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为了探讨戊型肝炎病毒衣壳蛋白同源二聚体形成的关键区域和相互作用结构域 ,以及二聚体形成与主要天然中和表位的形成之间的关系 ,通过末端缺失、定点突变技术研究戊型肝炎病毒 (HEV)ORF2的aa394_aa6 0 6片段NE2的聚合现象 ,发现其C端的aa5 97_aa6 0 2 (AVAVLA)疏水区是该片段同源聚合的核心区域 ,提高该区域氨基酸的亲水性将妨碍聚合现象的发生 ;半胱氨酸化学交联实验表明NE2形成同源二聚体时 ,aa5 97在空间位置上相接近 ,处于可生成化学键的距离 ,提示所处区域为疏水聚合的作用结构域 ;通过Blast程序估算核心区域的天然突变率 ,发现其疏水性高度保守 ;N端缺失实验表明 ,至少 6 5个氨基酸既不影响同源聚合也不直接参与主要的天然中和表位的形成 ,但可协助中和表位构象的形成 ,而这种协助作用可被ORF2的末端肽段所代替。aa5 97_aa6 0 2 (AVAVLA)疏水区为戊肝病毒衣壳组装的第一步骤的核心区域 ,并与重要的天然中和表位的形成直接相关 ,从而为戊肝病毒疫苗的研究提供更详细的信息。
In order to explore the key regions and interaction domains of hepatitis D virus capsid homodimers and the relationship between dimer formation and the formation of major natural neutralizing epitopes, To study the polymerization of NE2 in the aa394_aa6 0 6 fragment of HEV ORF2, we found that the hydrophobic region aa5 97_aa6 0 2 (AVAVLA) at the C-terminus is the core region of homologous polymerization of this fragment and enhances the hydrophilicity of amino acids in this region Will hinder the occurrence of polymerization phenomenon; cysteine chemical cross-linking experiments showed that NE2 homodimers, aa5 97 in the spatial position close to the chemical bond can be generated in the distance, suggesting that the region is hydrophobic polymerization Domain. The natural mutation rate of the core region was estimated by Blast program and its hydrophobicity was highly conserved. The N-terminal deletion experiment showed that at least 65 amino acids did not affect homologous polymerization nor directly participated in the major natural neutralizing epitopes But can assist in the formation of neutralizing epitope conformations that can be replaced by the terminal peptide of ORF2. aa5 97_aa6 0 2 (AVAVLA) The hydrophobic region is the core region of the first step in the assembly of the HEV capsid and is directly related to the formation of important natural neutralizing epitopes, providing a more detailed information.