Seneca Valley virus 3C(pro) degrades heterogeneous nuclear ribonucleoprotein A1 to facilitate viral replication.
Seneca Valley virus 3C(pro) degrades heterogeneous nuclear ribonucleoprotein A1 to facilitate viral replication.
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Seneca Valley病毒3C（pro）降解异质核核糖核蛋白A1以促进病毒复制。
DOI：
10.1080/21505594.2021.2014681
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发表时间：
2021-12
期刊：
影响因子：
5.2
通讯作者：
Liu J
中科院分区：
文献类型：
--
作者：
Song J;Wang D;Quan R;Liu J
塞内卡谷病毒（SVV）是最近发现的一种与猪特发性水疱病密切相关的重要病原体。SVV感染已被证明可诱导多种细胞因子，其激活对病毒复制至关重要，但异质核核糖核蛋白A1 （hnRNP A1）是否参与SVV复制尚不清楚。hnRNP A1的细胞质再分布被认为在病毒生命周期中起重要作用。在这里，我们证明了SVV感染可以促进核胞质穿梭rna结合蛋白hnRNP A1从细胞核重新分布到细胞质中，而hnRNP A1主要留在模拟感染细胞的细胞核中。sirna介导的敲低编码hnRNP A1的基因减弱了病毒的复制，这可以通过降低病毒蛋白表达和病毒产生来证明，而其过表达则增强了复制。此外，SVV感染诱导了hnRNP A1的降解，并且发现病毒3c蛋白酶（3cpro）负责其降解和易位。进一步的研究表明，3cpro通过蛋白酶活性，通过蛋白酶体途径诱导hnRNP A1降解。这种降解可以通过蛋白酶体抑制剂（MG132）和3cpro中保守催化盒的失活来减弱。综上所述，这些结果表明SVV 3c蛋白酶靶向细胞hnRNP A1的降解和易位，SVV利用其来帮助病毒复制，从而突出了SVV感染策略的控制潜力。
Seneca Valley virus (SVV) is a recently-identified important pathogen that is closely related to idiopathic vesicular disease in swine. Infection of SVV has been shown to induce a variety of cellular factors and their activations are essential for viral replication, but whether heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) involved in SVV replication is unknown. The cytoplasmic redistribution of hnRNP A1 is considered to play an important role in the virus life cycle. Here, we demonstrated that SVV infection can promote redistribution of the nucleocytoplasmic shuttling RNA-binding protein hnRNP A1 to the cytoplasm from the nucleus, whereas hnRNP A1 remained mainly in the nucleus of mock-infected cells. siRNA-mediated knockdown of the gene encoding hnRNP A1 attenuated viral replication as evidenced by decreased viral protein expression and virus production, whereas its overexpression enhanced replication. Moreover, infection with SVV induced the degradation of hnRNP A1, and viral 3 C protease (3 Cpro) was found to be responsible for its degradation and translocation. Further studies demonstrated that 3 Cpro induced hnRNP A1 degradation through its protease activity, via the proteasome pathway. This degradation could be attenuated by a proteasome inhibitor (MG132) and inactivation of the conserved catalytic box in 3 Cpro. Taken together, these results presented here reveal that SVV 3 C protease targets cellular hnRNP A1 for its degradation and translocation, which is utilized by SVV to aid viral replication, thereby highlighting the control potential of strategies for infection of SVV.
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影响因子：
5.4
作者：
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通讯作者：
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影响因子：
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作者：
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14.9
作者：
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通讯作者：
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影响因子：
5.4
作者：
Lin, Jing-Yi;Shih, Shin-Ru;Li, Mei-Ling
通讯作者：
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DOI：
10.1007/978-0-387-77374-2_8
发表时间：
2007-01-01
期刊：
ALTERNATIVE SPLICING IN THE POSTGENOMIC ERA
影响因子：
--
作者：
Martinez-Contreras, Rebeca;Cloutier, Philippe;Chabot, Benoit
通讯作者：
Chabot, Benoit