+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-26369 | |||||||||
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Title | SARS-2 CoV 6P Mut7 in complex with Fab CC25.36 | |||||||||
Map data | SARS-2 CoV 6P Mut7 in complex with CC25.36 | |||||||||
Sample |
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Keywords | spike protein / coronavirus / VIRAL PROTEIN-IMMUNE SYSTEM complex | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / negative staining / Resolution: 25.0 Å | |||||||||
Authors | Torres JL / Ward AB | |||||||||
Funding support | United States, 1 items
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Citation | Journal: Nat Immunol / Year: 2022 Title: Targeted isolation of diverse human protective broadly neutralizing antibodies against SARS-like viruses. Authors: Wan-Ting He / Rami Musharrafieh / Ge Song / Katharina Dueker / Longping V Tse / David R Martinez / Alexandra Schäfer / Sean Callaghan / Peter Yong / Nathan Beutler / Jonathan L Torres / ...Authors: Wan-Ting He / Rami Musharrafieh / Ge Song / Katharina Dueker / Longping V Tse / David R Martinez / Alexandra Schäfer / Sean Callaghan / Peter Yong / Nathan Beutler / Jonathan L Torres / Reid M Volk / Panpan Zhou / Meng Yuan / Hejun Liu / Fabio Anzanello / Tazio Capozzola / Mara Parren / Elijah Garcia / Stephen A Rawlings / Davey M Smith / Ian A Wilson / Yana Safonova / Andrew B Ward / Thomas F Rogers / Ralph S Baric / Lisa E Gralinski / Dennis R Burton / Raiees Andrabi / Abstract: The emergence of current severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants of concern (VOCs) and potential future spillovers of SARS-like coronaviruses into humans pose a major ...The emergence of current severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants of concern (VOCs) and potential future spillovers of SARS-like coronaviruses into humans pose a major threat to human health and the global economy. Development of broadly effective coronavirus vaccines that can mitigate these threats is needed. Here, we utilized a targeted donor selection strategy to isolate a large panel of human broadly neutralizing antibodies (bnAbs) to sarbecoviruses. Many of these bnAbs are remarkably effective in neutralizing a diversity of sarbecoviruses and against most SARS-CoV-2 VOCs, including the Omicron variant. Neutralization breadth is achieved by bnAb binding to epitopes on a relatively conserved face of the receptor-binding domain (RBD). Consistent with targeting of conserved sites, select RBD bnAbs exhibited protective efficacy against diverse SARS-like coronaviruses in a prophylaxis challenge model in vivo. These bnAbs provide new opportunities and choices for next-generation antibody prophylactic and therapeutic applications and provide a molecular basis for effective design of pan-sarbecovirus vaccines. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_26369.map.gz | 49.6 MB | EMDB map data format | |
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Header (meta data) | emd-26369-v30.xml emd-26369.xml | 13.2 KB 13.2 KB | Display Display | EMDB header |
Images | emd_26369.png | 30.6 KB | ||
Filedesc metadata | emd-26369.cif.gz | 4 KB | ||
Others | emd_26369_half_map_1.map.gz emd_26369_half_map_2.map.gz | 49.7 MB 49.7 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-26369 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-26369 | HTTPS FTP |
-Validation report
Summary document | emd_26369_validation.pdf.gz | 734.7 KB | Display | EMDB validaton report |
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Full document | emd_26369_full_validation.pdf.gz | 734.3 KB | Display | |
Data in XML | emd_26369_validation.xml.gz | 12.3 KB | Display | |
Data in CIF | emd_26369_validation.cif.gz | 14.5 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-26369 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-26369 | HTTPS FTP |
-Related structure data
Related structure data | C: citing same article (ref.) |
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-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_26369.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | SARS-2 CoV 6P Mut7 in complex with CC25.36 | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 2.06 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_26369_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_26369_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : SARS-2 CoV 6P Mut7 in complex with Fab CC25.36
Entire | Name: SARS-2 CoV 6P Mut7 in complex with Fab CC25.36 |
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Components |
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-Supramolecule #1: SARS-2 CoV 6P Mut7 in complex with Fab CC25.36
Supramolecule | Name: SARS-2 CoV 6P Mut7 in complex with Fab CC25.36 / type: complex / 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: 7.4 |
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Staining | Type: NEGATIVE / Material: Uranyl Formate |
-Electron microscopy
Microscope | FEI TECNAI SPIRIT |
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Image recording | Film or detector model: FEI EAGLE (4k x 4k) / Average electron dose: 25.0 e/Å2 |
Electron beam | Acceleration voltage: 120 kV / Electron source: LAB6 |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.5 µm / Nominal defocus min: 1.5 µm |
Experimental equipment | Model: Tecnai Spirit / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: NONE |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 25.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 5569 |
Initial angle assignment | Type: ANGULAR RECONSTITUTION |
Final angle assignment | Type: ANGULAR RECONSTITUTION |