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本文用具有中和活性单克隆抗体(McAb)筛选出7株蜱传脑炎病毒抗原变异株,进行RNA序列对比分析,结合蛋白E氨基末端序列分析,确定了蛋白E的四个免疫反应片段(IRF)在一级结构上的位置。根据已知的黄病毒结构特点尤其是二硫键的位置,构建了一个E蛋白结构模型,显示多肽链折迭成三个蛋白功能区(A、B及C)和一个跨膜结构。A功能区是由一级结构上远离的两个区段组成的不连续的结构,其中第98～111位氨基酸残基为最保守的序列,提示此段序列有极其重要的功能,可能为黄病
In this paper, seven strains of tick-borne encephalitis virus were screened by monoclonal antibody (McAb) with neutralizing activity and compared with RNA sequences. Based on amino-terminal sequence analysis of protein E, four immunoreactive fragments of protein E IRF) in the primary structure of the position. Based on the known flaviviral structural features, especially disulfide bonds, an E-protein structural model was constructed showing that the polypeptide chains fold into three protein domains (A, B and C) and a transmembrane structure. The A functional domain is a discontinuous structure consisting of two segments that are far away from the primary structure. The amino acid residues 98 to 111 are the most conserved sequences, suggesting that this sequence has an extremely important function and may be yellow disease