+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-11400 | |||||||||
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Title | Ferritin | |||||||||
Map data | Ferritin | |||||||||
Sample |
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Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / negative staining / Resolution: 19.0 Å | |||||||||
Authors | Perez L | |||||||||
Citation | Journal: PLoS Pathog / Year: 2020 Title: Rationally designed Human Cytomegalovirus gB nanoparticle vaccine with improved immunogenicity. Authors: Michela Perotti / Jessica Marcandalli / Davide Demurtas / Federica Sallusto / Laurent Perez / Abstract: Human cytomegalovirus (HCMV) is the primary viral cause of congenital birth defects and causes significant morbidity and mortality in immune-suppressed transplant recipients. Despite considerable ...Human cytomegalovirus (HCMV) is the primary viral cause of congenital birth defects and causes significant morbidity and mortality in immune-suppressed transplant recipients. Despite considerable efforts in vaccine development, HCMV infection still represents an unmet clinical need. In recent phase II trials, a MF59-adjuvanted gB vaccine showed only modest efficacy in preventing infection. These findings might be attributed to low level of antibodies (Abs) with a neutralizing activity induced by this vaccine. Here, we analyzed the immunogenicity of each gB antigenic domain (AD) and demonstrated that domain I of gB (AD5) is the main target of HCMV neutralizing antibodies. Furthermore, we designed, characterized and evaluated immunogenic responses to two different nanoparticles displaying a trimeric AD5 antigen. We showed that mice immunization with nanoparticles induces sera neutralization titers up to 100-fold higher compared to those obtained with the gB extracellular domain (gBECD). Collectively, these results illustrate with a medically relevant example the advantages of using a general approach combining antigen discovery, protein engineering and scaffold presentation for modern development of subunit vaccines against complex pathogens. | |||||||||
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_11400.map.gz | 58.9 MB | EMDB map data format | |
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Header (meta data) | emd-11400-v30.xml emd-11400.xml | 7.4 KB 7.4 KB | Display Display | EMDB header |
Images | emd_11400.png | 16.8 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-11400 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-11400 | HTTPS FTP |
-Validation report
Summary document | emd_11400_validation.pdf.gz | 294.7 KB | Display | EMDB validaton report |
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Full document | emd_11400_full_validation.pdf.gz | 294.3 KB | Display | |
Data in XML | emd_11400_validation.xml.gz | 6.5 KB | Display | |
Data in CIF | emd_11400_validation.cif.gz | 7.4 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-11400 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-11400 | HTTPS FTP |
-Related structure data
Related structure data | C: citing same article (ref.) |
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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_11400.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Ferritin | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 2.57813 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
-Entire : Ferritin
Entire | Name: Ferritin |
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Components |
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-Supramolecule #1: Ferritin
Supramolecule | Name: Ferritin / type: organelle_or_cellular_component / ID: 1 / Parent: 0 |
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Source (natural) | Organism: Homo sapiens (human) |
-Experimental details
-Structure determination
Method | negative staining |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7 |
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Staining | Type: NEGATIVE / Material: uranyl acetate |
Grid | Model: Quantifoil / Material: GRAPHENE OXIDE / Mesh: 400 / Pretreatment - Type: GLOW DISCHARGE |
-Electron microscopy
Microscope | FEI TECNAI 20 |
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Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: OTHER / Average electron dose: 70.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: OTHER |
-Image processing
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 19.0 Å / Resolution method: OTHER / Software - Name: cryoSPARC / Number images used: 2983 |
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Initial angle assignment | Type: NOT APPLICABLE |
Final angle assignment | Type: NOT APPLICABLE |