculeName: 47D11 neutralizing antibody heavy chain / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.205812 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
QVQLQESGPG LVKPSETLSL TCSVSGGSIS SHYWSWIRQP PGKGLEWIGY IYYSGSTNHN PSLKSRVTIS VDTSKNQFSL KLSSVTAAD TAVYYCARGV LLWFGEPIFE IWGQGTMVTV SS

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Macromolecule #3: 47D11 neutralizing antibody light chain

MacromoleculeName: 47D11 neutralizing antibody light chain / type: protein_or_peptide / ID: 3 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 11.350607 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
EIVMTQSPAT LSVSPGERAT LSCRASQSVS SSLAWYQQKP GQAPRLLIYG ASTRAPGIPA RFSGSGSGTE FTLTISSLQS EDFAVYYCQ QYNNWPLTFG GGTKVEI

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Macromolecule #7: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 7 / Number of copies: 36 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

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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

Concentration1.6 mg/mL
BufferpH: 8
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TALOS ARCTICA
Specialist opticsEnergy filter - Name: GIF Quantum LS / Energy filter - Slit width: 20 eV
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Number real images: 4231 / Average electron dose: 40.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 30.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.5 µm / Nominal magnification: 130000
Sample stageSpecimen holder model: OTHER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Talos Arctica / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 1500537
CTF correctionSoftware - Name: CTFFIND
Startup modelType of model: EMDB MAP
EMDB ID:

21457

Final reconstructionApplied symmetry - Point group: C3 (3 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 260941
Initial angle assignmentType: RANDOM ASSIGNMENT / Software - Name: RELION
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION
FSC plot (resolution estimation)

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