Decapping protein 1 phosphorylation modulates IL-8 expression during respiratory syncytial virus infection.
Decapping protein 1 phosphorylation modulates IL-8 expression during respiratory syncytial virus infection.
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DOI：
10.1016/j.virol.2015.02.043
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发表时间：
2015-07
期刊：
影响因子：
3.7
通讯作者：
Fearns, Rachel
中科院分区：
文献类型：
--
作者：
Dickey, Laura L.;Duncan, Julie K.;Hanley, Timothy M.;Fearns, Rachel
呼吸道合胞病毒（RSV）是一种负链RNA病毒，是毛细支气管炎和肺炎的重要原因。我们研究了RSV感染对参与调节mRNA翻译和降解的细胞蛋白质表达模式的影响，发现参与mRNA降解的加工体蛋白脱帽蛋白1a（DCP 1）在感染后迅速磷酸化。UV灭活和蔗糖纯化的RSV足以介导DCP 1磷酸化，表明它是RSV感染早期事件的结果。使用激酶抑制剂的分析表明，RSV诱导的DCP 1磷酸化通过ERK 1/2途径发生。DCP 1磷酸化位点仅限于丝氨酸315、丝氨酸319和苏氨酸321。过表达野生型DCP 1导致RSV诱导的IL-8产生减少，但这种作用在过表达磷酸化缺陷型DCP 1突变体的细胞中被废除。这些结果表明，DCP 1磷酸化调节宿主趋化因子对RSV感染的反应。
Respiratory syncytial virus (RSV) is a negative-strand RNA virus that is an important cause of bronchiolitis and pneumonia. We investigated the effect of RSV infection on the expression patterns of cellular proteins involved in regulating mRNA translation and degradation, and found that a processing-body protein involved in mRNA degradation, decapping protein 1a (DCP1), was phosphorylated rapidly following infection. UV-inactivated and sucrose-purified RSV were sufficient to mediate DCP1 phosphorylation, indicating that it occurs as a consequence of an early event in RSV infection. Analysis using kinase inhibitors showed that RSV-induced DCP1 phosphorylation occurred through the ERK1/2 pathway. The DCP1 phosphorylation sites were limited to serine 315, serine 319, and threonine 321. Overexpression of wt DCP1 led to a decrease in RSV-induced IL-8 production, but this effect was abrogated in cells overexpressing phosphorylation-deficient DCP1 mutants. These results suggest that DCP1 phosphorylation modulates the host chemokine response to RSV infection.
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