7TXZ

Nipah Virus attachment (G) glycoprotein ectodomain in complex with nAH1.3 neutralizing antibody Fab fragment (local refinement of the distal region)

7TXZ の概要

• エントリーDOI: 10.2210/pdb7txz/pdb
• EMDBエントリー: 26162
• 分子名称: Glycoprotein G, nAH1.3 Fab heavy chain, nAH1.3 Fab light chain, ... (6 entities in total)
• 機能のキーワード: niv, nivg, attachment protein, neutralizing antibodies, structural genomics, seattle structural genomics center for infectious disease, ssgcid, viral protein
• 由来する生物種: Nipah henipavirus; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 396647.67

構造登録者

Wang, Z.Q.,Seattle Structural Genomics Center for Infectious Disease (SSGCID),Veesler, D. (登録日: 2022-02-10, 公開日: 2022-03-09, 最終更新日: 2024-10-09)

主引用文献

Wang, Z.,Amaya, M.,Addetia, A.,Dang, H.V.,Reggiano, G.,Yan, L.,Hickey, A.C.,DiMaio, F.,Broder, C.C.,Veesler, D.
Architecture and antigenicity of the Nipah virus attachment glycoprotein.
Science, 375:1373-1378, 2022

PubMed Abstract: Nipah virus (NiV) and Hendra virus (HeV) are zoonotic henipaviruses (HNVs) responsible for outbreaks of encephalitis and respiratory illness. The entry of HNVs into host cells requires the attachment (G) and fusion (F) glycoproteins, which are the main targets of antibody responses. To understand viral infection and host immunity, we determined a cryo-electron microscopy structure of the NiV G homotetrameric ectodomain in complex with the nAH1.3 broadly neutralizing antibody Fab fragment. We show that a cocktail of two nonoverlapping G-specific antibodies neutralizes NiV and HeV synergistically and limits the emergence of escape mutants. Analysis of polyclonal serum antibody responses elicited by vaccination of macaques with NiV G indicates that the receptor binding head domain is immunodominant. These results pave the way for implementing multipronged therapeutic strategies against these deadly pathogens.

PubMed: 35239409
DOI: 10.1126/science.abm5561

実験手法

ELECTRON MICROSCOPY (3.2 Å)