8VWP

Langya Virus attachment (G) glycoprotein with K85L/L86K mutation

8VWP の概要

• エントリーDOI: 10.2210/pdb8vwp/pdb
• EMDBエントリー: 43593
• 分子名称: Langya virus attachment (G) protein, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• 機能のキーワード: langya, attachment, glycoprotein, structural genomics, seattle structural genomics center for infectious disease, ssgcid, viral protein
• 由来する生物種: Langya virus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 238495.28

構造登録者

Gibson, C.G.,McCallum, M.M.,Veesler, D.V.,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2024-02-02, 公開日: 2024-05-01, 最終更新日: 2024-10-30)

主引用文献

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

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

実験手法

ELECTRON MICROSCOPY (3.21 Å)