8TVI
Langya Virus G glycoprotein (LayV G) with stabilizing mutations
This is a non-PDB format compatible entry.
Summary for 8TVI
| Entry DOI | 10.2210/pdb8tvi/pdb |
| EMDB information | 41639 41640 41641 41642 41643 41644 |
| Descriptor | Langya virus attachment glycoprotein G, 2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION (3 entities in total) |
| Functional Keywords | layvg, layv, g protein, attachment protein, attachment glycoprotein, langya virus, protein design, protein stabilization, structural genomics, seattle structural genomics center for infectious disease, ssgcid, viral protein |
| Biological source | Langya virus |
| Total number of polymer chains | 4 |
| Total formula weight | 273351.59 |
| Authors | McCallum, M.,Veesler, D.,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2023-08-18, release date: 2024-05-01, Last modification date: 2024-10-09) |
| Primary citation | Wang, Z.,McCallum, M.,Yan, L.,Gibson, C.A.,Sharkey, W.,Park, Y.J.,Dang, H.V.,Amaya, M.,Person, A.,Broder, C.C.,Veesler, D. Structure and design of Langya virus glycoprotein antigens. Proc.Natl.Acad.Sci.USA, 121:e2314990121-e2314990121, 2024 Cited by PubMed 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 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. PubMed: 38593070DOI: 10.1073/pnas.2314990121 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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