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- PDB-8x0y: Crystal structure of JM-1A in complex with SARS-CoV-2 RBD -

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Basic information

Entry
Database: PDB / ID: 8x0y
TitleCrystal structure of JM-1A in complex with SARS-CoV-2 RBD
Components
  • Heavy chain of JM-1A Fab
  • Light chain of JM-1A Fab
  • Spike protein S1
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / Antibody / broad neutralization / class 1/2 / Omicron variants / vaccine / VIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM complex
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 / symbiont-mediated-mediated suppression 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 / symbiont-mediated-mediated suppression 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 / membrane fusion / Attachment and Entry / positive regulation of viral entry into host cell / receptor-mediated virion attachment to host cell / host cell surface receptor binding / symbiont-mediated suppression of host innate immune response / endocytosis involved in viral entry into host cell / receptor ligand activity / 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 / identical protein binding / membrane / 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 / Coronavirus spike glycoprotein S1, C-terminal / Coronavirus spike glycoprotein S1, C-terminal / Spike glycoprotein, betacoronavirus / Spike glycoprotein, N-terminal domain superfamily / Betacoronavirus spike (S) glycoprotein S1 subunit N-terminal (NTD) domain profile. / Betacoronavirus spike (S) glycoprotein S1 subunit C-terminal (CTD) domain profile. / Spike (S) protein S1 subunit, receptor-binding domain, betacoronavirus / Spike S1 subunit, receptor binding domain superfamily, betacoronavirus ...Spike (S) protein S1 subunit, receptor-binding domain, SARS-CoV-2 / Spike (S) protein S1 subunit, N-terminal domain, SARS-CoV-like / Coronavirus spike glycoprotein S1, C-terminal / Coronavirus spike glycoprotein S1, C-terminal / Spike glycoprotein, betacoronavirus / Spike glycoprotein, N-terminal domain superfamily / Betacoronavirus spike (S) glycoprotein S1 subunit N-terminal (NTD) domain profile. / Betacoronavirus spike (S) glycoprotein S1 subunit C-terminal (CTD) domain profile. / 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 1 (HR1) region profile. / Coronavirus spike (S) glycoprotein S2 subunit heptad repeat 2 (HR2) region profile. / Spike glycoprotein S2 superfamily, coronavirus / Spike glycoprotein S2, coronavirus / Coronavirus spike glycoprotein S2
Similarity search - Domain/homology
PHOSPHATE ION / Spike glycoprotein
Similarity search - Component
Biological speciesSevere acute respiratory syndrome coronavirus 2
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.94 Å
AuthorsMohapatra, A. / Chen, X.
Funding support Taiwan, 1items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, Taiwan) Taiwan
CitationJournal: PLoS Pathog / Year: 2024
Title: The presence of broadly neutralizing anti-SARS-CoV-2 RBD antibodies elicited by primary series and booster dose of COVID-19 vaccine.
Authors: Xiaorui Chen / Arpita Mohapatra / Hong Thuy Vy Nguyen / Lisa Schimanski / Tiong Kit Tan / Pramila Rijal / Cheng-Pin Chen / Shu-Hsing Cheng / Wen-Hsin Lee / Yu-Chi Chou / Alain R Townsend / ...Authors: Xiaorui Chen / Arpita Mohapatra / Hong Thuy Vy Nguyen / Lisa Schimanski / Tiong Kit Tan / Pramila Rijal / Cheng-Pin Chen / Shu-Hsing Cheng / Wen-Hsin Lee / Yu-Chi Chou / Alain R Townsend / Che Ma / Kuan-Ying A Huang /
Abstract: Antibody-mediated immunity plays a key role in protection against SARS-CoV-2. We characterized B-cell-derived anti-SARS-CoV-2 RBD antibody repertoires from vaccinated and infected individuals and ...Antibody-mediated immunity plays a key role in protection against SARS-CoV-2. We characterized B-cell-derived anti-SARS-CoV-2 RBD antibody repertoires from vaccinated and infected individuals and elucidate the mechanism of action of broadly neutralizing antibodies and dissect antibodies at the epitope level. The breadth and clonality of anti-RBD B cell response varies among individuals. The majority of neutralizing antibody clones lose or exhibit reduced activities against Beta, Delta, and Omicron variants. Nevertheless, a portion of anti-RBD antibody clones that develops after a primary series or booster dose of COVID-19 vaccination exhibit broad neutralization against emerging Omicron BA.2, BA.4, BA.5, BQ.1.1, XBB.1.5 and XBB.1.16 variants. These broadly neutralizing antibodies share genetic features including a conserved usage of the IGHV3-53 and 3-9 genes and recognize three clustered epitopes of the RBD, including epitopes that partially overlap the classically defined set identified early in the pandemic. The Fab-RBD crystal and Fab-Spike complex structures corroborate the epitope grouping of antibodies and reveal the detailed binding mode of broadly neutralizing antibodies. Structure-guided mutagenesis improves binding and neutralization potency of antibody with Omicron variants via a single amino-substitution. Together, these results provide an immunological basis for partial protection against severe COVID-19 by the ancestral strain-based vaccine and indicate guidance for next generation monoclonal antibody development and vaccine design.
History
DepositionNov 6, 2023Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jun 5, 2024Provider: repository / Type: Initial release
Revision 1.1Jun 26, 2024Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.pdbx_database_id_PubMed ..._citation.journal_volume / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.name
Revision 1.2Jul 3, 2024Group: Database references / Category: citation / citation_author
Item: _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID
Revision 1.3Oct 9, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
B: Spike protein S1
E: Heavy chain of JM-1A Fab
F: Light chain of JM-1A Fab
A: Spike protein S1
G: Heavy chain of JM-1A Fab
I: Light chain of JM-1A Fab
hetero molecules


