The non-structural 3 (NS3) protein of dengue virus type 2 interacts with human nuclear receptor binding protein and is associated with alterations in membrane structure
The non-structural 3 (NS3) protein of dengue virus type 2 interacts with human nuclear receptor binding protein and is associated with alterations in membrane structure
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DOI：
10.1016/j.virusres.2004.01.025
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发表时间：
2004-06-15
期刊：
影响因子：
5
通讯作者：
Chow, VTK
中科院分区：
文献类型：
--
作者：
Chua, JJE;Ng, MML;Chow, VTK
黄病毒感染产生与黄病毒复制机制相关的一系列不同的病毒诱导的细胞内膜改变。目前，仍不清楚哪种黄病毒蛋白负责这种诱导。使用酵母双杂交和免疫共沉淀分析，我们证明了登革病毒2型的NS 3蛋白特异性地与核受体结合蛋白（NRBP）相互作用，NRBP是一种影响内质网（ER）和高尔基体之间运输的宿主细胞蛋白，并且与Rho-GTdR家族的成员Rac 3相互作用。NS 3和NRBP在幼仓鼠肾细胞中的共表达显示出显著的亚细胞共定位，并揭示了NRBP从细胞质到核周区域的重新分布。此外，一组膜结构隶属于粗糙ER在核周区域诱导与NS 3转染细胞。这些结构让人想起以前在黄病毒感染的细胞中观察到的病毒诱导的卷曲膜。登革病毒和宿主细胞蛋白之间的这种相互作用以及NS 3诱导的膜结构的形成表明NS 3可能颠覆NRBP在ER-高尔基体运输中的作用。(C)2004 Elsevier B. V.保留所有权利。
Flaviviral infections produce a distinct array of virus-induced intracellular membrane alterations that are associated with the flaviviral replication machinery. Currently, it is still unknown which flaviviral protein(s) is/are responsible for this induction. Using yeast two-hybrid and co-immunoprecipitation analyses, we demonstrated that the NS3 protein of dengue virus type 2 interacted specifically with nuclear receptor binding protein (NRBP), a host cellular protein that influences trafficking between the endoplasmic reticulum (ER) and Golgi, and that interacts with Rac3, a member of the Rho-GTPase family. Co-expression of NS3 and NRBP in baby hamster kidney cells exhibited significant subcellular co-localization, and revealed the redistribution of NRBP from the cytoplasm to the perinuclear region. Furthermore, a set of membrane structures affiliated with the rough ER at the perinuclear region was induced in cells transfected with NS3. These structures are reminiscent of the virus-induced convoluted membranes previously observed in flavivirus-infected cells. This interaction between dengue viral and host cell proteins as well as the formation of the NS3-induced membrane structures suggest that NS3 may subvert the role of NRBP in ER-Golgi trafficking. (C) 2004 Elsevier B.V. All rights reserved.