7OZR

Subtomogram average of authentic mumps virus nucleocapsid from HeLa cell lysate of long helical pitch

7OZR の概要

• エントリーDOI: 10.2210/pdb7ozr/pdb
• EMDBエントリー: 13133
• 分子名称: Nucleocapsid, RNA (5'-R(P*UP*UP*UP*UP*UP*U)-3') (2 entities in total)
• 機能のキーワード: helical filament, nucleocapsid, protein-rna complex, scaffold, virus
• 由来する生物種: Mumps virus genotype A; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 63108.77

構造登録者

Mahamid, J.,Zhang, X. (登録日: 2021-06-28, 公開日: 2023-03-01, 最終更新日: 2024-03-13)

主引用文献

Zhang, X.,Sridharan, S.,Zagoriy, I.,Eugster Oegema, C.,Ching, C.,Pflaesterer, T.,Fung, H.K.H.,Becher, I.,Poser, I.,Muller, C.W.,Hyman, A.A.,Savitski, M.M.,Mahamid, J.
Molecular mechanisms of stress-induced reactivation in mumps virus condensates.
Cell, 186:1877-1894.e27, 2023

PubMed Abstract: Negative-stranded RNA viruses can establish long-term persistent infection in the form of large intracellular inclusions in the human host and cause chronic diseases. Here, we uncover how cellular stress disrupts the metastable host-virus equilibrium in persistent infection and induces viral replication in a culture model of mumps virus. Using a combination of cell biology, whole-cell proteomics, and cryo-electron tomography, we show that persistent viral replication factories are dynamic condensates and identify the largely disordered viral phosphoprotein as a driver of their assembly. Upon stress, increased phosphorylation of the phosphoprotein at its interaction interface with the viral polymerase coincides with the formation of a stable replication complex. By obtaining atomic models for the authentic mumps virus nucleocapsid, we elucidate a concomitant conformational change that exposes the viral genome to its replication machinery. These events constitute a stress-mediated switch within viral condensates that provide an environment to support upregulation of viral replication.

PubMed: 37116470
DOI: 10.1016/j.cell.2023.03.015

実験手法

ELECTRON MICROSCOPY (4.5 Å)