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

文献类型： 外文期刊

第一作者： Shi, Xibao

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

作者机构：

关键词： Porcine reproductive and respiratory syndrome virus (PRRSV);Nonstructural protein 1 alpha;Interferon-beta

期刊名称：CELLULAR IMMUNOLOGY （ 影响因子：4.868； 五年影响因子：4.706 ）

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收录情况： SCI

摘要： 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. (C) 2012 Published by Elsevier Inc.

分类号： Q2

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