Theoretical massNumber of molelcules
Total (without water)137,50010
Polymers136,2286
Non-polymers1,2724
Water18,7721042
1
B: Spike protein S1
E: Heavy chain of JM-1A Fab
F: Light chain of JM-1A Fab
hetero molecules


Theoretical massNumber of molelcules
Total (without water)68,8156
Polymers68,1143
Non-polymers7013
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6440 Å2
ΔGint-28 kcal/mol
Surface area26920 Å2
MethodPISA
2
A: Spike protein S1
G: Heavy chain of JM-1A Fab
I: Light chain of JM-1A Fab
hetero molecules


Theoretical massNumber of molelcules
Total (without water)68,6854
Polymers68,1143
Non-polymers5711
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6320 Å2
ΔGint-21 kcal/mol
Surface area26700 Å2
MethodPISA
Unit cell
Length a, b, c (Å)148.359, 107.030, 87.340
Angle α, β, γ (deg.)90.00, 100.75, 90.00
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11F-505-

HOH

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Components

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Antibody , 2 types, 4 molecules EGFI

#2: Antibody Heavy chain of JM-1A Fab


Mass: 23049.879 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): expiCHO / Production host: Cricetulus griseus (Chinese hamster)
#3: Antibody Light chain of JM-1A Fab


Mass: 23061.549 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): expiCHO / Production host: Cricetulus griseus (Chinese hamster)

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Protein / Sugars , 2 types, 4 molecules BA

#1: Protein Spike protein S1


Mass: 22002.676 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Severe acute respiratory syndrome coronavirus 2
Gene: S, 2 / Production host: Homo sapiens (human) / References: UniProt: P0DTC2
#4: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 570.542 Da / Num. of mol.: 2 / Source method: obtained synthetically
DescriptorTypeProgram
DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-1-2/a4-b1_a6-c1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}[(6+1)][a-L-Fucp]{}}LINUCSPDB-CARE

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Non-polymers , 3 types, 1044 molecules

#5: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#6: Chemical ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: PO4
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1042 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.51 Å3/Da / Density % sol: 50.99 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 4
Details: 1M lithium chloride, 0.1M citrate pH 4.0, 20% (w/v) polyethylene glycol 6000

