Mason P W, Zügel M U, Semproni A R, Fournier M J, Mason T L
Yale Arbovirus Research Unit, Yale University School of Medicine, New Haven, Connecticut 06510.
J Gen Virol. 1990 Sep;71 ( Pt 9):2107-14. doi: 10.1099/0022-1317-71-9-2107.
The antigenic structures of the envelope protein, E, and the non-structural protein, NS1, of dengue type 1 virus (DEN1) have been studied in the form of recombinant fusion proteins expressed in Escherichia coli. Deletion analysis was used to identify two distinct antigenic domains in E that reacted with subsets of antiviral monoclonal antibodies (MAbs). Domain I of E extends from amino acid residues (aa) 76 to 93 of E; domain II extends from aa 293 to 402 and contains an essential disulphide bridge. MAbs also reacted with several determinants clustered near the N terminus of the NS1 protein (aa 57 to 126). Recombinant fusion proteins containing E. coli trpE sequences and most of the sequences for either E or NS1 were immunogenic in mice. The antibodies elicited by the E fusion protein reacted with a portion of the protein containing domain II, whereas antibodies elicited by the NS1 fusion protein did not react with the antigenic determinants defined by our MAbs.
登革1型病毒（DEN1）包膜蛋白E和非结构蛋白NS1的抗原结构已通过在大肠杆菌中表达的重组融合蛋白形式进行了研究。缺失分析用于鉴定E中与抗病毒单克隆抗体（MAb）亚群反应的两个不同抗原结构域。E的结构域I从E的氨基酸残基（aa）76延伸至93；结构域II从aa 293延伸至402，并包含一个必需的二硫键。MAb还与NS1蛋白N端附近聚集的几个决定簇（aa 57至126）发生反应。含有大肠杆菌trpE序列以及E或NS1大部分序列的重组融合蛋白在小鼠中具有免疫原性。E融合蛋白引发的抗体与包含结构域II的一部分蛋白发生反应，而NS1融合蛋白引发的抗体不与我们的MAb所定义的抗原决定簇发生反应。
