与PEDV结构蛋白相互作用的RNASEK可以通过克拉斯林介导的内细胞分裂促进病毒的进入
Wenzhen Qin1, Ning Kong1,2, Shengsong Xie3
1Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai, China.
Journal of virology
|January 21, 2025
概括
主体蛋白质核糖核酶卡帕 (RNASEK) 通过与病毒蛋白相互作用并促进克拉斯林介导的内细胞分裂,促进猪流行性腹病毒 (PEDV) 进入主体细胞. 这一发现为开发PEDV疫苗和疗法提供了一个新的目标.
科学领域:
- 病毒学 病毒学
- 细胞生物学 细胞生物学
- 分子机制的分子机制
背景情况:
- 猪流行性腹病毒 (PEDV) 由于小猪的高死亡率,在猪业中造成重大经济损失.
- 目前的PEDV疫苗提供了不充分的保护,病毒的宿主细胞进入机制仍然不太清楚.
- 了解PEDV的进入对于开发有效的疫苗和抗病毒剂至关重要.
研究的目的:
- 为了阐明PEDV宿主细胞进入的分子机制.
- 确定参与PEDV复制和内化的主体因素.
- 探索PEDV感染的潜在治疗点.
主要方法:
- 研究了宿主蛋白质核糖核酶卡帕 (RNASEK) 在PEDV感染中的作用.
- 在LLC-PK1细胞中使用了RNASEK的淘汰和淘汰试验.
- 分析了RNASEK与PEDV结构蛋白 (S,E,M) 和内细胞机械 (clathrin,EPS15) 的相互作用.
- 研究了RNASEK通过克拉特林介导内细胞结核 (CME) 对PEDV病毒吸收的影响.
主要成果:
- 通过转录因子USF2调节的RNASEK被确定为一种促进PEDV复制的新型宿主因子.
- RNASEK与PEDV S,E和M蛋白质结合,通过CME增强PEDV病毒内部化.
- RNASEK增加了PEDV病毒和EPS15-clathrin复合体之间的相互作用,促进病毒进入.
- 淘汰或淘汰RNASEK显著减少了PEDV内部化.
结论:
- RNASEK是PEDV的关键宿主进入因素,通过CME促进病毒内部化.
- RNASEK与多种病毒蛋白和宿主内细胞机器的相互作用是其功能的关键.
- 对于开发抗PEDV疗法和改进疫苗来说,RNASEK是一个有前途的新目标.
相关概念视频
Receptor-mediated Endocytosis
6.0K
Receptor-mediated endocytosis is when bulk amounts of specific molecules are imported into a cell after binding to cell surface receptors. The molecules bound to these receptors are taken into the cell through inward folding of the cell surface membrane, which is eventually pinched off into a vesicle within the cell. Structural proteins, such as clathrin, coat the budding vesicle.
Clathrin-Mediated Endocytosis of LDL
One well-characterized example of receptor-mediated endocytosis is the...
Clathrin-Mediated Endocytosis of LDL
One well-characterized example of receptor-mediated endocytosis is the...
6.0K
Retrovirus Life Cycles
45.6K
Retroviruses have a single-stranded RNA genome that undergoes a special form of replication. Once the retrovirus has entered the host cell, an enzyme called reverse transcriptase synthesizes double-stranded DNA from the retroviral RNA genome. This DNA copy of the genome is then integrated into the host’s genome inside the nucleus via an enzyme called integrase. Consequently, the retroviral genome is transcribed into RNA whenever the host’s genome is transcribed, allowing the...
45.6K
Pinching-off of Coated Vesicles
3.1K
Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
3.1K
Regulation of Nuclear Protein Sorting
2.4K
Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
2.4K
Coat Assembly and GTPases
3.5K
Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
3.5K
Clathrin Coated Vesicles
6.8K
Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
6.8K


