8OP2

Stacks of nucleocapsid rings of the N1-370 mutant of the human Respiratory Syncytial Virus

8OP2 の概要

• エントリーDOI: 10.2210/pdb8op2/pdb
• EMDBエントリー: 17030 17031 17034 17035 17036 17037 17038
• 分子名称: Nucleoprotein, RNA (70-mer) (2 entities in total)
• 機能のキーワード: n-rna, nucleoprotein, nucleocapsid, rsv, viral protein
• 由来する生物種: Human respiratory syncytial virus A strain Long; 詳細
• タンパク質・核酸の鎖数: 22
• 化学式量合計: 864960.63

構造登録者

Gonnin, L.,Desfosses, A.,Gutsche, I. (登録日: 2023-04-06, 公開日: 2023-09-27, 最終更新日: 2025-07-02)

主引用文献

Gonnin, L.,Desfosses, A.,Bacia-Verloop, M.,Chevret, D.,Galloux, M.,Eleouet, J.F.,Gutsche, I.
Structural landscape of the respiratory syncytial virus nucleocapsids.
Nat Commun, 14:5732-5732, 2023

PubMed Abstract: Human Respiratory Syncytial Virus (HRSV) is a prevalent cause of severe respiratory infections in children and the elderly. The helical HRSV nucleocapsid is a template for the viral RNA synthesis and a scaffold for the virion assembly. This cryo-electron microscopy analysis reveals the non-canonical arrangement of the HRSV nucleocapsid helix, composed of 16 nucleoproteins per asymmetric unit, and the resulting systematic variations in the RNA accessibility. We demonstrate that this unique helical symmetry originates from longitudinal interactions by the C-terminal arm of the HRSV nucleoprotein. We explore the polymorphism of the nucleocapsid-like assemblies, report five structures of the full-length particles and two alternative arrangements formed by a C-terminally truncated nucleoprotein mutant, and demonstrate the functional importance of the identified longitudinal interfaces. We put all these findings in the context of the HRSV RNA synthesis machinery and delineate the structural basis for its further investigation.

PubMed: 37714861
DOI: 10.1038/s41467-023-41439-8

実験手法

ELECTRON MICROSCOPY (2.8 Å)