The V protein of human parainfluenza virus 2 antagonizes type 1 interferon responses by destabilizing signal transducer and activator of transcription 2
The V protein of human parainfluenza virus 2 antagonizes type 1 interferon responses by destabilizing signal transducer and activator of transcription 2
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DOI：
10.1006/viro.2001.0856
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发表时间：
2001-05-10
期刊：
影响因子：
3.7
通讯作者：
Horvath, CM
中科院分区：
文献类型：
--
作者：
Parisien, JP;Lau, JF;Horvath, CM
I型干扰素（IFN）通过包含亚基蛋白Stat1，STAT2和P48 /ISGF3 Gamma /irf9的ISGF3转录因子复合物的激活诱导抗病毒反应。已经检查了某些人类丙糖病毒通过特异性蛋白质水解克服IFN作用的能力。用2型的细胞感染，但没有1型或3型人类副粉状病毒（HPIV）导致细胞STAT2蛋白的丧失。在没有其他病毒蛋白的情况下，源自V开放式阅读框的单个HPIV2蛋白的表达会阻止IFN依赖性转录反应。 IFN反应的丢失是由于V蛋白诱导的STAT2蛋白水解降解引起的。 HPIV2 V的表达导致正常稳定的STAP2蛋白迅速降解，并且该蛋白水解活性可以通过蛋白酶体抑制作用部分缓解。未观察到对STAT2 mRNA水平的V蛋白特异性作用。结果表明，HPIV2的V蛋白足以识别并靶向特定的细胞转录因子，以通过细胞机械破坏。 （c）2001学术出版社。
Type I interferon (IFN) induces antiviral responses through the activation of the ISGF3 transcription factor complex that contains the subunit proteins STAT1, STAT2, and p48/ISGF3 gamma /IRF9. The ability of some human paramyxoviruses to overcome IFN actions by specific proteolysis of STAT proteins has been examined. Infection of cells with type 2, but not type 1 or type 3 human parainfluenza virus (HPIV) leads to a loss of cellular STAT2 protein. Expression of a single HPIV2 protein derived from the V open reading frame blocks IFN-dependent transcriptional responses in the absence of other viral proteins. The loss of IFN response is due to V-protein-induced proteolytic degradation of STAT2. Expression of HPIV2 V causes the normally stable STAT2 protein to be rapidly degraded, and this proteolytic activity can be partially alleviated by proteasome inhibition. No V-protein-specific effects on STAT2 mRNA levels were observed. The results indicate that the V protein of HPIV2 is sufficient to recognize and target a specific cellular transcription factor for destruction by cellular machinery. (C) 2001 Academic Press.