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- EMDB-49636: SARS-CoV-2 nsp1 bound to the Rhinolophus lepidus 40S ribosome (lo... -
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Open data
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Basic information
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Title | SARS-CoV-2 nsp1 bound to the Rhinolophus lepidus 40S ribosome (local refinement of the 40S head) | |||||||||
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![]() | SARS-CoV-2 / RIBOSOME / Seattle Structural Genomics Center for Infectious Disease / SSGCID | |||||||||
Biological species | ![]() ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.1 Å | |||||||||
![]() | Gen R / Seattle Structural Genomics Center for Infectious Disease (SSGCID) / Veesler D | |||||||||
Funding support | ![]()
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![]() | ![]() Title: SARS-CoV-2 nsp1 mediates broad inhibition of translation in mammals. Authors: Risako Gen / Amin Addetia / Daniel Asarnow / Young-Jun Park / Joel Quispe / Matthew C Chan / Jack T Brown / Jimin Lee / Melody G Campbell / Christopher P Lapointe / David Veesler / ![]() Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) non-structural protein 1 (nsp1) promotes innate immune evasion by inhibiting host translation in human cells. However, the role of nsp1 in ...Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) non-structural protein 1 (nsp1) promotes innate immune evasion by inhibiting host translation in human cells. However, the role of nsp1 in other host species remains elusive, especially in bats-natural reservoirs of sarbecoviruses with a markedly different innate immune system than humans. We reveal that nsp1 potently inhibits translation in Rhinolophus lepidus bat cells, which belong to the same genus as known sarbecovirus reservoir hosts. We determined a cryoelectron microscopy structure of nsp1 bound to the R. lepidus 40S ribosomal subunit, showing that it blocks the mRNA entry channel by targeting a highly conserved site among mammals. Accordingly, we found that nsp1 blocked protein translation in mammalian cells from several species, underscoring its broadly inhibitory activity and conserved role in numerous SARS-CoV-2 hosts. Our findings illuminate the arms race between coronaviruses and mammalian host immunity, providing a foundation for understanding the determinants of viral maintenance in bat hosts and spillover. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 257.9 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 36 KB 36 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 16.8 KB | Display | ![]() |
Images | ![]() | 42.1 KB | ||
Filedesc metadata | ![]() | 9.2 KB | ||
Others | ![]() ![]() ![]() | 483.3 MB 474.9 MB 474.9 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 940.6 KB | Display | ![]() |
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Full document | ![]() | 940.2 KB | Display | |
Data in XML | ![]() | 26.3 KB | Display | |
Data in CIF | ![]() | 34.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
EMDB pages | ![]() ![]() |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.829 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: #1
File | emd_49636_additional_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_49636_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_49636_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
+Entire : SARS-CoV-2 nsp1-Rhinolophus lepidus ribosome complex, head map
+Supramolecule #1: SARS-CoV-2 nsp1-Rhinolophus lepidus ribosome complex, head map
+Supramolecule #3: SARS-CoV-2 nsp1
+Supramolecule #4: Eukaryotic translation initiation factor 1
+Supramolecule #2: Rhinolophus lepidus ribosome
+Macromolecule #1: 40S ribosomal protein uS3, RPS3
+Macromolecule #2: 40S ribosomal protein eS10, RPS10
+Macromolecule #3: 40S ribosomal protein eS12, RPS12
+Macromolecule #4: 40S ribosomal protein uS19, RPS15
+Macromolecule #5: 40S ribosomal protein uS9, RPS16
+Macromolecule #6: 40S ribosomal protein eS17, RPS17
+Macromolecule #7: 40S ribosomal protein uS13, RPS18
+Macromolecule #8: 40S ribosomal protein eS19, RPS19
+Macromolecule #9: 40S ribosomal protein uS10, RPS20
+Macromolecule #10: 40S ribosomal protein eS25, RPS25
+Macromolecule #11: 40S ribosomal protein eS31, RPS27a
+Macromolecule #12: 40S ribosomal protein eS28, RPS28
+Macromolecule #13: 40S ribosomal protein uS14, RPS29
+Macromolecule #15: 40S ribosomal protein uS7, RPS5
+Macromolecule #16: RACK1
+Macromolecule #14: 18S ribosomal RNA
+Macromolecule #17: MAGNESIUM ION
+Macromolecule #18: ZINC ION
+Macromolecule #19: POTASSIUM ION
+Macromolecule #20: water
-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 | TFS KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 30.7 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.6 µm / Nominal defocus min: 0.6 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |