Blocking the dengue virus 2 infections on BHK-21 cells with purified recombinant dengue virus 2 E protein expressed in Escherichia coli
Blocking the dengue virus 2 infections on BHK-21 cells with purified recombinant dengue virus 2 E protein expressed in Escherichia coli
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DOI：
10.1016/j.bbrc.2003.08.053
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发表时间：
2003-09-26
影响因子：
3.1
通讯作者：
Yang, YL
中科院分区：
文献类型：
--
作者：
Chiu, MW;Yang, YL
登革病毒(DV)是由蚊子传播的传染病病原体。它们已经成为热带和亚热带地区日益严重的公共卫生问题。登革热包膜蛋白(E)是病毒结构蛋白之一，主要负责病毒附着和进入宿主细胞。它也是病毒中和的主要免疫原。在本研究中，我们构建了表达DV-2病毒PL046株截短的E蛋白的重组载体：去掉E蛋白的C端疏水结构域，代之以S肽序列，以便于表达和纯化。在大肠杆菌中表达时，重组E蛋白呈聚集态。通过变性和透析过程，纯化的重组E蛋白保持了与受体相互作用的功能，这表明它能够抑制哺乳动物BHK-21宿主细胞上DV-2空斑的形成。(C)2003 Elsevier Inc.保留所有权利。
Dengue viruses (DVs) are mosquito-borne infectious pathogens. They have become an expanding public health problem in the tropics and subtropics. The dengue envelope (E) protein is one of the viral structure proteins responsible mainly for the virus attachment and entry onto host cells. It is also the major immunogen for virus neutralization. In this study, we have constructed a recombinant plasmid expressing a truncated E protein of DV-2 virus PL046 strain: The C-terminal hydrophobic domain of the E protein was removed and replaced with the sequence of S peptide to facilitate expression and purification. When expressed in Escherichia coli, the recombinant E proteins were found to be in the form of aggregated state. Through denaturation and dialysis processes, the receptor-interacting function of the purified recombinant E proteins was maintained, which was demonstrated by its ability to inhibit the DV-2 plaque-forming efficiency on mammalian BHK-21 host cells. (C) 2003 Elsevier Inc. All rights reserved.