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运用高通量蛋白质组学方法鉴定与PRRSV NSP7结合的宿主细胞蛋白 被引量:2

Determination of the binding of non-structural protein 7 from highly pathogenic porcine reproductive and respiratory syndrome virus to host cellular proteins using high throughput proteomics
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摘要 猪繁殖与呼吸系统综合征病毒(porcine reproductive and respiratory syndrome virus,PRRSV)虽已被国内外科研工作者广泛研究,但其中一些非结构蛋白例如NSP7的结构和功能依然所知甚少,据推测此蛋白对病毒的RNA合成和蛋白翻译过程十分重要。本试验运用蛋白质组学技术偶联免疫共沉淀法,并结合生物信息学方法分析,鉴定出12种与PRRSV NSP7产生直接或间接相互作用的宿主细胞蛋白,NSP7与这些蛋白之间的互作关系能够为NSP7的深入研究提供新的途径和思路。 Porcine reproductive and respiratory syndrome virus(PRRSV) has caused tremendous e- conomic losses and continues to be a serious problem to the swine industry worldwide. Although extensive research has been focused on PRRSV, the structure and function of some viral proteins like nonstructural protein 7 (NSP7), which may play important roles in virus RNA synthesis and translation,still remain unknown. In order to better understand the function of NSP7, the interaction of NSP7 with cellular proteins was determined by using quantitative proteomics coupled with an immune-precipitation strategy. The data showed that 12 cellular proteins have a high probability to interact with NSP7-EGFP. This result will help us to better understand the character and biology of NSP7.
作者 董珊 陈红英
出处 《中国兽医学报》 CAS CSCD 北大核心 2017年第4期620-625,共6页 Chinese Journal of Veterinary Science
关键词 PRRSV NSP7 无标记蛋白组学 细胞互作 PRRSV NSP7 label free proteomics interactome
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