Henan Provincial Key Laboratory of Animal Immunology, Henan Academy of Agricultural Sciences, Zhengzhou 450002, China.
Mol Immunol. 2011 Jul;48(12-13):1568-72. doi: 10.1016/j.molimm.2011.03.004. Epub 2011 Apr 9.
Previous studies have shown that PRRSV nsp11, which was an endoribonuclease, was an interferon antagonist, however, the mechanism that nsp11 inhibited IFN-β production was unclear. To explore whether the endoribonuclease was required for nsp11 to disrupt the IFN-β production, substitutions of the presumed catalytic histidine and lysine residues of nsp11 were introduced into plasmid pcDNA 3.1-FLAG. The results showed that mutation that inactivated endoribonuclease made nsp11 lose its ability to inhibit Poly(I:C)-induced IFN-β promoter activity. In conclusion, our present work indicated that the endoribonuclease activity of nsp11 was essential for nsp11 to inhibit the IFN-β induction.
先前的研究表明,作为一种内切核酸酶的 PRRSV nsp11 是一种干扰素拮抗剂,然而,nsp11 抑制 IFN-β 产生的机制尚不清楚。为了探究内切核酸酶是否是 nsp11 破坏 IFN-β 产生所必需的,将假定的催化组氨酸和赖氨酸残基的取代物引入质粒 pcDNA 3.1-FLAG。结果表明,使内切核酸酶失活的突变使 nsp11 丧失抑制 Poly(I:C)诱导的 IFN-β 启动子活性的能力。总之,我们的工作表明,nsp11 的内切核酸酶活性对于 nsp11 抑制 IFN-β 的诱导是必不可少的。