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- PDB-4fqi: Crystal Structure of Fab CR9114 in Complex with a H5N1 influenza ... -

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Basic information

Entry
Database: PDB / ID: 4fqi
TitleCrystal Structure of Fab CR9114 in Complex with a H5N1 influenza virus hemagglutinin
Components
  • (Hemagglutinin ...) x 2
  • (antibody CR9114 ...) x 2
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / neutralizing antibodies / antibody affinity / antigens / epitopes / glycosylation / hemagglutinin glycoproteins / immunoglobulin Fab fragments / H5N1 subtype / influenza vaccines / avian flu / envelope protein / VIRAL PROTEIN-IMMUNE SYSTEM complex
Function / homology
Function and homology information


clathrin-dependent endocytosis of virus by host cell / host cell surface receptor binding / apical plasma membrane / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane / identical protein binding
Similarity search - Function
Hemagglutinin; Chain A, domain 2 / Hemagglutinin Chain A, Domain 2 / Hemagglutinin Ectodomain; Chain B - #10 / Hemagglutinin Ectodomain; Chain B / Hemagglutinin (Ha1 Chain); Chain: A; domain 1 / Haemagglutinin, alpha/beta domain, HA1 chain / Haemagglutinin, influenzavirus A / Haemagglutinin, HA1 chain, alpha/beta domain superfamily / Haemagglutinin / Haemagglutinin, influenzavirus A/B ...Hemagglutinin; Chain A, domain 2 / Hemagglutinin Chain A, Domain 2 / Hemagglutinin Ectodomain; Chain B - #10 / Hemagglutinin Ectodomain; Chain B / Hemagglutinin (Ha1 Chain); Chain: A; domain 1 / Haemagglutinin, alpha/beta domain, HA1 chain / Haemagglutinin, influenzavirus A / Haemagglutinin, HA1 chain, alpha/beta domain superfamily / Haemagglutinin / Haemagglutinin, influenzavirus A/B / Viral capsid/haemagglutinin protein / Ribbon / Immunoglobulins / Alpha-Beta Complex / Immunoglobulin-like / Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Biological speciesInfluenza A virus
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.71 Å
AuthorsDreyfus, C. / Wilson, I.A.
CitationJournal: Science / Year: 2012
Title: Highly conserved protective epitopes on influenza B viruses.
Authors: Cyrille Dreyfus / Nick S Laursen / Ted Kwaks / David Zuijdgeest / Reza Khayat / Damian C Ekiert / Jeong Hyun Lee / Zoltan Metlagel / Miriam V Bujny / Mandy Jongeneelen / Remko van der Vlugt ...Authors: Cyrille Dreyfus / Nick S Laursen / Ted Kwaks / David Zuijdgeest / Reza Khayat / Damian C Ekiert / Jeong Hyun Lee / Zoltan Metlagel / Miriam V Bujny / Mandy Jongeneelen / Remko van der Vlugt / Mohammed Lamrani / Hans J W M Korse / Eric Geelen / Özcan Sahin / Martijn Sieuwerts / Just P J Brakenhoff / Ronald Vogels / Olive T W Li / Leo L M Poon / Malik Peiris / Wouter Koudstaal / Andrew B Ward / Ian A Wilson / Jaap Goudsmit / Robert H E Friesen /
Abstract: Identification of broadly neutralizing antibodies against influenza A viruses has raised hopes for the development of monoclonal antibody-based immunotherapy and "universal" vaccines for influenza. ...Identification of broadly neutralizing antibodies against influenza A viruses has raised hopes for the development of monoclonal antibody-based immunotherapy and "universal" vaccines for influenza. However, a substantial part of the annual flu burden is caused by two cocirculating, antigenically distinct lineages of influenza B viruses. Here, we report human monoclonal antibodies, CR8033, CR8071, and CR9114, that protect mice against lethal challenge from both lineages. Antibodies CR8033 and CR8071 recognize distinct conserved epitopes in the head region of the influenza B hemagglutinin (HA), whereas CR9114 binds a conserved epitope in the HA stem and protects against lethal challenge with influenza A and B viruses. These antibodies may inform on development of monoclonal antibody-based treatments and a universal flu vaccine for all influenza A and B viruses.
History
DepositionJun 25, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 22, 2012Provider: repository / Type: Initial release
Revision 1.1Oct 3, 2012Group: Database references
Revision 1.2Jan 31, 2018Group: Database references / Category: citation_author / Item: _citation_author.name
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_special_symmetry / struct_asym / struct_conn / struct_ref_seq_dif / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _chem_comp.name / _chem_comp.type / _pdbx_entity_nonpoly.entity_id / _pdbx_entity_nonpoly.name / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_special_symmetry.label_asym_id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Hemagglutinin HA1
B: Hemagglutinin HA2
H: antibody CR9114 heavy chain
L: antibody CR9114 light chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)107,48920
Polymers105,6264
Non-polymers1,86316
Water19,6541091
1
A: Hemagglutinin HA1
B: Hemagglutinin HA2
H: antibody CR9114 heavy chain
L: antibody CR9114 light chain
hetero molecules

A: Hemagglutinin HA1
B: Hemagglutinin HA2
H: antibody CR9114 heavy chain
L: antibody CR9114 light chain
hetero molecules

A: Hemagglutinin HA1
B: Hemagglutinin HA2
H: antibody CR9114 heavy chain
L: antibody CR9114 light chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)322,46660
Polymers316,87812
Non-polymers5,58948
Water21612
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_665-y+1,x-y+1,z1
crystal symmetry operation3_565-x+y,-x+1,z1
Unit cell
Length a, b, c (Å)141.641, 141.641, 382.924
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number155
Space group name H-MH32
Components on special symmetry positions
IDModelComponents
11B-462-

