Real-time SPR characterization of the interactions between multi-epitope proteins and antibodies against classical swine fever virus

文献类型： 外文期刊

第一作者： Tian, Hong

作者： Tian, Hong;Hou, Xiangming;Liu, Xiangtao

作者机构：

关键词： Antigen-antibody interaction;Binding affinity and binding kinetics;BT22 and BT23 multi-epitope combination;Classical swine fever virus;Surface plasmon resonance

期刊名称：BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS （ 影响因子：3.575； 五年影响因子：3.381 ）

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收录情况： SCI

摘要： The envelope glycoprotein E2 is the major immunodominant protein of the classical swine fever virus and can induce neutralizing antibodies and protective host-immune responses in infected swine. We designed, expressed, and purified multi-epitope protein (GST-BT22) that contains a tandem repeat of the E2 antigenic-determinant residues 693-704, 770-780, and 826-843, each of which is separated by a GGSSGG sequence. In the same manner, we also designed, expressed, and purified a second protein (GST-BT23) that contains a C-terminal sequence consisting of residues 1446-1460 from the classical swine fever virus nonstructural protein NS2-3 separated from the GST-BT22 sequence by a GGSSGG sequence. Western blotting of GST-BT22 and GST-BT23 with serum from a swine that had been experimentally infected with the virus showed that the proteins reacted with anti-serum, whereas GST did not. Surface plasmon resonance was used to quantify the affinities of GST-BT22 and GST-BT23 for serum antibodies (Ka=4.31??108 and 5.01??108, respectively). GST, used as a control, was reacted an order of magnitude less strongly than did GST-BT22 and GST-BT23. Surface plasmon resonance, therefore, appears to be a sensitive and precise method for epitope evaluation and can be used to characterize the immunogenicity of a recombinant protein. ? 2013 Elsevier Inc.

分类号： Q5

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