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欧猥迭宫绦虫膜联蛋白E1基因的生物信息学分析
引用本文:邬强,李东冬,马盼盼,吕刚. 欧猥迭宫绦虫膜联蛋白E1基因的生物信息学分析[J]. 海南医学院学报, 2010, 16(9): 1106-1110
作者姓名:邬强  李东冬  马盼盼  吕刚
作者单位:海南医学院热带医学与检验医学院,海南,海口,571101
基金项目:国家自然科学基金,海南省教育厅科研课题 
摘    要:目的:从欧猥迭宫绦虫成虫cDNA文库中识别出膜联蛋白E1(Annexin E1)基因,并对其进行生物信息学分析和功能预测。方法:从欧猥迭宫绦虫cDNA文库中获取Annexin E1基因的核酸序列,应用NCBI、ExPASy等多种生物信息学在线分析工具结合Vector NTI Advance10、Geneious Pro等软件包,对所获基因及其编码蛋白的基本理化特征、亚细胞定位、保守功能域、抗原表位、二级结构及拓扑结构等进行预测,建立蛋白质三级空间结构模型及构建其分子进化树。结果:Annexin E1编码354个氨基酸残基,理论分子量为40168.0Da,具有4个完整的保守功能域。位于细胞内,无信号肽及跨膜结构,存在6个潜在抗原表位。二级结构主要以α螺旋为主,结构和功能有关的位点高度保守,具有多个磷酸化位点。在进化的过程中与绦虫类亲缘较近,而与脊椎类亲缘较远。结论:Annexin E1编码蛋白及潜在的抗原表位与宿主同源性低,可能作为研发新型免疫诊断方法的理想分子靶标。

关 键 词:欧猥迭宫绦虫  膜联蛋白  结构  功能  生物信息学

Application of bioinformatic analysis in Annexin E1 of Spirometra erinaceieuropaei
WU Qiang,LI Dong-dong,MA Pan-pan,LV Gang. Application of bioinformatic analysis in Annexin E1 of Spirometra erinaceieuropaei[J]. Journal of Hainan Medical College, 2010, 16(9): 1106-1110
Authors:WU Qiang  LI Dong-dong  MA Pan-pan  LV Gang
Affiliation:(School of Tropical and Laboratory Medicine, Hainan Medical University, Haikou 571101, China)
Abstract:Objective:To identify the Annexin E1 gene from cDNA library of Spirometra erinaceieuropaei adult worm and predict its structure and function by applying the bioinformatics.Methods:Nucleic acid sequences of Annexin E1 gene was obtained from cDNA library of Spirometra erinaceieuropaei,and application tools were provided by bioinformatics websites and other bioinformatics software packages such as Vector NTI Advance 10,Geneious Pro etc.The status of encoded proteins were predicted including the basic physical and chemical properties,subcellular localization,conservative functional domains,domains,antigenic epitopes,secondary structure and topology,etc.Besides,tertiary structure of the protein was established based on homology modeling,undertook multi-sequence homological alignment and phylogenetic analysis.Results:Annexin E1 encoded 354 amino acid residues with a theoretical molecular 40168.0Da.The main secondary structure was α-helix with four complete conservative domains.Structure and function of the highly conserved sites were with multiple phosphorylation sites.It contained no signal peptide and transmembrane helices,six potential antigenic epitopes,locates outside of membrane.In evolution,it was close relative to tapeworm and distant relative to the vertebrate.Conclusions:Homology is low between encoded protein and potential antigen epitopes of Annexin E1 and host's,it might be a desirable molecular target for immunological tests.
Keywords:Spirometra erinaceieuropaei; Annexin; Structure; Function; Bioinformatics;
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