HOH

21B-466-

HOH

31B-515-

HOH

41B-521-

HOH

51B-531-

HOH

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Components

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Hemagglutinin ... , 2 types, 2 molecules AB

#1: Protein Hemagglutinin HA1 / hemagglutinin receptor binding subunit HA1


Mass: 37948.020 Da / Num. of mol.: 1 / Fragment: UNP residues 17-346
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Influenza A virus / Strain: A/Viet Nam/1203/2004(H5N1) / Gene: HA / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q6DQ33
#2: Protein Hemagglutinin HA2 / hemagglutinin membrane fusion subunit HA2


Mass: 20414.504 Da / Num. of mol.: 1 / Fragment: UNP residues 347-520
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Influenza A virus / Strain: A/Viet Nam/1203/2004(H5N1) / Gene: HA / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q6DQ33

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Antibody , 2 types, 2 molecules HL

#3: Antibody antibody CR9114 heavy chain


Mass: 24423.191 Da / Num. of mol.: 1 / Fragment: Fab
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Trichoplusia ni (cabbage looper)
#4: Antibody antibody CR9114 light chain


Mass: 22840.172 Da / Num. of mol.: 1 / Fragment: Fab Lambda
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Trichoplusia ni (cabbage looper)

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Sugars , 2 types, 4 molecules

#5: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#7: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 3 types, 1103 molecules

#6: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 11 / Source method: obtained synthetically / Formula: C2H6O2
#8: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#9: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 1091 / Source method: isolated from a natural source / Formula: H2O

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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: 3.5 Å3/Da / Density % sol: 64.85 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7
Details: 0.16 M sodium thiocyanate, 15% PEG3350, 100 mM Tris, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 75 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL7-1 / Wavelength: 1.033 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: May 6, 2011
RadiationMonochromator: Side scattering I-beam bent single crystal, asymmetric cut 4.9650 degrees
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.033 Å / Relative weight: 1
ReflectionResolution: 1.71→50 Å / Num. all: 158783 / Num. obs: 158783 / % possible obs: 99.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3
Reflection shellResolution: 1.71→1.74 Å / % possible all: 89.4

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Processing

Software
NameVersionClassification
Blu-Icedata collection
PHASERphasing
PHENIX(phenix.refine: 1.7.2_869)refinement
HKL-2000data reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.71→36.553 Å / SU ML: 0.56 / σ(F): 1.33 / Phase error: 25.91 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2322 7881 5.01 %RANDOM
Rwork0.1983 ---
obs0.2 157212 98.87 %-
all-157212 --
Solvent computationShrinkage radii: 0.86 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 50.052 Å2 / ksol: 0.354 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-0.16 Å20 Å2-0 Å2
2--0.16 Å2-0 Å2
3----0.0001 Å2
Refinement stepCycle: LAST / Resolution: 1.71→36.553 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7154 0 120 1091 8365
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0187634
X-RAY DIFFRACTIONf_angle_d1.64210366
X-RAY DIFFRACTIONf_dihedral_angle_d15.0992818
X-RAY DIFFRACTIONf_chiral_restr0.1281130
X-RAY DIFFRACTIONf_plane_restr0.0081352
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.71-1.72960.38472300.35114849X-RAY DIFFRACTION96
1.7296-1.750.39252360.36284972X-RAY DIFFRACTION99
1.75-1.77130.41932510.34334992X-RAY DIFFRACTION100
1.7713-1.79370.36642590.32994970X-RAY DIFFRACTION100
1.7937-1.81730.40142470.32394993X-RAY DIFFRACTION99
1.8173-1.84220.3362930.31234922X-RAY DIFFRACTION99
1.8422-1.86850.34792570.30854970X-RAY DIFFRACTION99
1.8685-1.89640.29982700.28444922X-RAY DIFFRACTION99
1.8964-1.9260.35342400.28644963X-RAY DIFFRACTION99
1.926-1.95760.29562490.26564940X-RAY DIFFRACTION99
1.9576-1.99140.25532550.22975016X-RAY DIFFRACTION100
1.9914-2.02760.26272290.22045022X-RAY DIFFRACTION100
2.0276-2.06660.25832940.22484906X-RAY DIFFRACTION99
2.0666-2.10880.24622590.21535033X-RAY DIFFRACTION100
2.1088-2.15460.22972600.20224975X-RAY DIFFRACTION100
2.1546-2.20470.23672800.20234994X-RAY DIFFRACTION99
2.2047-2.25980.26982640.21114954X-RAY DIFFRACTION99
2.2598-2.32090.28012610.21494939X-RAY DIFFRACTION98
2.3209-2.38920.25632810.20724894X-RAY DIFFRACTION98
2.3892-2.46630.2322470.20474947X-RAY DIFFRACTION98
2.4663-2.55450.28032560.21124945X-RAY DIFFRACTION98
2.5545-2.65670.23712630.20524967X-RAY DIFFRACTION98
2.6567-2.77760.24742640.20064965X-RAY DIFFRACTION99
2.7776-2.9240.21762890.19894958X-RAY DIFFRACTION98
2.924-3.10710.24562840.19114948X-RAY DIFFRACTION99
3.1071-3.34680.2172810.19095049X-RAY DIFFRACTION99
3.3468-3.68330.21342890.17385024X-RAY DIFFRACTION100
3.6833-4.21560.1812600.15865097X-RAY DIFFRACTION100
4.2156-5.30870.16152890.14485105X-RAY DIFFRACTION100
5.3087-36.56110.22152440.18765100X-RAY DIFFRACTION95

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