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- EMDB-32449: SARS-CoV-2 Omicron variant spike RBD in complex with Fab XGv289 -

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Basic information

Entry
Database: EMDB / ID: EMD-32449
TitleSARS-CoV-2 Omicron variant spike RBD in complex with Fab XGv289
Map data
Sample
  • Complex: SARS-CoV-2 Omicron mutation spike protein in complex with Fab 265
    • Complex: Fab 289
      • Protein or peptide: The heavy chain of Fab XGv289
      • Protein or peptide: The light chain of Fab XGv289
    • Complex: SARS-CoV-2 Omicron mutation spike protein
      • Protein or peptide: Spike protein S1
Function / homology
Function and homology information


Maturation of spike protein / viral translation / Translation of Structural Proteins / Virion Assembly and Release / host cell surface / host extracellular space / suppression by virus of host tetherin activity / Induction of Cell-Cell Fusion / structural constituent of virion / entry receptor-mediated virion attachment to host cell ...Maturation of spike protein / viral translation / Translation of Structural Proteins / Virion Assembly and Release / host cell surface / host extracellular space / suppression by virus of host tetherin activity / Induction of Cell-Cell Fusion / structural constituent of virion / entry receptor-mediated virion attachment to host cell / host cell endoplasmic reticulum-Golgi intermediate compartment membrane / receptor-mediated endocytosis of virus by host cell / Attachment and Entry / membrane fusion / positive regulation of viral entry into host cell / receptor-mediated virion attachment to host cell / receptor ligand activity / host cell surface receptor binding / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / SARS-CoV-2 activates/modulates innate and adaptive immune responses / host cell plasma membrane / virion membrane / membrane / identical protein binding / plasma membrane
Similarity search - Function
Spike (S) protein S1 subunit, receptor-binding domain, SARS-CoV-2 / Spike (S) protein S1 subunit, N-terminal domain, SARS-CoV-like / Betacoronavirus spike (S) glycoprotein S1 subunit N-terminal (NTD) domain profile. / Spike glycoprotein, N-terminal domain superfamily / Betacoronavirus spike (S) glycoprotein S1 subunit C-terminal (CTD) domain profile. / 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 ...Spike (S) protein S1 subunit, receptor-binding domain, SARS-CoV-2 / Spike (S) protein S1 subunit, N-terminal domain, SARS-CoV-like / Betacoronavirus spike (S) glycoprotein S1 subunit N-terminal (NTD) domain profile. / Spike glycoprotein, N-terminal domain superfamily / Betacoronavirus spike (S) glycoprotein S1 subunit C-terminal (CTD) domain profile. / 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, coronavirus, heptad repeat 1 / Spike glycoprotein S2, coronavirus, heptad repeat 2 / Coronavirus spike (S) glycoprotein S2 subunit heptad repeat 2 (HR2) region profile. / Coronavirus spike (S) glycoprotein S2 subunit heptad repeat 1 (HR1) region profile. / 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 speciesHomo sapiens (human) / Severe acute respiratory syndrome coronavirus 2
Methodsingle particle reconstruction / cryo EM / Resolution: 3.8 Å
AuthorsWang X / Wang L
Funding support1 items
OrganizationGrant numberCountry
Not funded
CitationJournal: Nature / Year: 2022
Title: Memory B cell repertoire from triple vaccinees against diverse SARS-CoV-2 variants.
Authors: Kang Wang / Zijing Jia / Linilin Bao / Lei Wang / Lei Cao / Hang Chi / Yaling Hu / Qianqian Li / Yunjiao Zhou / Yinan Jiang / Qianhui Zhu / Yongqiang Deng / Pan Liu / Nan Wang / Lin Wang / ...Authors: Kang Wang / Zijing Jia / Linilin Bao / Lei Wang / Lei Cao / Hang Chi / Yaling Hu / Qianqian Li / Yunjiao Zhou / Yinan Jiang / Qianhui Zhu / Yongqiang Deng / Pan Liu / Nan Wang / Lin Wang / Min Liu / Yurong Li / Boling Zhu / Kaiyue Fan / Wangjun Fu / Peng Yang / Xinran Pei / Zhen Cui / Lili Qin / Pingju Ge / Jiajing Wu / Shuo Liu / Yiding Chen / Weijin Huang / Qiao Wang / Cheng-Feng Qin / Youchun Wang / Chuan Qin / Xiangxi Wang /
Abstract: Omicron (B.1.1.529), the most heavily mutated SARS-CoV-2 variant so far, is highly resistant to neutralizing antibodies, raising concerns about the effectiveness of antibody therapies and vaccines. ...Omicron (B.1.1.529), the most heavily mutated SARS-CoV-2 variant so far, is highly resistant to neutralizing antibodies, raising concerns about the effectiveness of antibody therapies and vaccines. Here we examined whether sera from individuals who received two or three doses of inactivated SARS-CoV-2 vaccine could neutralize authentic Omicron. The seroconversion rates of neutralizing antibodies were 3.3% (2 out of 60) and 95% (57 out of 60) for individuals who had received 2 and 3 doses of vaccine, respectively. For recipients of three vaccine doses, the geometric mean neutralization antibody titre for Omicron was 16.5-fold lower than for the ancestral virus (254). We isolated 323 human monoclonal antibodies derived from memory B cells in triple vaccinees, half of which recognized the receptor-binding domain, and showed that a subset (24 out of 163) potently neutralized all SARS-CoV-2 variants of concern, including Omicron. Therapeutic treatments with representative broadly neutralizing monoclonal antibodies were highly protective against infection of mice with SARS-CoV-2 Beta (B.1.351) and Omicron. Atomic structures of the Omicron spike protein in complex with three classes of antibodies that were active against all five variants of concern defined the binding and neutralizing determinants and revealed a key antibody escape site, G446S, that confers greater resistance to a class of antibodies that bind on the right shoulder of the receptor-binding domain by altering local conformation at the binding interface. Our results rationalize the use of three-dose immunization regimens and suggest that the fundamental epitopes revealed by these broadly ultrapotent antibodies are rational targets for a universal sarbecovirus vaccine.
History
DepositionDec 23, 2021-
Header (metadata) releaseMay 4, 2022-
Map releaseMay 4, 2022-
UpdateMay 4, 2022-
Current statusMay 4, 2022Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_32449.png

