7YR8

Lloviu cuevavirus nucleoprotein(1-450 residues)-RNA complex

7YR8 の概要

• エントリーDOI: 10.2210/pdb7yr8/pdb
• EMDBエントリー: 34049
• 分子名称: Nucleoprotein, RNA (5'-R(P*UP*UP*UP*UP*UP*U)-3') (2 entities in total)
• 機能のキーワード: nucleoprotein, viral protein
• 由来する生物種: Lloviu cuevavirus; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 44989.63

構造登録者

Hu, S.F.,Fujita-Fujiharu, Y.,Sugita, Y.,Wendt, L.,Muramoto, Y.,Nakano, M.,Hoenen, T.,Noda, T. (登録日: 2022-08-09, 公開日: 2023-04-19, 最終更新日: 2024-07-03)

主引用文献

Hu, S.,Fujita-Fujiharu, Y.,Sugita, Y.,Wendt, L.,Muramoto, Y.,Nakano, M.,Hoenen, T.,Noda, T.
Cryoelectron microscopic structure of the nucleoprotein-RNA complex of the European filovirus, Lloviu virus.
Pnas Nexus, 2:pgad120-pgad120, 2023

PubMed Abstract: Lloviu virus (LLOV) is a novel filovirus detected in Schreiber's bats in Europe. The isolation of the infectious LLOV from bats has raised public health concerns. However, the virological and molecular characteristics of LLOV remain largely unknown. The nucleoprotein (NP) of LLOV encapsidates the viral genomic RNA to form a helical NP-RNA complex, which acts as a scaffold for nucleocapsid formation and de novo viral RNA synthesis. In this study, using single-particle cryoelectron microscopy, we determined two structures of the LLOV NP-RNA helical complex, comprising a full-length and a C-terminally truncated NP. The two helical structures were identical, demonstrating that the N-terminal region determines the helical arrangement of the NP. The LLOV NP-RNA protomers displayed a structure similar to that in the Ebola and Marburg virus, but the spatial arrangements in the helix differed. Structure-based mutational analysis identified amino acids involved in the helical assembly and viral RNA synthesis. These structures advance our understanding of the filovirus nucleocapsid formation and provide a structural basis for the development of antifiloviral therapeutics.

PubMed: 37124400
DOI: 10.1093/pnasnexus/pgad120

実験手法

ELECTRON MICROSCOPY (3.2 Å)