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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Mojiang virus F ectodomain in prefusion form | |||||||||
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![]() | F ectodomain / prefusion / VIRAL PROTEIN | |||||||||
Function / homology | Precursor fusion glycoprotein F0, Paramyxoviridae / Fusion glycoprotein F0 / fusion of virus membrane with host plasma membrane / viral envelope / host cell plasma membrane / virion membrane / plasma membrane / Fusion glycoprotein F0![]() | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.66 Å | |||||||||
![]() | Low YS / Isaacs A / Modhiran N / Watterson D | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure and antigenicity of divergent Henipavirus fusion glycoproteins. Authors: Ariel Isaacs / Yu Shang Low / Kyle L Macauslane / Joy Seitanidou / Cassandra L Pegg / Stacey T M Cheung / Benjamin Liang / Connor A P Scott / Michael J Landsberg / Benjamin L Schulz / Keith ...Authors: Ariel Isaacs / Yu Shang Low / Kyle L Macauslane / Joy Seitanidou / Cassandra L Pegg / Stacey T M Cheung / Benjamin Liang / Connor A P Scott / Michael J Landsberg / Benjamin L Schulz / Keith J Chappell / Naphak Modhiran / Daniel Watterson / ![]() Abstract: In August 2022, a novel henipavirus (HNV) named Langya virus (LayV) was isolated from patients with severe pneumonic disease in China. This virus is closely related to Mòjiāng virus (MojV), and ...In August 2022, a novel henipavirus (HNV) named Langya virus (LayV) was isolated from patients with severe pneumonic disease in China. This virus is closely related to Mòjiāng virus (MojV), and both are divergent from the bat-borne HNV members, Nipah (NiV) and Hendra (HeV) viruses. The spillover of LayV is the first instance of a HNV zoonosis to humans outside of NiV and HeV, highlighting the continuing threat this genus poses to human health. In this work, we determine the prefusion structures of MojV and LayV F proteins via cryogenic electron microscopy to 2.66 and 3.37 Å, respectively. We show that despite sequence divergence from NiV, the F proteins adopt an overall similar structure but are antigenically distinct as they do not react to known antibodies or sera. Glycoproteomic analysis revealed that while LayV F is less glycosylated than NiV F, it contains a glycan that shields a site of vulnerability previously identified for NiV. These findings explain the distinct antigenic profile of LayV and MojV F, despite the extent to which they are otherwise structurally similar to NiV. Our results carry implications for broad-spectrum HNV vaccines and therapeutics, and indicate an antigenic, yet not structural, divergence from prototypical HNVs. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
Map data | ![]() | 32.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 19.4 KB 19.4 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 7.6 KB | Display | ![]() |
Images | ![]() | 38.3 KB | ||
Masks | ![]() | 64 MB | ![]() | |
Others | ![]() ![]() ![]() | 59.6 MB 59.5 MB 59.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 942.9 KB | Display | ![]() |
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Full document | ![]() | 942.4 KB | Display | |
Data in XML | ![]() | 15.1 KB | Display | |
Data in CIF | ![]() | 20.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8fmyMC ![]() 8fmxC C: citing same article ( M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Voxel size | X=Y=Z: 1 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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-Additional map: #1
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-Half map: #1
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-Half map: #2
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Density Histograms |
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Sample components
-Entire : Mojiang virus F glycoprotein ectodomain in the prefusion form
Entire | Name: Mojiang virus F glycoprotein ectodomain in the prefusion form |
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Components |
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-Supramolecule #1: Mojiang virus F glycoprotein ectodomain in the prefusion form
Supramolecule | Name: Mojiang virus F glycoprotein ectodomain in the prefusion form type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 200 KDa |
-Macromolecule #1: Fusion glycoprotein F0
Macromolecule | Name: Fusion glycoprotein F0 / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 52.636922 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MALNKNMFSS LFLGYLLVYA TTVQSSIHYD SLSKVGVIKG LTYNYKIKGS PSTKLMVVKL IPNIDSVKNC TQKQYDEYKN LVRKALEPV KMAIDTMLNN VKSGNNKYRF AGAIMAGVAL GVATAATVTA GIALHRSNEN AQAIANMKSA IQNTNEAVKQ L QLANKQTL ...String: MALNKNMFSS LFLGYLLVYA TTVQSSIHYD SLSKVGVIKG LTYNYKIKGS PSTKLMVVKL IPNIDSVKNC TQKQYDEYKN LVRKALEPV KMAIDTMLNN VKSGNNKYRF AGAIMAGVAL GVATAATVTA GIALHRSNEN AQAIANMKSA IQNTNEAVKQ L QLANKQTL AVIDTIRGEI NNNIIPVINQ LSCDTIGLSV GIRLTQYYSE IITAFGPALQ NPVNTRITIQ AISSVFNGNF DE LLKIMGY TSGDLYEILH SELIRGNIID VDVDAGYIAL EIEFPNLTLV PNAVVQELMP ISYNIDGDEW VTLVPRFVLT RTT LLSNID TSRCTITDSS VICDNDYALP MSHELIGCLQ GDTSKCAREK VVSSYVPKFA LSDGLVYANC LNTICRCMDT DTPI SQSLG ATVSLLDNKR CSVYQVGDVL ISVGSYLGDG EYNADNVELG PPIVIDKIDI GNQLAGINQT LQEAEDYIEK SEEFL KG |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 0.7 mg/mL |
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Buffer | pH: 6.8 |
Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE / Instrument: LEICA EM GP |
Details | 0.255% CHAPS added |
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Electron microscopy
Microscope | JEOL CRYO ARM 300 |
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Specialist optics | Energy filter - Name: In-column Omega Filter / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 40.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 25.0 µm / Nominal defocus min: 5.0 µm / Nominal magnification: 100000 |
Sample stage | Specimen holder model: JEOL CRYOSPECPORTER / Cooling holder cryogen: NITROGEN |
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Image processing
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: FLEXIBLE FIT / Overall B value: 102.7 |
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Output model | ![]() PDB-8fmy: |