Nonstructural protein 1 of influenza A virus interacts with human guanylate-binding protein 1 to antagonize antiviral activity.
Nonstructural protein 1 of influenza A virus interacts with human guanylate-binding protein 1 to antagonize antiviral activity.
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甲型流感病毒非结构蛋白 1 与人鸟苷酸结合蛋白 1 相互作用，拮抗抗病毒活性
DOI：
10.1371/journal.pone.0055920
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发表时间：
2013
期刊：
影响因子：
3.7
通讯作者：
Ma Z
中科院分区：
文献类型：
--
作者：
Zhu Z;Shi Z;Yan W;Wei J;Shao D;Deng X;Wang S;Li B;Tong G;Ma Z
人鸟苷结合蛋白1 （hGBP1）是一种干扰素诱导蛋白，参与宿主对病毒感染的免疫反应。在甲型流感病毒（IAV）感染下，hGBP1转录本和蛋白显著上调。过表达hGBP1在体外以剂量依赖的方式抑制IAV复制。hGBP1的51位赖氨酸残基（K51）对抑制IAV复制至关重要。K51突变导致hGBP1无法抑制IAV复制。发现病毒非结构蛋白1 （NS1）与hGBP1直接相互作用。hGBP1的K51和NS1残基123和144之间的区域被证明是NS1和hGBP1相互作用的关键。NS1与hGBP1结合导致GTPase活性和hGBP1抗iav活性显著降低。这些发现表明，hGBP1参与了宿主对IAV复制的免疫应答，并且hGBP1介导的抗病毒活性通过与hGBP1的结合被NS1拮抗。
Human guanylate-binding protein 1 (hGBP1) is an interferon-inducible protein involved in the host immune response against viral infection. In response to infection by influenza A virus (IAV), hGBP1 transcript and protein were significantly upregulated. Overexpression of hGBP1 inhibited IAV replication in a dose-dependent manner in vitro. The lysine residue at position 51 (K51) of hGBP1 was essential for inhibition of IAV replication. Mutation of K51 resulted in an hGBP1 that was unable to inhibit IAV replication. The viral nonstructural protein 1 (NS1) was found to interact directly with hGBP1. K51 of hGBP1 and a region between residues 123 and 144 in NS1 were demonstrated to be essential for the interaction between NS1 and hGBP1. Binding of NS1 to hGBP1 resulted in a significant reduction in both GTPase activity and the anti-IAV activity of hGBP1. These findings indicated that hGBP1 contributed to the host immune response against IAV replication and that hGBP1-mediated antiviral activity was antagonized by NS1 via binding to hGBP1.
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影响因子：
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作者：
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作者：
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