Amino acid at position 176 was essential for porcine reproductive and respiratory syndrome virus (PRRSV) non-structural protein 1 alpha (nsp1 alpha) as an inhibitor to the induction of IFN-beta

作者：Shi, Xibao; Chen, Jing; Xing, Guangxu; Zhang, Xiaozhuan; Hu, Xiaofei; Zhi, Yubao; Guo, Junqing; Wang, Li; Qiao, Songlin; Lu, Qingxia; Zhang, Gaiping^*

来源：Cellular Immunology, 2012, 280(2): 125-131.

DOI：10.1016/j.cellimm.2012.10.003

• Porcine reproductive and respiratory syndrome virus (PRRSV)
• Nonstructural protein 1 alpha
• Interferon-beta

Previous studies have shown that porcine reproductive and respiratory syndrome virus (PRRSV) non-structural protein 1 alpha (nsp1 alpha) was the interferon (IFN) antagonist. However, the mechanism was unclear. In the present study, deletion of the carboxyl-terminal extension (CTE) (167-180 amino acid (aa)) made nsp1 alpha lose its inhibitory ability to the induction of IFN-beta. And a series of C-terminal truncated mutants for nsp1 alpha showed that 1-176 aa of nsp1 alpha was able to inhibit the induction of IFN-beta and deleting or mutating the amino acid F176 made nsp1 alpha not inhibit the induction of IFN-beta. In conclusion, the CTE and the amino acid F176 were critical for nsp1 alpha as the IFN antagonist and the region representing 167-176 was the minimal subunit of the CTE for nsp1 alpha to retain its suppressive activity to the induction of IFN-beta.

• 出版日期2012-12
• 单位河南省农业科学院; 河南农业大学; 河南省科学院化学研究所