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8TVE

Langya henipavirus fusion protein in postfusion state

Summary for 8TVE
Entry DOI10.2210/pdb8tve/pdb
EMDB information41639 41640 41641 41642 41643 41644
DescriptorLangya henipavirus fusion protein in postfusion state, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
Functional Keywordslangya, henipavirus, fusion protein, postfusion, layvf, ssgcid, viral protein, structural genomics, seattle structural genomics center for infectious disease
Biological sourceLangya virus
Total number of polymer chains3
Total formula weight176769.68
Authors
Wang, Z.,Seattle Structural Genomics Center for Infectious Disease (SSGCID),Veesler, D. (deposition date: 2023-08-18, release date: 2024-05-08, Last modification date: 2024-10-30)
Primary citationWang, 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: 38593070
DOI: 10.1073/pnas.2314990121
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.9 Å)
Structure validation

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