8ZDW

The cryoEM structure of H5N1 HA split from symmetric filament in conformation A

8ZDW の概要

• エントリーDOI: 10.2210/pdb8zdw/pdb
• EMDBエントリー: 60015
• 分子名称: Hemagglutinin, H5M9 Fab, light chain, Anti-H5N1 hemagglutinin monoclonal anitbody H5M9 heavy chain, ... (8 entities in total)
• 機能のキーワード: influenza, glycosylation, sialic acid, viral protein/immune system, viral protein-immune system complex
• 由来する生物種: Influenza A virus (strain A/Vietnam/1203/2004 H5N1); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 345800.44

構造登録者

Li, R.,Gao, J.,Wang, L.,Gui, M.,Xiang, Y. (登録日: 2024-05-03, 公開日: 2024-09-25, 最終更新日: 2025-05-14)

主引用文献

Li, R.,Gao, J.,Wang, L.,Gui, M.,Xiang, Y.
Multivalent interactions between fully glycosylated influenza virus hemagglutinins mediated by glycans at distinct N-glycosylation sites.
Npj Viruses, 2:48-48, 2024

PubMed Abstract: The hemagglutinin (HA) glycoprotein of influenza virus binds host cell receptors and mediates viral entry. Here we present cryo-EM structures of fully glycosylated HAs from H5N1 and H5N8 influenza viruses. We find that the H5N1 HA can form filaments that comprise two head-to-head HA trimers. Multivalent interactions between the two HA trimers are mediated by glycans attached to N158. The distal Sia1-Gal2-NAG3 sugar moiety of N158 interacts with the receptor binding site on the opposing HA trimer. Additional interactions are observed between NAG3 and residues K222 and K193. The H5N8 HA lacks the N158 glycosylation site and does not form the filamentous structure. However, the H5N8 HA exhibits an auto-inhibition conformation, where the receptor binding site is occupied by the glycan chain attached to residue N169 from a neighboring protomer. These structures represent native HA-glycan interactions, which may closely mimic the receptor-HA interactions on the cell surface.

PubMed: 40295773
DOI: 10.1038/s44298-024-00059-9

実験手法

ELECTRON MICROSCOPY (3.45 Å)