Human parainfluenza virus type 2 V protein inhibits and antagonizes tetherin.
Human parainfluenza virus type 2 V protein inhibits and antagonizes tetherin.
复制标题
人副流感病毒2型V蛋白抑制并拮抗tetherin。
DOI：
10.1099/jgv.0.000373
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发表时间：
2016
期刊：
影响因子：
3.8
通讯作者：
Nishio M
中科院分区：
文献类型：
--
作者：
Ohta K;Goto H;Yumine N;Nishio M
Tetherin(BST-2/CD317/HM1.24)是一种抗病毒膜蛋白，可阻止被包裹的病毒从细胞表面释放。我们发现Tetherin对人副流感病毒2型(hPIV-2)的生长有抑制作用，但对V蛋白缺陷型重组hPIV-2的生长无抑制作用。V蛋白与Tetherin发生免疫共沉淀，这种相互作用需要其C末端的Trp残基。与V蛋白结合所必需的是Tetherin的糖基磷脂酰肌醇附着信号，而不是细胞质中的尾巴。当与tetherin共表达时，V蛋白的分布发生了明显变化。HPIV-2感染HeLa细胞使细胞表面粘连蛋白减少，但不影响细胞总粘连蛋白。这种减少也发生在结构性表达V的HeLa细胞中，而突变的V蛋白不影响细胞表面的锚链。我们的结果表明，hPIV-2V蛋白通过与Tetherin结合并减少其在细胞表面的存在而拮抗Tetherin。
Tetherin (BST-2/CD317/HM1.24) is an antiviral membrane protein that prevents the release of enveloped viruses from the cell surface. We found that the growth of human parainfluenza virus type 2 (hPIV-2), but not that of V protein-deficient recombinant hPIV-2, was inhibited by tetherin. V protein immunoprecipitates with tetherin, and this interaction requires its C-terminal Trp residues. The glycosyl phosphatidylinositol attachment signal of tetherin, but not its cytoplasmic tail, was necessary for its binding with V. The distribution of the V protein clearly changed when co-expressed with tetherin in plasmid-transfected cells. hPIV-2 infection of HeLa cells reduced cell surface tetherin without affecting total cellular tetherin. This reduction also occurred in HeLa cells constitutively expressing V, whereas mutated V protein did not affect the cell surface tetherin. Our results suggest that hPIV-2 V protein antagonizes tetherin by binding it and reducing its presence at the cell surface.