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Yorodumi- EMDB-41644: Langya henipavirus postfusion fusion protein in complex with 4G5 ... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-41644 | |||||||||
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Title | Langya henipavirus postfusion fusion protein in complex with 4G5 Fab (global refinement) | |||||||||
Map data | ||||||||||
Sample |
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Keywords | Langya / henipavirus / fusion protein / postfusion / LayVF / SSGCID / VIRAL PROTEIN | |||||||||
Biological species | Langya virus / Mus sp. (mice) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
Authors | Wang Z / Veesler D | |||||||||
Funding support | United States, 1 items
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Citation | Journal: Proc Natl Acad Sci U S A / Year: 2024 Title: 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. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_41644.map.gz | 399 MB | EMDB map data format | |
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Header (meta data) | emd-41644-v30.xml emd-41644.xml | 18.4 KB 18.4 KB | Display Display | EMDB header |
Images | emd_41644.png | 50.7 KB | ||
Filedesc metadata | emd-41644.cif.gz | 5.4 KB | ||
Others | emd_41644_additional_1.map.gz emd_41644_half_map_1.map.gz emd_41644_half_map_2.map.gz | 211.3 MB 392.1 MB 392.1 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-41644 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-41644 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_41644.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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Voxel size | X=Y=Z: 0.9835 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: Unsharpened
File | emd_41644_additional_1.map | ||||||||||||
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Annotation | Unsharpened | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_41644_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_41644_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Langya henipavirus postfusion fusion protein in complex with 4G5 Fab
Entire | Name: Langya henipavirus postfusion fusion protein in complex with 4G5 Fab |
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Components |
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-Supramolecule #1: Langya henipavirus postfusion fusion protein in complex with 4G5 Fab
Supramolecule | Name: Langya henipavirus postfusion fusion protein in complex with 4G5 Fab type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Langya virus |
-Macromolecule #1: Langya henipavirus fusion protein in postfusion state
Macromolecule | Name: Langya henipavirus fusion protein in postfusion state / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Langya virus |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: MAFLKSAIIC YLLFYPHIVK SSLHYDSLSK VGIIKGLTYN YKIKGSPSTK LMVVKLIPNI DGVRNCTQKQ FDEYKNLVKN VLEPVKLALN AMLDNVKSGN NKYRFAGAIM AGVALGVATA ATVTAGIALH RSNENAQAIA NMKNAIQNTN EAVKQLQLAN KQTLAVIDTI ...String: MAFLKSAIIC YLLFYPHIVK SSLHYDSLSK VGIIKGLTYN YKIKGSPSTK LMVVKLIPNI DGVRNCTQKQ FDEYKNLVKN VLEPVKLALN AMLDNVKSGN NKYRFAGAIM AGVALGVATA ATVTAGIALH RSNENAQAIA NMKNAIQNTN EAVKQLQLAN KQTLAVIDTI RGEINNNIIP VINQLSCDTI GLSVGIKLTQ YYSEILTAFG PALQNPVNTR ITIQAISSVF NRNFDELLKI MGYTSGDLYE ILHSGLIRGN IIDVDVEAGY IALEIEFPNL TLVPNAVVQE LMPISYNVDG DEWVTLVPRF VLTRTTLLSN IDTSRCTVTE SSVICDNDYA LPMSYELIGC LQGDTSKCAR EKVVSSYVPR FALSDGLVYA NCLNTICRCM DTDTPISQSL GTTVSLLDNK KCLVYQVGDI LISVGSYLGE GEYSADNVEL GPPVVIDKID IGNQLAGINQ TLQNAEDYIE KSEEFLKGIN PSMKQIEDKI EEILSKIYHI ENEIARIKKL IGEAPGGSIE GRGSGGGSHH HHHH |
-Macromolecule #2: 4G5 Fab heavy chain variable domain
Macromolecule | Name: 4G5 Fab heavy chain variable domain / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Mus sp. (mice) |
Sequence | String: EVQLQQSGAD LVKPGASVKL SCTASGFNIK DTYIHWVKQR PEQGLEWIGR IDPANDNFKY DPKFQGKATI TTDTSSNTAY LQLSSLTSED TAVYYCASVI TTTGYALDYW GQGTSVTVSS |
-Macromolecule #3: 4G5 Fab light chain variable domain
Macromolecule | Name: 4G5 Fab light chain variable domain / type: protein_or_peptide / ID: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: Mus sp. (mice) |
Sequence | String: DIQMTQSPAS LSASVGETVT ITCRASGNIH NYLAWYQQKQ GKSPQLLVYS AKTLADGVPS RFSGSGSGTQ YSLKINSLQP EDFGSYYCQH FWSSPRTFGG GTKLEIK |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 24 K / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | TFS KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 1.7 µm / Nominal defocus min: 1.3 µm |
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 63.0 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: OTHER |
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Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |
Final reconstruction | Applied symmetry - Point group: C3 (3 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 60440 |