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Yorodumi- EMDB-44280: Chimeric flavivirus between BinJV and YFV-17D in complex with 2C9 Fab -
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Open data
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Basic information
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| Title | Chimeric flavivirus between BinJV and YFV-17D in complex with 2C9 Fab | |||||||||
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Keywords | Flavivirus / Envelope protein / Yellow fever virus / Chimera / VIRUS | |||||||||
| Biological species | ![]() Yellow fever virus | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 7.3 Å | |||||||||
Authors | Bibby S / Jung J / Modhiran N / Watterson D | |||||||||
| Funding support | Australia, 2 items
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Citation | Journal: Nat Commun / Year: 2025Title: A single residue in the yellow fever virus envelope protein modulates virion architecture and antigenicity. Authors: Summa Bibby / James Jung / Yu Shang Low / Alberto A Amarilla / Natalee D Newton / Connor A P Scott / Jessica Balk / Yi Tian Ting / Morgan E Freney / Benjamin Liang / Timothy Grant / Fasséli ...Authors: Summa Bibby / James Jung / Yu Shang Low / Alberto A Amarilla / Natalee D Newton / Connor A P Scott / Jessica Balk / Yi Tian Ting / Morgan E Freney / Benjamin Liang / Timothy Grant / Fasséli Coulibaly / Paul Young / Roy A Hall / Jody Hobson-Peters / Naphak Modhiran / Daniel Watterson / ![]() Abstract: Yellow fever virus (YFV) is a re-emerging flavivirus that causes severe hepatic disease and mortality in humans. Despite being researched for over a century, the structure of YFV has remained elusive. ...Yellow fever virus (YFV) is a re-emerging flavivirus that causes severe hepatic disease and mortality in humans. Despite being researched for over a century, the structure of YFV has remained elusive. Here we use a chimeric virus platform to resolve the first high resolution cryo-EM structures of YFV. Stark differences in particle morphology and homogeneity are observed between vaccine and virulent strains of YFV, and these are found to have significant implications on antibody recognition and neutralisation. We identify a single residue (R380) in the YFV envelope protein that stabilises the virion surface, and leads to reduced exposure of the cross-reactive fusion loop epitope. The differences in virion morphology between YFV strains also contribute to the reduced sensitivity of the virulent YFV virions to vaccine-induced antibodies. These findings have significant implications for YFV biology, vaccinology and structure-based flavivirus antigen design. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_44280.map.gz | 510.3 MB | EMDB map data format | |
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| Header (meta data) | emd-44280-v30.xml emd-44280.xml | 16.5 KB 16.5 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_44280_fsc.xml | 26.7 KB | Display | FSC data file |
| Images | emd_44280.png | 197.6 KB | ||
| Filedesc metadata | emd-44280.cif.gz | 4.5 KB | ||
| Others | emd_44280_half_map_1.map.gz emd_44280_half_map_2.map.gz | 1.3 GB 1.3 GB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-44280 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-44280 | HTTPS FTP |
-Validation report
| Summary document | emd_44280_validation.pdf.gz | 1.2 MB | Display | EMDB validaton report |
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| Full document | emd_44280_full_validation.pdf.gz | 1.1 MB | Display | |
| Data in XML | emd_44280_validation.xml.gz | 33.4 KB | Display | |
| Data in CIF | emd_44280_validation.cif.gz | 45.2 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-44280 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-44280 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_44280.map.gz / Format: CCP4 / Size: 1.6 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.96 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #1
| File | emd_44280_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_44280_half_map_2.map | ||||||||||||
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Sample components
-Entire : Yellow fever virus
| Entire | Name: Yellow fever virus |
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| Components |
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-Supramolecule #1: Yellow fever virus
| Supramolecule | Name: Yellow fever virus / type: complex / ID: 1 / Parent: 0 Details: YFV envelope and membrane proteins expressed in the backbone of Binjari virus |
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-Supramolecule #3: 2C9 Fab
| Supramolecule | Name: 2C9 Fab / type: complex / ID: 3 / Parent: 1 |
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| Source (natural) | Organism: ![]() |
-Supramolecule #2: Yellow fever virus
| Supramolecule | Name: Yellow fever virus / type: virus / ID: 2 / Parent: 1 / NCBI-ID: 11089 / Sci species name: Yellow fever virus / Virus type: VIRION / Virus isolate: OTHER / Virus enveloped: Yes / Virus empty: No |
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-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 8 Component:
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| Vitrification | Cryogen name: ETHANE / Instrument: LEICA EM GP |
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Electron microscopy
| Microscope | JEOL CRYO ARM 300 |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 54.25 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 20.0 µm / Nominal defocus min: 20.0 µm |
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About Yorodumi



Yellow fever virus
Keywords
Authors
Australia, 2 items
Citation






















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Processing
FIELD EMISSION GUN
