[English] 日本語
![](img/lk-miru.gif)
- EMDB-29032: Langya Virus Fusion Protein (LayV-F) in Post-Fusion Conformation -
+
Open data
-
Basic information
Entry | ![]() | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Langya Virus Fusion Protein (LayV-F) in Post-Fusion Conformation | |||||||||
![]() | Half Map B | |||||||||
![]() |
| |||||||||
![]() | Glycoprotein / Fusion / Paramyxovirus / Henipavirus / Viral Protein | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.64 Å | |||||||||
![]() | May AJ / Pothula KR / Janowska K / Acharya P | |||||||||
Funding support | ![]()
| |||||||||
![]() | ![]() Title: Structures of Langya Virus Fusion Protein Ectodomain in Pre- and Postfusion Conformation. Authors: Aaron J May / Karunakar Reddy Pothula / Katarzyna Janowska / Priyamvada Acharya / ![]() Abstract: Langya virus (LayV) is a paramyxovirus in the genus, closely related to the deadly Nipah (NiV) and Hendra (HeV) viruses, that was identified in August 2022 through disease surveillance following ...Langya virus (LayV) is a paramyxovirus in the genus, closely related to the deadly Nipah (NiV) and Hendra (HeV) viruses, that was identified in August 2022 through disease surveillance following animal exposure in eastern China. Paramyxoviruses present two glycoproteins on their surface, known as attachment and fusion proteins, that mediate entry into cells and constitute the primary antigenic targets for immune response. Here, we determine cryo-electron microscopy (cryo-EM) structures of the uncleaved LayV fusion protein (F) ectodomain in pre- and postfusion conformations. The LayV-F protein exhibits pre- and postfusion architectures that, despite being highly conserved across paramyxoviruses, show differences in their surface properties, in particular at the apex of the prefusion trimer, that may contribute to antigenic variability. While dramatic conformational changes were visualized between the pre- and postfusion forms of the LayV-F protein, several domains remained invariant, held together by highly conserved disulfides. The LayV-F fusion peptide (FP) is buried within a highly conserved, hydrophobic interprotomer pocket in the prefusion state and is notably less flexible than the rest of the protein, highlighting its "spring-loaded" state and suggesting that the mechanism of pre-to-post transition must involve perturbations to the pocket and release of the fusion peptide. Together, these results offer a structural basis for how the Langya virus fusion protein compares to its Henipavirus relatives and propose a mechanism for the initial step of pre- to postfusion conversion that may apply more broadly to paramyxoviruses. The genus is quickly expanding into new animal hosts and geographic locations. This study compares the structure and antigenicity of the Langya virus fusion protein to other henipaviruses, which have important vaccine and therapeutic development implications. Furthermore, the study proposes a new mechanism to explain the early steps of the fusion initiation process that can be more broadly applied to the family. | |||||||||
History |
|
-
Structure visualization
Supplemental images |
---|
-
Downloads & links
-EMDB archive
Map data | ![]() | 167.9 MB | ![]() | |
---|---|---|---|---|
Header (meta data) | ![]() ![]() | 17.7 KB 17.7 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 8.5 KB | Display | ![]() |
Images | ![]() | 30.7 KB | ||
Filedesc metadata | ![]() | 5.9 KB | ||
Others | ![]() ![]() ![]() | 167.4 MB 165.1 MB 165.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
EMDB pages | ![]() ![]() |
---|
-
Map
File | ![]() | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Half Map B | ||||||||||||||||||||
Voxel size | X=Y=Z: 1.08 Å | ||||||||||||||||||||
Density |
| ||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
|
-Supplemental data
-Additional map: Supplemental map prior to final local refinement.
File | emd_29032_additional_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Supplemental map prior to final local refinement. | ||||||||||||
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: Final 3D Refinement
File | emd_29032_half_map_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Final 3D Refinement | ||||||||||||
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: Half Map A
File | emd_29032_half_map_2.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Half Map A | ||||||||||||
Projections & Slices |
| ||||||||||||
Density Histograms |
-
Sample components
-Entire : Langya Virus Fusion Protein Ectodomain Post-fusion Conformation
Entire | Name: Langya Virus Fusion Protein Ectodomain Post-fusion Conformation |
---|---|
Components |
|
-Supramolecule #1: Langya Virus Fusion Protein Ectodomain Post-fusion Conformation
Supramolecule | Name: Langya Virus Fusion Protein Ectodomain Post-fusion Conformation type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
---|---|
Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 180 KDa |
-Macromolecule #1: Fusion Protein
Macromolecule | Name: Fusion Protein / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 59.02577 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: SLHYDSLSKV GIIKGLTYNY KIKGSPSTKL MVVKLIPNID GVRNCTQKQF DEYKNLVKNV LEPVKLALNA MLDNVKSGNN KYRFAGAIM AGVALGVATA ATVTAGIALH RSNENAQAIA NMKNAIQNTN EAVKQLQLAN KQTLAVIDTI RGEINNNIIP V INQLSCDT ...String: SLHYDSLSKV GIIKGLTYNY KIKGSPSTKL MVVKLIPNID GVRNCTQKQF DEYKNLVKNV LEPVKLALNA MLDNVKSGNN KYRFAGAIM AGVALGVATA ATVTAGIALH RSNENAQAIA NMKNAIQNTN EAVKQLQLAN KQTLAVIDTI RGEINNNIIP V INQLSCDT IGLSVGIKLT QYYSEILTAF GPALQNPVNT RITIQAISSV FNRNFDELLK IMGYTSGDLY EILHSGLIRG NI IDVDVEA GYIALEIEFP NLTLVPNAVV QELMPISYNV DGDEWVTLVP RFVLTRTTLL SNIDTSRCTV TESSVICDND YAL PMSYEL IGCLQGDTSK CAREKVVSSY VPRFALSDGL VYANCLNTIC RCMDTDTPIS QSLGTTVSLL DNKKCLVYQV GDIL ISVGS YLGEGEYSAD NVELGPPVVI DKIDIGNQLA GINQTLQNAE DYIEKSEEFL KGINPSIGSG YIPEAPRDGQ AYVRK DGEW VLLSTFLGRS LEVLFQGPGH HHHHHHHSAW SHPQFEKGGG SGGGGSGGSA WSHPQFEK |
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
![]() | single particle reconstruction |
Aggregation state | particle |
-
Sample preparation
Buffer | pH: 8 |
---|---|
Grid | Model: Quantifoil R1.2/1.3 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 15 sec. |
Vitrification | Cryogen name: ETHANE |
-
Electron microscopy
Microscope | TFS KRIOS |
---|---|
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 1 / Number real images: 6179 / Average electron dose: 56.3 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 0.5 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
+
Image processing
-Atomic model buiding 1
Initial model | Chain - Source name: SwissModel / Chain - Initial model type: in silico model |
---|---|
Refinement | Space: REAL |
Output model | ![]() PDB-8fel: |