Downloads & links

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Map

FileDownload / File: emd_32449.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.07 Å
Density
Contour LevelBy AUTHOR: 0.0354
Minimum - Maximum-0.11642579 - 0.179945
Average (Standard dev.)0.00020877502 (±0.0023082476)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions360360360
Spacing360360360
CellA=B=C: 385.2 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : SARS-CoV-2 Omicron mutation spike protein in complex with Fab 265

EntireName: SARS-CoV-2 Omicron mutation spike protein in complex with Fab 265
Components
  • Complex: SARS-CoV-2 Omicron mutation spike protein in complex with Fab 265
    • Complex: Fab 289
      • Protein or peptide: The heavy chain of Fab XGv289
      • Protein or peptide: The light chain of Fab XGv289
    • Complex: SARS-CoV-2 Omicron mutation spike protein
      • Protein or peptide: Spike protein S1

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Supramolecule #1: SARS-CoV-2 Omicron mutation spike protein in complex with Fab 265

SupramoleculeName: SARS-CoV-2 Omicron mutation spike protein in complex with Fab 265
type: complex / Chimera: Yes / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #2: Fab 289

SupramoleculeName: Fab 289 / type: complex / Chimera: Yes / ID: 2 / Parent: 1 / Macromolecule list: #1, #3
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Homo sapiens (human)

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Supramolecule #3: SARS-CoV-2 Omicron mutation spike protein

SupramoleculeName: SARS-CoV-2 Omicron mutation spike protein / type: complex / Chimera: Yes / ID: 3 / Parent: 1 / Macromolecule list: #2

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Macromolecule #1: The heavy chain of Fab XGv289

MacromoleculeName: The heavy chain of Fab XGv289 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.098562 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
QVQLVQSGAE VKKPGASLKV SCRASGYTFT SHFIHWVRQA PGQGLEWMGI INPSGGASYA QNFRDRVTMT TDPSTSTVYM ELGSLRSED TAVYYCARAE GSSWLGWFDP WGQGTLVTVS S

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Macromolecule #2: Spike protein S1

MacromoleculeName: Spike protein S1 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Severe acute respiratory syndrome coronavirus 2
Molecular weightTheoretical: 22.806828 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: PNITNLCPFD EVFNATRFAS VYAWNRKRIS NCVADYSVLY NLAPFFTFKC YGVSPTKLND LCFTNVYADS FVIRGDEVRQ IAPGQTGKI ADYNYKLPDD FTGCVIAWNS NNLDSKVGGN YNYLYRLFRK SNLKPFERDI STEIYQAGNK PCNGVAGFNC Y FPLRSYSF ...String:
PNITNLCPFD EVFNATRFAS VYAWNRKRIS NCVADYSVLY NLAPFFTFKC YGVSPTKLND LCFTNVYADS FVIRGDEVRQ IAPGQTGKI ADYNYKLPDD FTGCVIAWNS NNLDSKVGGN YNYLYRLFRK SNLKPFERDI STEIYQAGNK PCNGVAGFNC Y FPLRSYSF RPTYGVGHQP YRVVVLSFEL LHAPATVCGP KKS

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Macromolecule #3: The light chain of Fab XGv289

MacromoleculeName: The light chain of Fab XGv289 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 11.586687 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
SVLTQPPSAS GTPGQRVTIP CSGSSSNIGN NYVYWYQQLP GTAPKLLVYG NNQRPSGVPD RFSVSKSGTS ASLAISGLRS EDEADYYCA AWDDGLSGSG WVFGGGTKLT VL

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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: 8.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: DARK FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.5 µm
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2

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Image processing

Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 401170

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