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Yorodumi- EMDB-54510: Echovirus 18 particle missing two pentamers in situ, asymmetric r... -
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Basic information
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| Title | Echovirus 18 particle missing two pentamers in situ, asymmetric reconstruction | |||||||||
Map data | Main map | |||||||||
Sample |
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Keywords | Virus / in situ structure | |||||||||
| Biological species | Echovirus E18 | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 9.6 Å | |||||||||
Authors | Mukhamedova L / Plevka P / Trebichalska Z / Novacek J | |||||||||
| Funding support | European Union, 1 items
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Citation | Journal: Proc Natl Acad Sci U S A / Year: 2026Title: Particles of echovirus 18 open to release their genomes in vivo. Authors: Liya Mukhamedova / David Buchta / Zuzana Trebichalská / Yevgen Levdansky / Jana Moravcová / David Potěšil / Zbyněk Zdráhal / Dominik Hrebík / Lucie Nepovímová / Torleif Tollefsrud ...Authors: Liya Mukhamedova / David Buchta / Zuzana Trebichalská / Yevgen Levdansky / Jana Moravcová / David Potěšil / Zbyněk Zdráhal / Dominik Hrebík / Lucie Nepovímová / Torleif Tollefsrud Gjølberg / Jan Terje Andersen / Jiří Nováček / Tibor Füzik / Pavel Plevka / ![]() Abstract: Enteroviruses cause a broad spectrum of human diseases, ranging from mild respiratory or gastrointestinal infections to severe neurological disorders such as aseptic meningitis and encephalitis. ...Enteroviruses cause a broad spectrum of human diseases, ranging from mild respiratory or gastrointestinal infections to severe neurological disorders such as aseptic meningitis and encephalitis. Enterovirus cell entry involves receptor-mediated endocytosis followed by destabilizing rearrangements of the virus capsid that enable genome release. However, the mechanism of enterovirus genome release has not been visualized in infected cells. Here, we used cryoelectron tomography and microscopy to image echovirus 18 (E18) entry into host cells and its interaction with the neonatal Fc receptor (FcRn). 30 min postinfection, endosomes and cytoplasm contained empty capsids missing one or several pentamers of capsid proteins, providing evidence that in vivo E18 releases its genome through capsid opening. In vitro, FcRn binding induced the expulsion of pocket factors from hydrophobic pockets in VP1, priming the virus for uncoating. The cryoelectron microscopy reconstruction of genome-containing particles of E18 inside infected cells did not reveal pocket factors, indicating that receptor binding triggers the same priming process during infection. We did not detect activated particles in infected cells, suggesting that these intermediates are short-lived and rapidly release their genomes in vivo. Our results identify capsid opening as the in vivo mechanism of echovirus 18 genome release, providing structural evidence for a process previously only inferred from in vitro experiments. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_54510.map.gz | 31.6 MB | EMDB map data format | |
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| Header (meta data) | emd-54510-v30.xml emd-54510.xml | 17.3 KB 17.3 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_54510_fsc.xml | 8.5 KB | Display | FSC data file |
| Images | emd_54510.png | 182.9 KB | ||
| Masks | emd_54510_msk_1.map | 64 MB | Mask map | |
| Filedesc metadata | emd-54510.cif.gz | 4.8 KB | ||
| Others | emd_54510_half_map_1.map.gz emd_54510_half_map_2.map.gz | 59.4 MB 59.4 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-54510 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-54510 | 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_54510.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Main map | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 2.08047 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_54510_msk_1.map | ||||||||||||
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-Half map: Half A
| File | emd_54510_half_map_1.map | ||||||||||||
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| Annotation | Half A | ||||||||||||
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-Half map: Half B
| File | emd_54510_half_map_2.map | ||||||||||||
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| Annotation | Half B | ||||||||||||
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Sample components
-Entire : Echovirus E18
| Entire | Name: Echovirus E18 |
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| Components |
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-Supramolecule #1: Echovirus E18
| Supramolecule | Name: Echovirus E18 / type: virus / ID: 1 / Parent: 0 / NCBI-ID: 47506 / Sci species name: Echovirus E18 / Virus type: VIRION / Virus isolate: OTHER / Virus enveloped: No / Virus empty: Yes |
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| Host (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 7.9 MDa |
| Virus shell | Shell ID: 1 / Diameter: 330.0 Å |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | cell |
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Sample preparation
| Concentration | 2 mg/mL |
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| Buffer | pH: 7.4 |
| Grid | Model: Quantifoil R2/1 / Material: GOLD / Mesh: 200 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE |
| Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Specialist optics | Phase plate: OTHER |
| Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: COUNTING / Number grids imaged: 1 / Number real images: 1290 / Average exposure time: 8.0 sec. / Average electron dose: 34.0 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: 4.5 µm / Nominal defocus min: 2.5 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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About Yorodumi



Echovirus E18
Keywords
Authors
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Z (Sec.)
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Homo sapiens (human)
Processing
FIELD EMISSION GUN


