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Yorodumi- EMDB-8761: CryoEM structure of rhinovirus B14 in complex with C5 Fab (4 degr... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-8761 | |||||||||
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Title | CryoEM structure of rhinovirus B14 in complex with C5 Fab (4 degrees Celsius, molar ratio 1:3, full particle) | |||||||||
Map data | Inner density masked out. The map has been sharpened. | |||||||||
Sample |
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Function / homology | Function and homology information lysis of host organelle involved in viral entry into host cell / protein complex oligomerization / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / monoatomic ion channel activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane ...lysis of host organelle involved in viral entry into host cell / protein complex oligomerization / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / monoatomic ion channel activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / endocytosis involved in viral entry into host cell / nucleoside-triphosphate phosphatase / DNA replication / RNA helicase activity / induction by virus of host autophagy / RNA-directed RNA polymerase / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / virus-mediated perturbation of host defense response / DNA-templated transcription / host cell nucleus / virion attachment to host cell / structural molecule activity / ATP hydrolysis activity / proteolysis / RNA binding / ATP binding / membrane / metal ion binding Similarity search - Function | |||||||||
Biological species | HRV-14, Human rhinovirus B14 / Mouse (mice) / Human rhinovirus B14 | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.71 Å | |||||||||
Authors | Liu Y / Dong Y / Rossmann MG | |||||||||
Funding support | United States, 1 items
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Citation | Journal: Proc Natl Acad Sci U S A / Year: 2017 Title: Antibody-induced uncoating of human rhinovirus B14. Authors: Yangchao Dong / Yue Liu / Wen Jiang / Thomas J Smith / Zhikai Xu / Michael G Rossmann / Abstract: Rhinoviruses (RVs) are the major causes of common colds in humans. They have a nonenveloped, icosahedral capsid surrounding a positive-strand RNA genome. Here we report that the antigen-binding (Fab) ...Rhinoviruses (RVs) are the major causes of common colds in humans. They have a nonenveloped, icosahedral capsid surrounding a positive-strand RNA genome. Here we report that the antigen-binding (Fab) fragment of a neutralizing antibody (C5) can trigger genome release from RV-B14 to form emptied particles and neutralize virus infection. Using cryo-electron microscopy, structures of the C5 Fab in complex with the full and emptied particles have been determined at 2.3 Å and 3.0 Å resolution, respectively. Each of the 60 Fab molecules binds primarily to a region on viral protein 3 (VP3). Binding of the C5 Fabs to RV-B14 results in significant conformational changes around holes in the capsid through which the viral RNA might exit. These results are so far the highest resolution view of an antibody-virus complex and elucidate a mechanism whereby antibodies neutralize RVs and related viruses by inducing virus uncoating. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_8761.map.gz | 1.1 GB | EMDB map data format | |
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Header (meta data) | emd-8761-v30.xml emd-8761.xml | 24.4 KB 24.4 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_8761_fsc.xml | 23.4 KB | Display | FSC data file |
Images | emd_8761.png | 250.8 KB | ||
Others | emd_8761_half_map_1.map.gz emd_8761_half_map_2.map.gz | 226.4 MB 226.4 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-8761 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-8761 | HTTPS FTP |
-Validation report
Summary document | emd_8761_validation.pdf.gz | 693.1 KB | Display | EMDB validaton report |
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Full document | emd_8761_full_validation.pdf.gz | 692.6 KB | Display | |
Data in XML | emd_8761_validation.xml.gz | 30.6 KB | Display | |
Data in CIF | emd_8761_validation.cif.gz | 41.6 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-8761 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-8761 | HTTPS FTP |
-Related structure data
Related structure data | 5w3lMC 8754C 8762C 8763C 5w3eC 5w3mC 5w3oC C: citing same article (ref.) M: atomic model generated by this map |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_8761.map.gz / Format: CCP4 / Size: 1.1 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Inner density masked out. The map has been sharpened. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Half map: Unmasked, unsharpened half map #1
File | emd_8761_half_map_1.map | ||||||||||||
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Annotation | Unmasked, unsharpened half map #1 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Unmasked, unsharpened half map #2
File | emd_8761_half_map_2.map | ||||||||||||
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Annotation | Unmasked, unsharpened half map #2 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Human rhinovirus B14
Entire | Name: Human rhinovirus B14 |
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Components |
