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Open data
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Basic information
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Title | 2-fold block local reconstruction of SFTSV virion | |||||||||
![]() | Local reconstruction of the 2-fold block | |||||||||
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![]() | SFTSV / virion structure / Gn/Gc glycoproteins / VIRUS / VIRAL PROTEIN | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.8 Å | |||||||||
![]() | Du S / Peng R / Qi J / Li C | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM structure of severe fever with thrombocytopenia syndrome virus. Authors: Shouwen Du / Ruchao Peng / Wang Xu / Xiaoyun Qu / Yuhang Wang / Jiamin Wang / Letian Li / Mingyao Tian / Yudong Guan / Jigang Wang / Guoqing Wang / Hao Li / Lingcong Deng / Xiaoshuang Shi / ...Authors: Shouwen Du / Ruchao Peng / Wang Xu / Xiaoyun Qu / Yuhang Wang / Jiamin Wang / Letian Li / Mingyao Tian / Yudong Guan / Jigang Wang / Guoqing Wang / Hao Li / Lingcong Deng / Xiaoshuang Shi / Yidan Ma / Fengting Liu / Minhua Sun / Zhengkai Wei / Ningyi Jin / Wei Liu / Jianxun Qi / Quan Liu / Ming Liao / Chang Li / ![]() ![]() Abstract: The severe fever with thrombocytopenia syndrome virus (SFTSV) is a tick-borne human-infecting bunyavirus, which utilizes two envelope glycoproteins, Gn and Gc, to enter host cells. However, the ...The severe fever with thrombocytopenia syndrome virus (SFTSV) is a tick-borne human-infecting bunyavirus, which utilizes two envelope glycoproteins, Gn and Gc, to enter host cells. However, the structure and organization of these glycoproteins on virion surface are not yet known. Here we describe the structure of SFTSV determined by single particle reconstruction, which allows mechanistic insights into bunyavirus assembly at near-atomic resolution. The SFTSV Gn and Gc proteins exist as heterodimers and further assemble into pentameric and hexameric peplomers, shielding the Gc fusion loops by both intra- and inter-heterodimer interactions. Individual peplomers are associated mainly through the ectodomains, in which the highly conserved glycans on N914 of Gc play a crucial role. This elaborate assembly stabilizes Gc in the metastable prefusion conformation and creates some cryptic epitopes that are only accessible in the intermediate states during virus entry. These findings provide an important basis for developing vaccines and therapeutic drugs. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 30.1 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 16.7 KB 16.7 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 11.1 KB | Display | ![]() |
Images | ![]() | 108.1 KB | ||
Filedesc metadata | ![]() | 5.5 KB | ||
Others | ![]() ![]() | 88.8 MB 88.8 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1 MB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 18.6 KB | Display | |
Data in CIF | ![]() | 24.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
EMDB pages | ![]() ![]() |
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Map
File | ![]() | ||||||||||||||||||||
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Annotation | Local reconstruction of the 2-fold block | ||||||||||||||||||||
Voxel size | X=Y=Z: 1.68 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: 2-fold block half map 2
File | emd_35176_half_map_1.map | ||||||||||||
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Annotation | 2-fold block half map 2 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: 2-fold block half map 1
File | emd_35176_half_map_2.map | ||||||||||||
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Annotation | 2-fold block half map 1 | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Dabie bandavirus
Entire | Name: ![]() |
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Components |
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-Supramolecule #1: Dabie bandavirus
Supramolecule | Name: Dabie bandavirus / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 2748958 / Sci species name: Dabie bandavirus / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: Yes / Virus empty: No |
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-Macromolecule #1: Gn glycoprotein
Macromolecule | Name: Gn glycoprotein / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Sequence | String: MMKVIWFSSL ICLVIQCGGD SGPIICAGPI HSNKSANIPH LLGYSEKICQ IDRLIHVSSW LRNHSQFQGY VGQRGGRSQV SYYPAENSY SRWSGLLSPC DADWLGMLVV KKAKGSDMIV PGPSYKGKVF FERPTFDGYV GWGCSSGKSR TESGELCSSD S GTSSGLLP ...String: MMKVIWFSSL ICLVIQCGGD SGPIICAGPI HSNKSANIPH LLGYSEKICQ IDRLIHVSSW LRNHSQFQGY VGQRGGRSQV SYYPAENSY SRWSGLLSPC DADWLGMLVV KKAKGSDMIV PGPSYKGKVF FERPTFDGYV GWGCSSGKSR TESGELCSSD S GTSSGLLP SDRVLWIGDV ACQPMTPIPE ETFLELKSFS QSEFPDICKI DGVVFNQCEG ESLPQPFDVA WMDVGHSHKI IM REHKTKW VQESSSKDFV CYKAGTGPCS ESEEKTCKTS GSCRGDMQFC KVAGCEHGEE ASEAKCRCSL VHKPGEVVVS YGG MRVRPK CYGFSRMMAT LEVNPPEQRT GQCTGCHLEC INGGVRLITL TSELKSATVC ASHFCSSATS GKKSTEIQFH SGSL VGRTA IHVKGALVDG TEFTFEGSCM FPDGCDAVDC TFCREFLKNP QCYPAKKWLF IIIVILLGYA GLMLLTNVLK AIGIW GSWV IAPVKLIFAI IKKLMRTVSC LMGKLMDRGR QVIHEEIGEN REGNQDDVRI EMARPRRVRH WMYSPVILTI LAIGLA |
-Macromolecule #2: Gc glycoprotein
Macromolecule | Name: Gc glycoprotein / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Sequence | String: ESCDEMVHAD SKLVSCRQGS GNMKECVTTG RALLPAVNPG QEACLHFTAP GSPDSKCLKI KVKRINLKCK KSSSYFVPDA RSRCTSVRR CRWAGDCQSG CPPHSTSNSF SDDWAGKMDR AGLGFSGCSD GCGGAACGCF NAAPSCIFWR KWVENPHGII W KVSPCAAW ...String: ESCDEMVHAD SKLVSCRQGS GNMKECVTTG RALLPAVNPG QEACLHFTAP GSPDSKCLKI KVKRINLKCK KSSSYFVPDA RSRCTSVRR CRWAGDCQSG CPPHSTSNSF SDDWAGKMDR AGLGFSGCSD GCGGAACGCF NAAPSCIFWR KWVENPHGII W KVSPCAAW VPSAVIELTM PSGEVRTFHP MSGIPTQVFK GVSVTYLGSD MEVSGLTDLC EIEELKSKKL ALAPCNQAGM GV VGKVGEI QCSSEESART IKKDGCIWNA DLVGIELRVD DAVCYSKITS VEAVANYSAI PTTIGGLRFE RSHDSLGKIS GSP LDITAI RGSFSVNYRG LRLSLSEITA TCTGEVTNVS GCYSCMTGAK VSIKLHSSKN STAHVRCKGD ETAFSVLEGV HSYT VSLSF DHAVVDEQCQ LNCGGHESQV TLKGNLIFLD VPKFVDGSYM QTYHSSVPTG ANIPSPTDWL NALFGNGLSR WILGV IGVL LGGLALFFLI MSLFKLGTKQ VFRSRTKLA |
-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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Grid | Model: Quantifoil R2/1 / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Support film - topology: HOLEY ARRAY / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.5 µm / Nominal defocus min: 1.0 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
Refinement | Space: REAL / Protocol: FLEXIBLE FIT |
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