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: NSRRC / Beamline: BL15A1 / Wavelength: 1 Å
DetectorType: RAYONIX MX300HE / Detector: CCD / Date: Apr 23, 2022
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.94→19.92 Å / Num. obs: 98913 / % possible obs: 99.86 % / Redundancy: 4.8 % / Biso Wilson estimate: 24 Å2 / CC1/2: 0.995 / CC star: 0.999 / Rmerge(I) obs: 0.071 / Rpim(I) all: 0.071 / Rrim(I) all: 0.101 / Χ2: 0.94 / Net I/σ(I): 5.8
Reflection shellResolution: 1.94→2.01 Å / Redundancy: 4.7 % / Rmerge(I) obs: 0.589 / Mean I/σ(I) obs: 1.34 / Num. unique obs: 9822 / CC1/2: 0.617 / CC star: 0.874 / Rpim(I) all: 0.589 / Rrim(I) all: 0.832 / Χ2: 0.84 / % possible all: 99.95

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Processing

Software
NameVersionClassification
PHENIX(1.19.2_4158: ???)refinement
iMOSFLMdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.94→19.92 Å / SU ML: 0.25 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 25.47 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2234 4955 5.01 %
Rwork0.1939 --
obs0.1954 98881 99.97 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.94→19.92 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9584 0 1 1042 10627
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0089824
X-RAY DIFFRACTIONf_angle_d1.03213381
X-RAY DIFFRACTIONf_dihedral_angle_d14.2963488
X-RAY DIFFRACTIONf_chiral_restr0.061508
X-RAY DIFFRACTIONf_plane_restr0.0081709
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.94-1.960.37251360.3153089X-RAY DIFFRACTION100
1.96-1.990.37191800.30013166X-RAY DIFFRACTION100
1.99-2.010.33241770.29753074X-RAY DIFFRACTION100
2.01-2.030.30631510.28683129X-RAY DIFFRACTION100
2.03-2.060.33531880.27093077X-RAY DIFFRACTION100
2.06-2.090.31321740.26873134X-RAY DIFFRACTION100
2.09-2.120.28681770.2533117X-RAY DIFFRACTION100
2.12-2.150.26711580.23993089X-RAY DIFFRACTION100
2.15-2.180.27771660.23893165X-RAY DIFFRACTION100
2.18-2.220.27251440.23253124X-RAY DIFFRACTION100
2.22-2.260.26921770.23063076X-RAY DIFFRACTION100
2.26-2.30.29861760.23263153X-RAY DIFFRACTION100
2.3-2.340.29171550.23283130X-RAY DIFFRACTION100
2.34-2.390.2831740.22443099X-RAY DIFFRACTION100
2.39-2.440.25361470.22563139X-RAY DIFFRACTION100
2.44-2.50.25441680.21863125X-RAY DIFFRACTION100
2.5-2.560.26271700.21493129X-RAY DIFFRACTION100
2.56-2.630.24741490.21143132X-RAY DIFFRACTION100
2.63-2.710.27771980.21533119X-RAY DIFFRACTION100
2.71-2.80.23841660.20943117X-RAY DIFFRACTION100
2.8-2.90.24041630.20613147X-RAY DIFFRACTION100
2.9-3.010.23541650.20513114X-RAY DIFFRACTION100
3.01-3.150.19721780.18823173X-RAY DIFFRACTION100
3.15-3.310.18791560.17483110X-RAY DIFFRACTION100
3.31-3.520.1841680.1683138X-RAY DIFFRACTION100
3.52-3.790.17171480.15343155X-RAY DIFFRACTION100
3.79-4.170.17361690.15133164X-RAY DIFFRACTION100
4.17-4.760.15181600.13373154X-RAY DIFFRACTION100
4.76-5.970.15661640.15263160X-RAY DIFFRACTION100
5.98-19.920.18621530.16483228X-RAY DIFFRACTION100

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