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Yorodumi- EMDB-32872: S protein of Delta variant in complex with ZWC6 focused on RBD_ZW... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-32872 | |||||||||
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Title | S protein of Delta variant in complex with ZWC6 focused on RBD_ZWC6 sub-complex | |||||||||
Map data | ||||||||||
Sample |
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Biological species | Severe acute respiratory syndrome coronavirus 2 / Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
Authors | Guo YY / Zhang YY | |||||||||
Funding support | China, 2 items
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Citation | Journal: Signal Transduct Target Ther / Year: 2022 Title: Broadly neutralizing antibodies against Omicron-included SARS-CoV-2 variants induced by vaccination. Authors: Xiangyang Chi / Yingying Guo / Guanying Zhang / Hancong Sun / Jun Zhang / Min Li / Zhengshan Chen / Jin Han / Yuanyuan Zhang / Xinghai Zhang / Pengfei Fan / Zhe Zhang / Busen Wang / Xiaodong ...Authors: Xiangyang Chi / Yingying Guo / Guanying Zhang / Hancong Sun / Jun Zhang / Min Li / Zhengshan Chen / Jin Han / Yuanyuan Zhang / Xinghai Zhang / Pengfei Fan / Zhe Zhang / Busen Wang / Xiaodong Zai / Xuelian Han / Meng Hao / Ting Fang / Jinghan Xu / Shipo Wu / Yi Chen / Yingying Fang / Yunzhu Dong / Bingjie Sun / Jinlong Zhang / Jianmin Li / Guangyu Zhao / Changming Yu / Qiang Zhou / Wei Chen / Abstract: The SARS-CoV-2 Omicron variant shows substantial resistance to neutralization by infection- and vaccination-induced antibodies, highlighting the demands for research on the continuing discovery of ...The SARS-CoV-2 Omicron variant shows substantial resistance to neutralization by infection- and vaccination-induced antibodies, highlighting the demands for research on the continuing discovery of broadly neutralizing antibodies (bnAbs). Here, we developed a panel of bnAbs against Omicron and other variants of concern (VOCs) elicited by vaccination of adenovirus-vectored COVID-19 vaccine (Ad5-nCoV). We also investigated the human longitudinal antibody responses following vaccination and demonstrated how the bnAbs evolved over time. A monoclonal antibody (mAb), named ZWD12, exhibited potent and broad neutralization against SARS-CoV-2 variants Alpha, Beta, Gamma, Kappa, Delta, and Omicron by blocking the spike protein binding to the angiotensin-converting enzyme 2 (ACE2) and provided complete protection in the challenged prophylactic and therapeutic K18-hACE2 transgenic mouse model. We defined the ZWD12 epitope by determining its structure in complex with the spike (S) protein via cryo-electron microscopy. This study affords the potential to develop broadly therapeutic mAb drugs and suggests that the RBD epitope bound by ZWD12 is a rational target for the design of a broad spectrum of vaccines. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_32872.map.gz | 86 MB | EMDB map data format | |
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Header (meta data) | emd-32872-v30.xml emd-32872.xml | 11.3 KB 11.3 KB | Display Display | EMDB header |
Images | emd_32872.png | 19.8 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-32872 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-32872 | HTTPS FTP |
-Validation report
Summary document | emd_32872_validation.pdf.gz | 417.2 KB | Display | EMDB validaton report |
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Full document | emd_32872_full_validation.pdf.gz | 416.8 KB | Display | |
Data in XML | emd_32872_validation.xml.gz | 6.1 KB | Display | |
Data in CIF | emd_32872_validation.cif.gz | 7 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-32872 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-32872 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_32872.map.gz / Format: CCP4 / Size: 91.1 MB / 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: 1.087 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Sample components
-Entire : S protein of Delta variant in complex with ZWC6
Entire | Name: S protein of Delta variant in complex with ZWC6 |
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Components |
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-Supramolecule #1: S protein of Delta variant in complex with ZWC6
Supramolecule | Name: S protein of Delta variant in complex with ZWC6 / type: complex / Chimera: Yes / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 |
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-Supramolecule #2: S protein of Delta variant
Supramolecule | Name: S protein of Delta variant / type: complex / Chimera: Yes / ID: 2 / Parent: 1 / Macromolecule list: #1 |
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Source (natural) | Organism: Severe acute respiratory syndrome coronavirus 2 |
Recombinant expression | Organism: Homo sapiens (human) |
-Supramolecule #3: ZWC6
Supramolecule | Name: ZWC6 / type: complex / Chimera: Yes / ID: 3 / Parent: 1 / Macromolecule list: #2-#3 |
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Source (natural) | Organism: Homo sapiens (human) |
Recombinant expression | Organism: Homo sapiens (human) |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 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: 2.2 µm / Nominal defocus min: 1.2 µm |
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
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.0.6) / Number images used: 79751 |
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Initial angle assignment | Type: ANGULAR RECONSTITUTION |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |