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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | EEEV + EEEV-179 Fab at pH 5.6 | |||||||||
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Sample |
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Keywords | Eastern Equine Encephalitis Virus / Cryo-EM / Single Particle Averaging / localized reconstruction / asymmetric unit / low pH back neutralization. / VIRUS | |||||||||
| Biological species | ![]() Eastern equine encephalitis virus | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 11.3 Å | |||||||||
Authors | Bandyopadhyay A / Klose T / Kuhn RJ | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: Nat Commun / Year: 2026Title: Asymmetric structural transitions in the icosahedral organization of Eastern equine encephalitis virus. Authors: Abhishek Bandyopadhyay / Lauren E Williamson / Cameron D Buchman / Thomas Klose / James E Crowe / Richard J Kuhn / ![]() Abstract: Delivery of the viral genome into host cells is a critical step in successful viral infection. Alphaviruses achieve this step by fusing the viral and endosomal membranes under acidic conditions. This ...Delivery of the viral genome into host cells is a critical step in successful viral infection. Alphaviruses achieve this step by fusing the viral and endosomal membranes under acidic conditions. This process requires significant structural changes in the alphavirus glycoprotein organization. Structural characterization of acidic pH-induced conformational changes in alphavirus virions has remained elusive due to the rapid, transient nature of these states, conformational heterogeneity, and particle aggregation. Antibody binding studies conducted at elevated temperatures or under acidic pH conditions have further revealed the presence of transitional epitopes that are inaccessible on alphaviruses at room temperature or neutral pH. In this report, we present structural snapshots of the conformational changes in the glycoproteins and nucleocapsid core of a prototypical alphavirus, Eastern equine encephalitis virus, caused by exposure to 40 °C or pH 5.6. These findings provide insights into the structural transitions that occur prior to viral fusion with the endosomal membrane. This approach has also allowed us to define the molecular basis for recognition of a pan-alphavirus epitope by a patient-derived human antibody. | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_73024.map.gz | 30.9 MB | EMDB map data format | |
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| Header (meta data) | emd-73024-v30.xml emd-73024.xml | 16.3 KB 16.3 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_73024_fsc.xml | 8.5 KB | Display | FSC data file |
| Images | emd_73024.png | 47.4 KB | ||
| Filedesc metadata | emd-73024.cif.gz | 4.6 KB | ||
| Others | emd_73024_half_map_1.map.gz emd_73024_half_map_2.map.gz | 59.1 MB 59.1 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-73024 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-73024 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_73024.map.gz / Format: CCP4 / Size: 64 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: 4.16 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #1
| File | emd_73024_half_map_1.map | ||||||||||||
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-Half map: #2
| File | emd_73024_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : Eastern equine encephalitis virus
| Entire | Name: ![]() Eastern equine encephalitis virus |
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| Components |
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-Supramolecule #1: Eastern equine encephalitis virus
| Supramolecule | Name: Eastern equine encephalitis virus / type: virus / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 / NCBI-ID: 11021 / Sci species name: Eastern equine encephalitis virus / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: Yes / Virus empty: No |
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| Host (natural) | Organism: Culiseta melanura (mosquito) |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 1 mg/mL |
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| Buffer | pH: 5.6 |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 90 % / Chamber temperature: 298 K |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 36.2 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: 2.0 µm / Nominal defocus min: 0.6 µm |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Initial model | Chain - Source name: Other / Chain - Initial model type: other |
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| Refinement | Protocol: OTHER |
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About Yorodumi





Eastern equine encephalitis virus
Keywords
Authors
United States, 1 items
Citation














Z (Sec.)
Y (Row.)
X (Col.)




































Culiseta melanura (mosquito)
FIELD EMISSION GUN

