PLP2, a potent deubiquitinase from murine hepatitis virus, strongly inhibits cellular type I interferon production.
PLP2, a potent deubiquitinase from murine hepatitis virus, strongly inhibits cellular type I interferon production.
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PLP2是一种来自鼠肝炎病毒的有效去泛素酶，强烈抑制了I型干扰素的产生。
DOI：
10.1038/cr.2008.294
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发表时间：
2008-11
期刊：
影响因子：
44.1
通讯作者：
Tang H
中科院分区：
文献类型：
--
作者：
Zheng D;Chen G;Guo B;Cheng G;Tang H
Infections by coronaviruses such as severe acute respiratory syndrome (SARS) coronavirus (SCoV) and mouse hepatitis virus A59 (MHV-A59) result in very little type I interferon (IFN) production by host cells, which is potentially responsible for the rapid viral growth and severe immunopathology associated with SARS. However, the molecular mechanisms for the low IFN production in cells infected with coronaviruses remain unclear. Here, we provide evidence that Papain-like protease domain 2 (PLP2), a catalytic domain of the nonstructural protein 3 (nsp3) of MHV-A59, can bind to IRF3, cause its deubiquitination and prevent its nuclear translocation. As a consequence, co-expression of PLP2 strongly inhibits CARDIF-, TBK1- and IRF3-mediated IFNβ reporter activities. In addition, we show that wild-type PLP2 but not the mutant PLP2 lacking the deubiquitinase (DUB) activity can reduce IFN induction and promote viral growth in cells infected with VSV. Thus, our study uncovered a viral DUB which coronaviruses may use to escape from the host innate antiviral responses. The online version of this article (doi:10.1038/cr.2008.294) contains supplementary material, which is available to authorized users.
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