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首页> 外文期刊>Virology >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.
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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.

机译：猪生殖和呼吸综合征病毒对I型干扰素诱导的调节以及非结构蛋白1在MARC-145和HeLa细胞中对CREB结合蛋白的降解。

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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.
机译：猪繁殖与呼吸综合症（PRRS）是一种新兴的猪疾病，其特征在于I型IFN的反应可忽略不计和病毒持续存在。我们显示PRRSV非结构蛋白1（Nsp1）是负责IFN反应调节的病毒成分。 Nsp1阻止dsRNA诱导的IRF3和IFN启动子活性。 Nsp1不会阻止IRF3的磷酸化和核易位，但会抑制IRF3与CREB结合蛋白（CBP）在细胞核中的缔合。虽然IRF3稳定，但CBP降解，并且CBP降解是蛋白酶体依赖性的，这表明CBP降解不是由于Nsp1的蛋白酶活性引起的，而是一种中介作用。我们的数据表明，Nsp1介导的CBP降解抑制CBP募集用于增强体装配，从而导致IFN反应的阻滞。 CBP降解是一种从宿主反应中逃逸病毒的新策略，Nsp1可能会形成一类新的针对IFN调节的病毒拮抗剂。

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