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- EMDB-32676: Cryo-EM structure of SARS-CoV-2 recombinant spike protein STFK in... -
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Open data
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Basic information
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Title | Cryo-EM structure of SARS-CoV-2 recombinant spike protein STFK in complex with three neutralizing antibodies | |||||||||
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![]() | SARS-CoV-2 / spike / vaccine / neutralizing antibody / Cryo-EM / VIRAL PROTEIN / IMMUNE SYSTEM-VIRAL PROTEIN complex | |||||||||
Function / homology | ![]() Maturation of spike protein / viral translation / Translation of Structural Proteins / Virion Assembly and Release / host cell surface / host extracellular space / suppression by virus of host tetherin activity / Induction of Cell-Cell Fusion / structural constituent of virion / entry receptor-mediated virion attachment to host cell ...Maturation of spike protein / viral translation / Translation of Structural Proteins / Virion Assembly and Release / host cell surface / host extracellular space / suppression by virus of host tetherin activity / Induction of Cell-Cell Fusion / structural constituent of virion / entry receptor-mediated virion attachment to host cell / host cell endoplasmic reticulum-Golgi intermediate compartment membrane / receptor-mediated endocytosis of virus by host cell / Attachment and Entry / membrane fusion / symbiont-mediated suppression of host innate immune response / positive regulation of viral entry into host cell / receptor-mediated virion attachment to host cell / receptor ligand activity / host cell surface receptor binding / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / SARS-CoV-2 activates/modulates innate and adaptive immune responses / host cell plasma membrane / virion membrane / identical protein binding / membrane / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.81 Å | |||||||||
![]() | Zheng Q / Sun H | |||||||||
Funding support | 1 items
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![]() | ![]() Title: Lineage-mosaic and mutation-patched spike proteins for broad-spectrum COVID-19 vaccine. Authors: Yangtao Wu / Shaojuan Wang / Yali Zhang / Lunzhi Yuan / Qingbing Zheng / Min Wei / Yang Shi / Zikang Wang / Jian Ma / Kai Wang / Meifeng Nie / Jin Xiao / Zehong Huang / Peiwen Chen / Huilin ...Authors: Yangtao Wu / Shaojuan Wang / Yali Zhang / Lunzhi Yuan / Qingbing Zheng / Min Wei / Yang Shi / Zikang Wang / Jian Ma / Kai Wang / Meifeng Nie / Jin Xiao / Zehong Huang / Peiwen Chen / Huilin Guo / Miaolin Lan / Jingjing Xu / Wangheng Hou / Yunda Hong / Dabing Chen / Hui Sun / Hualong Xiong / Ming Zhou / Che Liu / Wenjie Guo / Huiyu Guo / Jiahua Gao / Congling Gan / Zhixiong Li / Haitao Zhang / Xinrui Wang / Shaowei Li / Tong Cheng / Qinjian Zhao / Yixin Chen / Ting Wu / Tianying Zhang / Jun Zhang / Hua Cao / Huachen Zhu / Quan Yuan / Yi Guan / Ningshao Xia / ![]() Abstract: SARS-CoV-2 spread in humans results in continuous emergence of new variants, highlighting the need for vaccines with broad-spectrum antigenic coverage. Using inter-lineage chimera and mutation-patch ...SARS-CoV-2 spread in humans results in continuous emergence of new variants, highlighting the need for vaccines with broad-spectrum antigenic coverage. Using inter-lineage chimera and mutation-patch strategies, we engineered a recombinant monomeric spike variant (STFK1628x) that contains key regions and residues across multiple SAR-CoV-2 variants. STFK1628x demonstrated high immunogenicity and mutually complementary antigenicity to its prototypic form (STFK). In hamsters, a bivalent vaccine composed of STFK and STFK1628x elicited high titers of broad-spectrum neutralizing antibodies to 19 circulating SARS-CoV-2 variants, including Omicron sublineages BA.1, BA.1.1, BA.2, BA.2.12.1, BA.2.75, and BA.4/5. Furthermore, this vaccine conferred robust protection against intranasal challenges by either SARS-CoV-2 ancestral strain or immune-evasive Beta and Omicron BA.1. Strikingly, vaccination with the bivalent vaccine in hamsters effectively blocked within-cage virus transmission of ancestral SARS-CoV-2, Beta variant, and Omicron BA.1 to unvaccinated sentinels. Thus, our study provided insight and antigen candidates for the development of next-generation COVID-19 vaccines. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 230 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 18 KB 18 KB | Display Display | ![]() |
Images | ![]() | 24.8 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7wp6MC ![]() 7wp8C M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Voxel size | X=Y=Z: 0.778 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
+Entire : Cryo-EM structure of SARS-CoV-2 recombinant spike protein STFK in...
+Supramolecule #1: Cryo-EM structure of SARS-CoV-2 recombinant spike protein STFK in...
+Supramolecule #2: neutralizing antibodies
+Supramolecule #3: spike protein STFK
+Macromolecule #1: 36H6 heavy chain
+Macromolecule #2: 83H7 light chain
+Macromolecule #3: 83H7 heavy chain
+Macromolecule #4: Spike protein S1
+Macromolecule #5: 85F7 heavy chain
+Macromolecule #6: 36H6 light chain
+Macromolecule #7: 85F7 light chain
+Macromolecule #9: 2-acetamido-2-deoxy-beta-D-glucopyranose
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TECNAI F30 |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.5 µm / Nominal defocus min: 1.2 µm |
Experimental equipment | ![]() Model: Tecnai F30 / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: OTHER |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.81 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 162177 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |