Physical interaction between bovine viral diarrhea virus nonstructural protein 4A and adenosine deaminase acting on RNA (ADAR).
Physical interaction between bovine viral diarrhea virus nonstructural protein 4A and adenosine deaminase acting on RNA (ADAR).
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牛病毒性腹泻病毒非结构蛋白 4A 和作用于 RNA (ADAR) 的腺苷脱氨酶之间的物理相互作用。
DOI：
10.1007/s00705-014-1997-3
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发表时间：
2014
期刊：
影响因子：
--
通讯作者：
et al.
中科院分区：
文献类型：
--
作者：
Mohamed YM; Horimoto T;et al.
牛病毒性腹泻病毒（BVDV）是一种正义RNA病毒，已知在细胞质复制过程中产生双链RNA （dsRNA）。扩展的dsRNA双链可以通过作用于RNA的腺苷脱氨酶（ADAR）进行超编辑，该酶催化腺苷(A)到肌苷(I)的编辑。已经报道了针对各种病毒的A-to-I编辑。dsRNA刺激了许多细胞抗病毒防御策略，这可能涉及到ADARs对dsRNA的超编辑，然后是细胞质内切酶的靶向切割。在此，我们在体内鉴定出ADAR是BVDV ns4in vitroandin的结合伙伴，并证明NS4A的n端结构域是ADAR结合结构域。我们还发现，当ADAR在BVDV感染的牛细胞中过表达时，它对BVDV复制有抑制作用。我们的研究结果表明NS4A在BVDV与ADAR的相互作用中起着促进病毒复制的作用。
Bovine viral diarrhea virus (BVDV) is a positive-sense RNA virus known to produce double-stranded RNA (dsRNA) during its replication in the cytoplasm. Extended dsRNA duplexes can be hyperedited by adenosine deaminase acting on RNA (ADAR), which catalyzes adenosine (A)-to-inosine (I) editing. A-to-I editing has been reported for various viruses. A number of cellular antiviral defense strategies are stimulated by dsRNA, and this may involve hyperediting of dsRNA by ADARs, followed by targeted cleavage by cytoplasmic endonucleases. Here, we identify ADAR as a binding partner of BVDV NS4Ain vitroandin vivoand show that the N-terminal domain of NS4A is the ADAR-binding domain. We also show that ADAR has an inhibitory effect on BVDV replication when overexpressed in BVDV-infected bovine cells. Our findings suggest a role of NS4A in the interaction of BVDV with ADAR that favors virus replication.