日本脑炎病毒包膜蛋白结构域III上的一个功能性表位决定簇与中和抗体结合位点相互作用。
A functional epitope determinant on domain III of the Japanese encephalitis virus envelope protein interacted with neutralizing-antibody combining sites.
作者信息
Lin Cheng-Wen, Wu Suh-Chin
机构信息
Institute of Biotechnology and Department of Life Science, National Tsing-Hua University, Hsinchu 30013, Taiwan.
出版信息
J Virol. 2003 Feb;77(4):2600-6. doi: 10.1128/jvi.77.4.2600-2606.2003.
Abstract
The envelope (E) protein of Japanese encephalitis virus (JEV) is associated with viral binding to cellular receptors, membrane fusion, and the induction of protective neutralizing-antibody responses in hosts. Most previous studies have not provided detailed molecular information about the spatial configuration of the functional epitopes on domain III of the E protein. Here site-directed mutagenesis was performed to demonstrate that the functional epitope determinants at Ser331 and Asp332 on domain III of the JEV E protein interacted with neutralizing monoclonal antibody (MAb) E3.3. Bacterial expression of the recombinant Fab E3.3 confirmed the molecular interactions of Arg94 in complementary determining region H3 with Ser331 and Asp332 on domain III. This study elucidates the detailed molecular structures of the neutralizing epitope determinants on JEV domain III, which can provide useful information for designing new vaccines.
摘要
日本脑炎病毒（JEV）的包膜（E）蛋白与病毒与细胞受体的结合、膜融合以及宿主中保护性中和抗体反应的诱导有关。以前的大多数研究都没有提供关于E蛋白结构域III上功能表位空间构型的详细分子信息。在此进行了定点诱变，以证明JEV E蛋白结构域III上Ser331和Asp332处的功能表位决定簇与中和单克隆抗体（MAb）E3.3相互作用。重组Fab E3.3的细菌表达证实了互补决定区H3中的Arg94与结构域III上的Ser331和Asp332之间的分子相互作用。本研究阐明了JEV结构域III上中和表位决定簇的详细分子结构，可为新型疫苗的设计提供有用信息。
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