Database: EMDB / ID: EMD-25000
*YMImages and movies for this entry are currently under preparation
|Title||Structure of SARS-CoV-2 spike in complex with polyclonal Fab15|
|Map data||Sharpened map|
|Biological species||Severe acute respiratory syndrome coronavirus 2|
|Method||single particle reconstruction / cryo EM / Resolution: 4.1 Å|
|Authors||Ward AB / Bangaru S / Antanasijevic A|
|Funding support|| United States, 2 items |
|Citation||Journal: Sci Adv / Year: 2022|
Title: Structural mapping of antibody landscapes to human betacoronavirus spike proteins.
Authors: Sandhya Bangaru / Aleksandar Antanasijevic / Nurgun Kose / Leigh M Sewall / Abigail M Jackson / Naveenchandra Suryadevara / Xiaoyan Zhan / Jonathan L Torres / Jeffrey Copps / Alba Torrents ...Authors: Sandhya Bangaru / Aleksandar Antanasijevic / Nurgun Kose / Leigh M Sewall / Abigail M Jackson / Naveenchandra Suryadevara / Xiaoyan Zhan / Jonathan L Torres / Jeffrey Copps / Alba Torrents de la Peña / James E Crowe / Andrew B Ward /
Abstract: Preexisting immunity against seasonal coronaviruses (CoVs) represents an important variable in predicting antibody responses and disease severity to severe acute respiratory syndrome CoV-2 (SARS-CoV- ...Preexisting immunity against seasonal coronaviruses (CoVs) represents an important variable in predicting antibody responses and disease severity to severe acute respiratory syndrome CoV-2 (SARS-CoV-2) infections. We used electron microscopy-based polyclonal epitope mapping (EMPEM) to characterize the antibody specificities against β-CoV spike proteins in prepandemic (PP) sera or SARS-CoV-2 convalescent (SC) sera. We observed that most PP sera had antibodies specific to seasonal human CoVs (HCoVs) OC43 and HKU1 spike proteins while the SC sera showed reactivity across all human β-CoVs. Detailed molecular mapping of spike-antibody complexes revealed epitopes that were differentially targeted by preexisting antibodies and SC serum antibodies. Our studies provide an antigenic landscape to β-HCoV spikes in the general population serving as a basis for cross-reactive epitope analyses in SARS-CoV-2-infected individuals.
Downloads & links
|File||Download / File: emd_25000.map.gz / Format: CCP4 / Size: 209.3 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.045 Å|
|Symmetry||Space group: 1|
|Projections & Slices|
-Half map: Half map 1
|Annotation||Half map 1|
|Projections & Slices|
-Half map: Half map 2
-Entire : Structure of SARS-CoV-2 spike in complex with polyclonal Fab15
|Entire||Name: Structure of SARS-CoV-2 spike in complex with polyclonal Fab15|
-Supramolecule #1: Structure of SARS-CoV-2 spike in complex with polyclonal Fab15
|Supramolecule||Name: Structure of SARS-CoV-2 spike in complex with polyclonal Fab15|
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
|Source (natural)||Organism: Severe acute respiratory syndrome coronavirus 2|
|Recombinant expression||Organism: Homo sapiens (human) / Recombinant cell: 293F cells|
|Processing||single particle reconstruction|
|Buffer||pH: 7.4 |
Details: TBS 1X
|Grid||Model: Quantifoil R1.2/1.3 / Pretreatment - Type: PLASMA CLEANING|
|Vitrification||Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 283 K / Instrument: FEI VITROBOT MARK IV|
|Microscope||FEI TITAN KRIOS|
|Electron beam||Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN|
|Electron optics||C2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 1.7 µm / Nominal defocus min: 0.7000000000000001 µm / Nominal magnification: 29000|
|Sample stage||Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN|
|Image recording||Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Number real images: 5405 / Average exposure time: 7.5 sec. / Average electron dose: 50.0 e/Å2|
Model: Titan Krios / Image courtesy: FEI Company
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