西藏藏猪戊型肝炎病毒全基因组生物信息学分析

Genome-wide Bioinformatics Analysis on HEV in Zang Pigs in Xizang Autonomous Region

为了解藏猪源戊型肝炎病毒(HEV)分子特性,选取1株西藏藏猪源HEV4d型(GenBank登录号OQ981960)进行全基因组克隆,并通过多种生物信息学工具对其非结构蛋白、衣壳蛋白和磷蛋白进行生物信息学分析。结果显示:非结构蛋白为不稳定、亲水性蛋白,无跨膜区和信号肽,分别有27和29个T、B细胞抗原表位,二级结构以α-螺旋和无规则卷曲为主,三级结构包含锌离子受体、多个甲基化位点及多种解旋酶;衣壳蛋白为不稳定、亲水性蛋白,有跨膜区和信号肽,分别有14和29个T、B细胞抗原表位,二级结构以无规则卷曲和延伸链为主,三级结构包含推定的糖基水解酶、镁离子位点、合成酶、连接酶、异构酶等;磷蛋白为稳定、亲水性蛋白,无跨膜区和信号肽,分别有7和15个T、B细胞抗原表位,二级结构以α-螺旋和无规则卷曲为主,三级结构包含多个转移酶、聚合酶、连接酶、分泌系统、甲基转移酶、金属离子结合蛋白等。本研究为进一步了解西藏藏猪源HEV基因组和蛋白功能奠定了基础。

In order to investigate the molecular characteristics of hepatitis E virus(HEV)derived from Xizang pigs,one strain of HEV type 4d(GenBank accession No.OQ981960)was selected for whole genome cloning,and its nonstructural protein,capsid protein and phosphoprotein were bioinformatically analyzed by various bioinformatic tools.The results showed that the non-structural protein was unstable and hydrophilic without any transmembrane region or signal peptide,including 27 T cell antigenic epitopes and 29 B cell antigenic epitopes,and its secondary structure was dominated by a-helixes and random coils,while its tertiary structure contained zinc ion receptor,multiple methylation sites and a variety of deconjugating enzymes;the capsid protein was unstable and hydrophilic with transmembrane region and signal peptide,including 14 T cell antigenic epitopes and 29 B cell antigenic epitopes,its secondary structure was dominated by random coils and extended strands,while its tertiary structure contained putative glycosyl hydrolases,magnesium ion sites,synthetases,ligases,isomerases and others;phosphoprotein was stable and hydrophilic without any transmembrane region or signal peptide,including 7 T cell antigenic epitopes and 15 B cell antigenic epitopes,and its secondary structure was dominated byα-helixes and random coils,while its tertiary structure contained multiple transferases,polymerases,ligases,secretory system,methyltransferases,metal ion binding proteins,etc.A foundation was laid by the study for further understanding of the genome and protein functions of HEV derived from Zang pigs.