Human polyomavirus JC small regulatory agnoprotein forms highly stable dimers and oligomers: implications for their roles in agnoprotein function.

Human polyomavirus JC small regulatory agnoprotein forms highly stable dimers and oligomers: implications for their roles in agnoprotein function.
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DOI:
10.1016/j.virol.2011.08.015
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发表时间:
2011-11-10
期刊:
影响因子:
3.7
通讯作者:
Safak M
Safak M
中科院分区:
医学3区
文献类型:
--
作者:
Saribas AS;Arachea BT;White MK;Viola RE;Safak M

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JC病毒(JCV)编码一种来自编码后期区域的小的碱性磷蛋白,称为agnoprotein,该蛋白在病毒复制周期中起重要的调节作用。在这项研究中,我们报告了agno蛋白形成高度稳定的二聚体和高阶低聚物复合物。免疫印迹和质谱研究证实了这一点。这些配合物对强变性剂(包括尿素和SDS)具有极强的抵抗力。蛋白质的中心部分,从17到42的氨基酸对二聚体/低聚物的形成很重要。从病毒背景中去除17 ~ 42aa区严重影响了JCV的复制效率。jcv感染细胞提取液在体内表现为agnoprotein双带型。总的来说,这些发现表明,agno蛋白形成功能活跃的同型二聚体/低聚物复合物,这些复合物可能对其在病毒传播过程中的功能和PML的进展很重要。
JC virus (JCV) encodes a small basic phosphoprotein from the late coding region called agnoprotein, which has been shown to play important regulatory roles in the viral replication cycle. In this study, we report that agnoprotein forms highly stable dimers and higher order oligomer complexes. This was confirmed by immunoblotting and mass spectrometry studies. These complexes are extremely resistant to strong denaturing agents, including urea and SDS. Central portion of the protein, amino acids spanning from 17 to 42 is important for dimer/oligomer formation. Removal of 17 to 42 aa region from the viral background severely affected the efficiency of the JCV replication. Extracts prepared from JCV-infected cells showed a double banding pattern for agnoprotein in vivo. Collectively, these findings suggest that agnoprotein forms functionally active homodimer/oligomer complexes and these may be important for its function during viral propagation and thus for the progression of PML.
DOI: 10.1126/science.2832944
发表时间: 1988-04-01
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