低病毒诱导的CpIre1酸化调节了Cryphonectria parasitica中的未折叠蛋白质反应和病毒性
Lijiu Zhao1,2, Feng Wang1, Fengyue Chen1
1State Key Laboratory for Conservation and Utilization of Subtropical Agro-Bioresources, College of Life Science and Technology, Guangxi University, Nanning, China.
Molecular plant pathology
|February 16, 2026
概括
Cryphonectria parasitica hypovirus 1 (CHV1) 感染改变了真菌蛋白质的酸化,特别是 CpIre1.1. 这种酸化对真菌特征,应激反应和有效的病毒复制至关重要,揭示了宿主重编程机制.
科学领域:
- 菌类学 菌类学是指菌类学.
- 病毒学 病毒学
- 分子生物学分子生物学
背景情况:
- 栗子病菌Cryphonectria parasitica及其下病毒 (CHV1) 为研究真菌病原和病毒与宿主相互作用提供了一个模型.
- 了解病毒如何操纵宿主细胞功能,如蛋白质酸化,是破译感染机制的关键.
研究的目的:
- 调查Cryphonectria低病毒1 (CHV1) 在C. parasitica.中调节蛋白质酸化中的作用.
- 为了确定特定的宿主蛋白和酸化位,这些位是CHV1.1的目标.
- 阐明这些修改对真菌生物学和病毒复制的影响.
主要方法:
- 野生型和CHV1感染的C.寄生虫菌株之间的比较基蛋白质分析.
- 西方斑点分析以确认蛋白质酸化.
- 在CpIre1.1.上确定酸化位点的特定位点突变发生.
- 反转录定量PCR (RT-qPCR) 用于评估基因表达和病毒RNA水平.
主要成果:
- 鉴定了700多个不同的化部位,在CHV1感染时有174个上调和526个下调.
- 在Ser-896和Ser-897中,内质网膜 (ER) 压力感应蛋白CpIre1的酸化受到CHV1编码蛋白 (p29,p40,p48) 的显著影响.
- 化CpIre1对于真菌特征,毒性,耐压力,ER稳定性和有效的CHV1复制至关重要,缺乏突变体显示病毒RNA积累受损.
结论:
- 感染CHV1诱导了C.寄生虫的蛋白质组的显著变化,特别是针对CpIre1.1.
- 病毒蛋白对CpIre1的酸化对于调节真菌ER应激反应,致病性和宿主病毒相互作用至关重要.
- 这项研究揭示了CHV1通过针对性CpIre1的翻译后修改对宿主重编程的新机制,影响了真菌和病毒生物学.
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