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-Supramolecule #1: Human rhinovirus B14
Supramolecule | Name: Human rhinovirus B14 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: #1-#6 / Details: Viruses were grown in HeLa-H1 cells. / NCBI-ID: 12131 / Sci species name: Human rhinovirus B14 / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: No |
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-Macromolecule #1: viral protein 1
Macromolecule | Name: viral protein 1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: HRV-14, Human rhinovirus B14 |
Molecular weight | Theoretical: 32.560549 KDa |
Sequence | String: GLGDELEEVI VEKTKQTVAS ISSGPKHTQK VPILTANETG ATMPVLPSDS IETRTTYMHF NGSETDVECF LGRAACVHVT EIQNKDATG IDNHREAKLF NDWKINLSSL VQLRKKLELF TYVRFDSEYT ILATASQPDS ANYSSNLVVQ AMYVPPGAPN P KEWDDYTW ...String: GLGDELEEVI VEKTKQTVAS ISSGPKHTQK VPILTANETG ATMPVLPSDS IETRTTYMHF NGSETDVECF LGRAACVHVT EIQNKDATG IDNHREAKLF NDWKINLSSL VQLRKKLELF TYVRFDSEYT ILATASQPDS ANYSSNLVVQ AMYVPPGAPN P KEWDDYTW QSASNPSVFF KVGDTSRFSV PYVGLASAYN CFYDGYSHDD AETQYGITVL NHMGSMAFRI VNEHDEHKTL VK IRVYHRA KHVEAWIPRA PRALPYTSIG RTNYPKNTEP VIKKRKGDIK SY |
-Macromolecule #2: viral protein 3
Macromolecule | Name: viral protein 3 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: HRV-14, Human rhinovirus B14 |
Molecular weight | Theoretical: 26.236754 KDa |
Sequence | String: GLPTTTLPGS GQFLTTDDRQ SPSALPNYEP TPRIHIPGKV HNLLEIIQVD TLIPMNNTHT KDEVNSYLIP LNANRQNEQV FGTNLFIGD GVFKTTLLGE IVQYYTHWSG SLRFSLMYTG PALSSAKLIL AYTPPGARGP QDRREAMLGT HVVWDIGLQS T IVMTIPWT ...String: GLPTTTLPGS GQFLTTDDRQ SPSALPNYEP TPRIHIPGKV HNLLEIIQVD TLIPMNNTHT KDEVNSYLIP LNANRQNEQV FGTNLFIGD GVFKTTLLGE IVQYYTHWSG SLRFSLMYTG PALSSAKLIL AYTPPGARGP QDRREAMLGT HVVWDIGLQS T IVMTIPWT SGVQFRYTDP DTYTSAGFLS CWYQTSLILP PETTGQVYLL SFISACPDFK LRLMKDTQTI SQTVALTE |
-Macromolecule #3: viral protein 2
Macromolecule | Name: viral protein 2 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: HRV-14, Human rhinovirus B14 |
Molecular weight | Theoretical: 28.501361 KDa |
Sequence | String: SPNVEACGYS DRVQQITLGN STITTQEAAN AVVCYAEWPE YLPDVDASDV NKTSKPDTSV CRFYTLDSKT WTTGSKGWCW KLPDALKDM GVFGQNMFFH SLGRSGYTVH VQCNATKFHS GCLLVVVIPE HQLASHEGGN VSVKYTFTHP GERGIDLSSA N EVGGPVKD ...String: SPNVEACGYS DRVQQITLGN STITTQEAAN AVVCYAEWPE YLPDVDASDV NKTSKPDTSV CRFYTLDSKT WTTGSKGWCW KLPDALKDM GVFGQNMFFH SLGRSGYTVH VQCNATKFHS GCLLVVVIPE HQLASHEGGN VSVKYTFTHP GERGIDLSSA N EVGGPVKD VIYNMNGTLL GNLLIFPHQF INLRTNNTAT IVIPYINSVP IDSMTRHNNV SLMVIPIAPL TVPTGATPSL PI TVTIAPM CTEFSGIRSK SIVPQ |
-Macromolecule #4: viral protein 4
Macromolecule | Name: viral protein 4 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: HRV-14, Human rhinovirus B14 |
Molecular weight | Theoretical: 7.183863 KDa |
Sequence | String: GAQVSTQKSG SHENQNILTN GSNQTFTVIN YYKDAASTSS AGQSLSMDPS KFTEPVKDLM LKGAPALN |
-Macromolecule #5: C5 antibody variable heavy domain
Macromolecule | Name: C5 antibody variable heavy domain / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Mouse (mice) |
Molecular weight | Theoretical: 11.989335 KDa |
Sequence | String: AVQLAESGPA LVAPSQALSI TCTVAGFSLT AYGVAWVRQP PGAGLEWLGA IWAAGATDYN AALKSRASIA KDNSKSQVFL AMASLATAD TAAYYCAREW DAYGDYWGQG TTVTVSA |
-Macromolecule #6: C5 antibody variable light domain
Macromolecule | Name: C5 antibody variable light domain / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Mouse (mice) |
Molecular weight | Theoretical: 10.897161 KDa |
Sequence | String: DIVLTQSPAA LSAAAGATVA ATCRASGNIH NALAWYQQKA GKSPQLLVYA AAALAAGVPS RFSGSGSGTA YALAINSLAA DDFGAYYCQ HFWSTPYTFG GGTKLEIK |
-Macromolecule #7: water
Macromolecule | Name: water / type: ligand / ID: 7 / Number of copies: 166 / Formula: HOH |
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Molecular weight | Theoretical: 18.015 Da |
Chemical component information | ChemComp-HOH: |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 8 Details: 20 mM Tris, 120 mM sodium chloride, 1 mM EDTA, pH 8.0 |
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Grid | Model: Ted Pella, Ultrathin lacey carbon / Material: COPPER / Mesh: 400 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Support film - Film thickness: 3.0 nm / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 0.02 kPa |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 85 % / Chamber temperature: 298 K / Instrument: GATAN CRYOPLUNGE 3 |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Digitization - Dimensions - Width: 3710 pixel / Digitization - Dimensions - Height: 3838 pixel / Digitization - Sampling interval: 5.0 µm / Digitization - Frames/image: 4-49 / Number grids imaged: 1 / Number real images: 537 / Average exposure time: 6.0 sec. / Average electron dose: 30.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | C2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 29000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
+Image processing
-Atomic model buiding 1
Details | A combination of the following approaches was used: (1) model rebuilding using Coot, (2) real space refinement using Phenix, (3) reciprocal space refinment using Phenix (as in standard crystallographic refinement). |
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Refinement | Space: REAL / Protocol: RIGID BODY FIT / Target criteria: Correlation coeffcient |
Output model | PDB-5w3l: |