来自人类冠状病毒的核体蛋白具有相分离能力,并促进FUS病理聚合
Hui Dong1, Hong Zhang1, Julie Jalin1
1School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, China.
Protein science : a publication of the Protein Society
|October 31, 2023
概括
冠状病毒的核体 (N) 蛋白具有相同的液体-液体相分离 (LLPS) 能力. 这些N蛋白还可以促进宿主蛋白的病态聚合,在病毒感染期间影响细胞健康.
科学领域:
- 病毒学 病毒学
- 分子生物学分子生物学
- 生物化学 生物化学
背景情况:
- 核体 (N) 蛋白对于像SARS-CoV-2和MERS-CoV这样的人类冠状病毒 (HCoV) 至关重要,有助于基因组包装和复制.
- 最近的研究强调了SARS-CoV-2 N蛋白质显著的液体-液体相分离 (LLPS) 能力,涉及到病毒感染和复制过程.
研究的目的:
- 系统地研究来自不同HCoV的七种同源N蛋白的LLPS能力.
- 探索这些N蛋白与宿主因子的相互作用,特别是FUS,以及它们对细胞过程的影响.
主要方法:
- 使用高通量蛋白相分离试验来评估LLPS.
- 为了分析相互作用,进行了与FUS的同相分离试验和结合研究.
主要成果:
- 确定LLPS是被研究的HCoV N蛋白共享的内在性质.
- 在不同的体外条件下,在N蛋白质同类体中观察到不同的相分离概况.
- 发现N种蛋白质同类物与FUS共相分离,加速其过渡到固态和粉样蛋白聚合.
- 证明了N蛋白同类物与FUS低复杂性域的直接结合.
结论:
- 来自各种HCoV的N蛋白质本质上具有相分离能力.
- 这些LLPS特性可能会导致压力颗粒恒温的破坏,并在HCoV感染期间促进宿主细胞中的病态蛋白质聚合.
- 这些发现表明,HCoV N蛋白与宿主因子相互作用的保存机制,可能有助于疾病的发病.
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