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- EMDB-42197: Eastern equine encephalitis virus (PE-6) VLP in complex with VLDL... -
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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Eastern equine encephalitis virus (PE-6) VLP in complex with VLDLR LA(1-6)[W132A, W210A] (icosahedral) | |||||||||
![]() | EEEV PE-6 VLP in complex with VLDLR LA(1-6) W132A, W210A icosahedral reconstruction | |||||||||
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![]() | virus / receptor / VIRUS LIKE PARTICLE | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.05 Å | |||||||||
![]() | Adams LJ / Fremont DH | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural and functional basis of VLDLR usage by Eastern equine encephalitis virus. Authors: Lucas J Adams / Saravanan Raju / Hongming Ma / Theron Gilliland / Douglas S Reed / William B Klimstra / Daved H Fremont / Michael S Diamond / ![]() Abstract: The very-low-density lipoprotein receptor (VLDLR) comprises eight LDLR type A (LA) domains and supports entry of distantly related alphaviruses, including Eastern equine encephalitis virus (EEEV) and ...The very-low-density lipoprotein receptor (VLDLR) comprises eight LDLR type A (LA) domains and supports entry of distantly related alphaviruses, including Eastern equine encephalitis virus (EEEV) and Semliki Forest virus (SFV). Here, by resolving multiple cryo-electron microscopy structures of EEEV-VLDLR complexes and performing mutagenesis and functional studies, we show that EEEV uses multiple sites (E1/E2 cleft and E2 A domain) to engage more than one LA domain simultaneously. However, no single LA domain is necessary or sufficient to support efficient EEEV infection. Whereas all EEEV strains show conservation of two VLDLR-binding sites, the EEEV PE-6 strain and a few other EEE complex members feature a single amino acid substitution that enables binding of LA domains to an additional site on the E2 B domain. These structural and functional analyses informed the design of a minimal VLDLR decoy receptor that neutralizes EEEV infection and protects mice from lethal challenge. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 1.3 GB | ![]() | |
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Header (meta data) | ![]() ![]() | 14.2 KB 14.2 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 25.2 KB | Display | ![]() |
Images | ![]() | 52.7 KB | ||
Filedesc metadata | ![]() | 3.9 KB | ||
Others | ![]() ![]() ![]() | 711.6 MB 1.3 GB 1.3 GB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
EMDB pages | ![]() ![]() |
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Map
File | ![]() | ||||||||||||||||||||
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Annotation | EEEV PE-6 VLP in complex with VLDLR LA(1-6) W132A, W210A icosahedral reconstruction | ||||||||||||||||||||
Voxel size | X=Y=Z: 1.081 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: EEEV PE-6 VLP in complex with VLDLR LA(1-6)...
File | emd_42197_additional_1.map | ||||||||||||
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Annotation | EEEV PE-6 VLP in complex with VLDLR LA(1-6) W132A, W210A icosahedral reconstruction (unsharpened map) | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: EEEV PE-6 VLP in complex with VLDLR LA(1-6)...
File | emd_42197_half_map_1.map | ||||||||||||
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Annotation | EEEV PE-6 VLP in complex with VLDLR LA(1-6) W132A, W210A icosahedral reconstruction (half map A) | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: EEEV PE-6 VLP in complex with VLDLR LA(1-6)...
File | emd_42197_half_map_2.map | ||||||||||||
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Annotation | EEEV PE-6 VLP in complex with VLDLR LA(1-6) W132A, W210A icosahedral reconstruction (half map B) | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Eastern equine encephalitis virus
Entire | Name: ![]() ![]() |
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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 / NCBI-ID: 11021 / Sci species name: Eastern equine encephalitis virus / Sci species strain: PE-6 / Virus type: VIRUS-LIKE PARTICLE / Virus isolate: STRAIN / Virus enveloped: Yes / Virus empty: Yes |
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-Experimental details
-Structure determination
Method | cryo EM |
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![]() | 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 | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 44.4 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.2 µm / Nominal defocus min: 0.7000000000000001 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |