[English] 日本語
Yorodumi- EMDB-15956: Tomogram of an extracellular EBOV particle adjacent to an EBOV-in... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-15956 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Tomogram of an extracellular EBOV particle adjacent to an EBOV-infected Huh7 cell | |||||||||
Map data | Tomogram of an extracellular EBOV particle adjacent to an EBOV-infected Huh7 cell | |||||||||
Sample |
| |||||||||
Keywords | Ebola virus / neutral pH / VIRUS | |||||||||
Biological species | Ebola virus - Mayinga, Zaire, 1976 | |||||||||
Method | electron tomography / cryo EM | |||||||||
Authors | Winter SL / Chlanda P | |||||||||
Funding support | Germany, 1 items
| |||||||||
Citation | Journal: EMBO J / Year: 2023 Title: The Ebola virus VP40 matrix layer undergoes endosomal disassembly essential for membrane fusion. Authors: Sophie L Winter / Gonen Golani / Fabio Lolicato / Melina Vallbracht / Keerthihan Thiyagarajah / Samy Sid Ahmed / Christian Lüchtenborg / Oliver T Fackler / Britta Brügger / Thomas Hoenen / ...Authors: Sophie L Winter / Gonen Golani / Fabio Lolicato / Melina Vallbracht / Keerthihan Thiyagarajah / Samy Sid Ahmed / Christian Lüchtenborg / Oliver T Fackler / Britta Brügger / Thomas Hoenen / Walter Nickel / Ulrich S Schwarz / Petr Chlanda / Abstract: Ebola viruses (EBOVs) assemble into filamentous virions, whose shape and stability are determined by the matrix viral protein 40 (VP40). Virus entry into host cells occurs via membrane fusion in late ...Ebola viruses (EBOVs) assemble into filamentous virions, whose shape and stability are determined by the matrix viral protein 40 (VP40). Virus entry into host cells occurs via membrane fusion in late endosomes; however, the mechanism of how the remarkably long virions undergo uncoating, including virion disassembly and nucleocapsid release into the cytosol, remains unknown. Here, we investigate the structural architecture of EBOVs entering host cells and discover that the VP40 matrix disassembles prior to membrane fusion. We reveal that VP40 disassembly is caused by the weakening of VP40-lipid interactions driven by low endosomal pH that equilibrates passively across the viral envelope without a dedicated ion channel. We further show that viral membrane fusion depends on VP40 matrix integrity, and its disassembly reduces the energy barrier for fusion stalk formation. Thus, pH-driven structural remodeling of the VP40 matrix acts as a molecular switch coupling viral matrix uncoating to membrane fusion during EBOV entry. | |||||||||
History |
|
-Structure visualization
Supplemental images |
---|
-Downloads & links
-EMDB archive
Map data | emd_15956.map.gz | 373.5 MB | EMDB map data format | |
---|---|---|---|---|
Header (meta data) | emd-15956-v30.xml emd-15956.xml | 9 KB 9 KB | Display Display | EMDB header |
Images | emd_15956.png | 143.7 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-15956 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-15956 | HTTPS FTP |
-Validation report
Summary document | emd_15956_validation.pdf.gz | 417.1 KB | Display | EMDB validaton report |
---|---|---|---|---|
Full document | emd_15956_full_validation.pdf.gz | 416.7 KB | Display | |
Data in XML | emd_15956_validation.xml.gz | 5 KB | Display | |
Data in CIF | emd_15956_validation.cif.gz | 6.1 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-15956 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-15956 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
---|
-Map
File | Download / File: emd_15956.map.gz / Format: CCP4 / Size: 507 MB / Type: IMAGE STORED AS SIGNED BYTE | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Tomogram of an extracellular EBOV particle adjacent to an EBOV-infected Huh7 cell | ||||||||||||||||||||
Voxel size | X=Y=Z: 8.013 Å | ||||||||||||||||||||
Density |
| ||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
|
-Supplemental data
-Sample components
-Entire : Ebola virus - Mayinga, Zaire, 1976
Entire | Name: Ebola virus - Mayinga, Zaire, 1976 |
---|---|
Components |
|
-Supramolecule #1: Ebola virus - Mayinga, Zaire, 1976
Supramolecule | Name: Ebola virus - Mayinga, Zaire, 1976 / type: virus / ID: 1 / Parent: 0 / NCBI-ID: 128952 / Sci species name: Ebola virus - Mayinga, Zaire, 1976 / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: Yes / Virus empty: No |
---|
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
Processing | electron tomography |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 |
---|---|
Vitrification | Cryogen name: ETHANE |
Sectioning | Focused ion beam - Instrument: OTHER / Focused ion beam - Ion: OTHER / Focused ion beam - Voltage: 30 / Focused ion beam - Current: 0.3 / Focused ion beam - Duration: 600 / Focused ion beam - Temperature: 100 K / Focused ion beam - Initial thickness: 6000 / Focused ion beam - Final thickness: 150 Focused ion beam - Details: The value given for _em_focused_ion_beam.instrument is Aquilos FIB-SEM. This is not in a list of allowed values {'DB235', 'OTHER'} so OTHER is written into the XML file. |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 3.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 4.0 µm / Nominal defocus min: 4.0 µm / Nominal magnification: 33000 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Final reconstruction | Software - Name: IMOD / Number images used: 41 |
---|