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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | JN.1.11+S31deletion spike with 1 missing RBD | |||||||||
Map data | ||||||||||
Sample |
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Keywords | SARS-CoV-2 / COVID-19 / SPIKE / VIRAL PROTEIN | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.0 Å | |||||||||
Authors | Feng Z / Huang J / Ward AB | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: Cell Rep / Year: 2025Title: Structural and functional insights into the evolution of SARS-CoV-2 KP.3.1.1 spike protein. Authors: Ziqi Feng / Jiachen Huang / Sabyasachi Baboo / Jolene K Diedrich / Sandhya Bangaru / James C Paulson / John R Yates / Meng Yuan / Ian A Wilson / Andrew B Ward / ![]() Abstract: The JN.1-sublineage KP.3.1.1 recently emerged as the globally prevalent SARS-CoV-2 variant, demonstrating increased infectivity and antibody escape. We investigate how mutations and a deletion in the ...The JN.1-sublineage KP.3.1.1 recently emerged as the globally prevalent SARS-CoV-2 variant, demonstrating increased infectivity and antibody escape. We investigate how mutations and a deletion in the KP.3.1.1 spike protein (S) affect hACE2 binding and antibody escape. Mass spectrometry confirms a new glycan site at residue N30 that alters the glycoforms at neighboring N61. Cryoelectron microscopy (cryo-EM) structures show that the N30 glycan and rearrangement of adjacent residues do not significantly change the overall spike structure, up-down ratio of receptor-binding domains (RBDs), or hACE2 binding. Furthermore, a KP.3.1.1 S with hACE2 structure further confirms an epistatic effect between F456L and Q493E on hACE2 binding. Our analysis shows that SARS-CoV-2 variants that emerged after late 2023 are now incorporating reversions to residues found in other sarbecoviruses, including the N30 glycan, Q493E, and others. Overall, these results inform on the structural and functional consequences of the KP.3.1.1 mutations, the current SARS-CoV-2 evolutionary trajectory, and immune evasion. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_49907.map.gz | 484 MB | EMDB map data format | |
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| Header (meta data) | emd-49907-v30.xml emd-49907.xml | 13.9 KB 13.9 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_49907_fsc.xml | 17 KB | Display | FSC data file |
| Images | emd_49907.png | 114.8 KB | ||
| Masks | emd_49907_msk_1.map | 512 MB | Mask map | |
| Filedesc metadata | emd-49907.cif.gz | 4.1 KB | ||
| Others | emd_49907_half_map_1.map.gz emd_49907_half_map_2.map.gz | 475.2 MB 475.2 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-49907 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-49907 | HTTPS FTP |
-Validation report
| Summary document | emd_49907_validation.pdf.gz | 1.2 MB | Display | EMDB validaton report |
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| Full document | emd_49907_full_validation.pdf.gz | 1.2 MB | Display | |
| Data in XML | emd_49907_validation.xml.gz | 26.6 KB | Display | |
| Data in CIF | emd_49907_validation.cif.gz | 35.1 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-49907 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-49907 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9eleC ![]() 9elfC ![]() 9elgC ![]() 9elhC ![]() 9eliC ![]() 9eljC ![]() 9elkC ![]() 9ellC ![]() 9elmC ![]() 9elnC ![]() 9eloC ![]() 9elpC ![]() 9elqC C: citing same article ( |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_49907.map.gz / Format: CCP4 / Size: 512 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: 0.718 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_49907_msk_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_49907_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_49907_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : JN.1.11+S31deletion spike with 1 missing RBD
| Entire | Name: JN.1.11+S31deletion spike with 1 missing RBD |
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| Components |
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-Supramolecule #1: JN.1.11+S31deletion spike with 1 missing RBD
| Supramolecule | Name: JN.1.11+S31deletion spike with 1 missing RBD / type: complex / ID: 1 / Parent: 0 |
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| Source (natural) | Organism: ![]() |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | 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 | TFS GLACIOS |
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| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 44.84 e/Å2 |
| Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.7 µm / Nominal defocus min: 0.7000000000000001 µm |
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Keywords
Authors
United States, 1 items
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Processing
FIELD EMISSION GUN

