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Yorodumi- EMDB-43593: Langya Virus attachment (G) glycoprotein with K85L/L86K mutation -
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Open data
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Basic information
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| Title | Langya Virus attachment (G) glycoprotein with K85L/L86K mutation | |||||||||
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Keywords | langya / attachment / glycoprotein / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID / VIRAL PROTEIN | |||||||||
| Biological species | Langya virus | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.21 Å | |||||||||
Authors | Gibson CG / McCallum MM / Veesler DV | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: Proc Natl Acad Sci U S A / Year: 2024Title: Structure and design of Langya virus glycoprotein antigens. Authors: Zhaoqian Wang / Matthew McCallum / Lianying Yan / Cecily A Gibson / William Sharkey / Young-Jun Park / Ha V Dang / Moushimi Amaya / Ashley Person / Christopher C Broder / David Veesler / ![]() Abstract: Langya virus (LayV) is a recently discovered henipavirus (HNV), isolated from febrile patients in China. HNV entry into host cells is mediated by the attachment (G) and fusion (F) glycoproteins which ...Langya virus (LayV) is a recently discovered henipavirus (HNV), isolated from febrile patients in China. HNV entry into host cells is mediated by the attachment (G) and fusion (F) glycoproteins which are the main targets of neutralizing antibodies. We show here that the LayV F and G glycoproteins promote membrane fusion with human, mouse, and hamster target cells using a different, yet unknown, receptor than Nipah virus (NiV) and Hendra virus (HeV) and that NiV- and HeV-elicited monoclonal and polyclonal antibodies do not cross-react with LayV F and G. We determined cryoelectron microscopy structures of LayV F, in the prefusion and postfusion states, and of LayV G, revealing their conformational landscape and distinct antigenicity relative to NiV and HeV. We computationally designed stabilized LayV G constructs and demonstrate the generalizability of an HNV F prefusion-stabilization strategy. Our data will support the development of vaccines and therapeutics against LayV and closely related HNVs. | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_43593.map.gz | 307 MB | EMDB map data format | |
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| Header (meta data) | emd-43593-v30.xml emd-43593.xml | 16.7 KB 16.7 KB | Display Display | EMDB header |
| Images | emd_43593.png | 53 KB | ||
| Filedesc metadata | emd-43593.cif.gz | 5.8 KB | ||
| Others | emd_43593_additional_1.map.gz emd_43593_half_map_1.map.gz emd_43593_half_map_2.map.gz | 162 MB 301.5 MB 301.5 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-43593 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-43593 | HTTPS FTP |
-Validation report
| Summary document | emd_43593_validation.pdf.gz | 903.4 KB | Display | EMDB validaton report |
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| Full document | emd_43593_full_validation.pdf.gz | 903 KB | Display | |
| Data in XML | emd_43593_validation.xml.gz | 17 KB | Display | |
| Data in CIF | emd_43593_validation.cif.gz | 20.3 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-43593 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-43593 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8vwpMC ![]() 8tvbC ![]() 8tveC ![]() 8tvfC ![]() 8tvgC ![]() 8tvhC ![]() 8tviC M: atomic model generated by this map C: citing same article ( |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_43593.map.gz / Format: CCP4 / Size: 325 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.89 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: #1
| File | emd_43593_additional_1.map | ||||||||||||
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-Half map: #1
| File | emd_43593_half_map_1.map | ||||||||||||
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-Half map: #2
| File | emd_43593_half_map_2.map | ||||||||||||
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Sample components
-Entire : Langya virus attachment (G) protein
| Entire | Name: Langya virus attachment (G) protein |
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| Components |
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-Supramolecule #1: Langya virus attachment (G) protein
| Supramolecule | Name: Langya virus attachment (G) protein / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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| Source (natural) | Organism: Langya virus |
-Macromolecule #1: Langya virus attachment (G) protein
| Macromolecule | Name: Langya virus attachment (G) protein / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO |
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| Source (natural) | Organism: Langya virus |
| Molecular weight | Theoretical: 59.402613 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: LKAIQAMLKI IQDEVNSLKE MLVSLDQLVK TEIKPKVSLI NTAVSVSIPA QISNLQTKVL QKLVYLEESI TKQCT(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) ...String: LKAIQAMLKI IQDEVNSLKE MLVSLDQLVK TEIKPKVSLI NTAVSVSIPA QISNLQTKVL QKLVYLEESI TKQCT(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) DTTDDDKVDT TIKPVEYYKP DGCNKTNDHF TMQPGVNFYT VPNLGPSSSS ADECYTNPS FSIGSSIYMF SQEIRKTDCT TGEILSIQIV LGRIVDKGQQ GPQASPLLVW SVPNPKIINS CAVAAGDETG W VLCSVTLT AASGEPIPHM FDGFWLYKFE PDTEVVAYRI TGFAYLLDKV YDSVFIGKGG GIQRGNDLYF QMFGLSRNRQ SI KALCEHG SCL(UNK)(UNK)(UNK)(UNK)GGY QVLCDRAVMS FGSEESLISN AYLKVNDVAS GKPTIISQTF PPSDSYK GS NGRIYTIGER YGIYLAPSSW NRYLRFGLTP DISVRSTTWL KEKDPIMKVL TTCTNTDKDM CPEICNTRGY QDIFPLSE D SSFYTYIGIT PSNEGTKSFV AVKDDAGHVA SITILPNYYS ITSATISCFM YKEEIWCIAV TEGRKQKENP QRIYAHSYR VQKMCFNI |
-Macromolecule #2: 2-acetamido-2-deoxy-beta-D-glucopyranose
| Macromolecule | Name: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 2 / Number of copies: 4 / Formula: NAG |
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| Molecular weight | Theoretical: 221.208 Da |
| Chemical component information | ![]() ChemComp-NAG: |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.8 |
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| Grid | Model: UltrAuFoil / Material: GOLD |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS GLACIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 47.0 e/Å2 |
| Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.5 µm |
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Image processing
| Startup model | Type of model: OTHER / Details: CryoSPARC ab initio |
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| Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.21 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 79301 |
| Initial angle assignment | Type: PROJECTION MATCHING |
| Final angle assignment | Type: PROJECTION MATCHING |
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About Yorodumi



Keywords
Langya virus
Authors
United States, 1 items
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Homo sapiens (human)
FIELD EMISSION GUN