Modulation of type I interferon induction by porcine reproductive and respiratory syndrome virus and degradation of CREB-binding protein by non-structural protein 1 in MARC-145 and HeLa cells

被引:133
|
作者
Kim, Oekyung [1 ]
Sun, Yan [1 ]
Lai, Frances W. [1 ]
Song, Cheng [1 ]
Yoo, Dongwan [1 ]
机构
[1] Univ Illinois, Dept Pathobiol, Urbana, IL 61802 USA
关键词
PRRS; Non-structural protein 1; Nsp1; Arterivirus; Interferon antagonist; CREB-binding protein; CBP; EQUINE ARTERITIS VIRUS; SWINE-FEVER VIRUS; REPLICASE ORF1A PROTEIN; MESSENGER-RNA SYNTHESIS; INNATE IMMUNE-RESPONSE; REGULATORY FACTOR-3; PAPAIN-LIKE; N-PRO; COACTIVATOR CBP; TERMINAL DOMAIN;
D O I
10.1016/j.virol.2010.03.039
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Porcine reproductive and respiratory syndrome (PRRS) is an emerged disease of swine characterized by negligible response of type I IFNs and viral persistence. We show that the PRRSV non-structural protein 1 (Nsp1) is the viral component responsible for modulation of IFN response. Nsp1 blocked dsRNA-induced IRF3 and IFN promoter activities. Nsp1 did not block phosphorylation and nuclear translocation of IRF3 but inhibited IRF3 association with CREB-binding protein (CBP) in the nucleus. While IRF3 was stable, CBP was degraded, and CBP degradation was proteasome-dependent, suggesting that CBP degradation is not due to the protease activity of Nsp1 but an intermediary is involved. Our data suggest that the Nsp1-mediated CBP degradation inhibits the recruitment of CBP for enhanceosome assembly, leading to the block of IFN response. CBP degradation is a novel strategy for viral evasion from the host response, and Nsp1 may form a new class of viral antagonists for IFN modulation. (C) 2010 Elsevier Inc. All rights reserved.
引用
收藏
页码:315 / 326
页数:12
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