丙型肝炎病毒E2蛋白的生物信息学分析
|
摘要
目的探讨研究丙型肝炎病毒E2蛋白的生物学特征。方法从NCBI数据库中获取丙型肝炎病毒E2蛋白氨基酸序列,利用在线分析软件分析其生物学特征,包括分子式、半衰期、疏水性、跨膜区、信号肽,磷酸化位点、二级结构特征等,通过综合分析丙型肝炎病毒E2蛋白的各类性质,得到最佳抗原表位区域,并对丙型肝炎病毒E2蛋白氨基酸序列预测结果进行了比对分析。结果丙肝病毒E2蛋白由344个氨基酸组成,分子式为C_(1696)H_(2543)N_(463)O_(490)S_(21),不稳定系数为35.6,理论等电点为7.2,总体平均亲水性为-0.131,为稳定性亲水蛋白质,E2蛋白二级结构中主要成分为无规则卷曲(占比43.6%)。该蛋白无信号肽且无跨膜区,约存在50个磷酸化位点,最佳抗原区域位于95-100氨基酸位置。结论生物信息学方法预测丙型肝炎病毒E2蛋白属于稳定性亲水蛋白,含有抗原表位区域,可为丙型肝炎表位疫苗的研制提供参考依据。
Objective Analyzing sequence characteristics of E2 protein in Hepatitis C Virus(HCV) were studied via bioinformatics tools. Methods The hepatitis C virus E2 protein amino acid sequence was obtained from the National Center for Biotechnology Information(NCBI) database. The online analysis software was used to analyze and study the sequence characteristics of hepatitis C virus E2 protein. The basic information analysis included molecular formula, half-life, hydrophobicity, transmembrane region, and signal peptide. Functional information analysis included phosphorylation sites and secondary structure characteristics. Finally, a comprehensive analysis of the various properties of the hepatitis C virus E2 protein was done to obtain the best epitope region, and the analysis of the above-mentioned prediction results of the amino acid sequence characteristics of the hepatitis C virus E2 protein were compared. Results E2 protein in Hepatitis C Virus consists of 344 amino acids, its molecular formula is C1696 H2543 N463 O490 S21, and the instability coefficient is 35.6. The protein is predicted to be a stable protein, the theoretical isoelectric point is 7.20, and the total average hydrophilicity is-0.131, which denotes that the E2 protein is a hydrophilic protein. The main component of the secondary structure is irregularly coiled(43.6%), the protein has no signal peptide, and no transmembrane region, 50 phosphorylation sites. Conclusion Best antigenic epitope formation area was determined via a comprehensive analysis of the availability of E2 protein in HCV, β turn angle, antigenicity and hydrophobicity, etc. The study of E2 protein in HCV provides reference for the development of an epitope vaccine against HCV.
Objective Analyzing sequence characteristics of E2 protein in Hepatitis C Virus(HCV) were studied via bioinformatics tools. Methods The hepatitis C virus E2 protein amino acid sequence was obtained from the National Center for Biotechnology Information(NCBI) database. The online analysis software was used to analyze and study the sequence characteristics of hepatitis C virus E2 protein. The basic information analysis included molecular formula, half-life, hydrophobicity, transmembrane region, and signal peptide. Functional information analysis included phosphorylation sites and secondary structure characteristics. Finally, a comprehensive analysis of the various properties of the hepatitis C virus E2 protein was done to obtain the best epitope region, and the analysis of the above-mentioned prediction results of the amino acid sequence characteristics of the hepatitis C virus E2 protein were compared. Results E2 protein in Hepatitis C Virus consists of 344 amino acids, its molecular formula is C1696 H2543 N463 O490 S21, and the instability coefficient is 35.6. The protein is predicted to be a stable protein, the theoretical isoelectric point is 7.20, and the total average hydrophilicity is-0.131, which denotes that the E2 protein is a hydrophilic protein. The main component of the secondary structure is irregularly coiled(43.6%), the protein has no signal peptide, and no transmembrane region, 50 phosphorylation sites. Conclusion Best antigenic epitope formation area was determined via a comprehensive analysis of the availability of E2 protein in HCV, β turn angle, antigenicity and hydrophobicity, etc. The study of E2 protein in HCV provides reference for the development of an epitope vaccine against HCV.
引文
[1] Kong L,Giang E,Nieusma T,et al.Hepatitis C Virus E2 envelope glycoprotein core structure [J].Science,2013,342(6162):1090-4.
[2] Yagnik AT,Lahm A,Meola A,et al.A model for the hepatitis C virus envelope glycoprotein E2 [J].Prot Struce Fun Bio,2015,40(3):355-66.
[3] 卫敏,高文军,邓向红,等.丙型肝炎病毒E1、E2蛋白的表达及初步用于丙型肝炎患儿血清学诊断的临床研究[J].临床肝胆病杂志,2006,22(4):286-7.
[4] 何素梅,周见远,肖建华,等.丙型肝炎病毒E2蛋白的研究进展[J].微生物学免疫学进展,2010,38(4):79-82.
[5] 张德峰,付玉荣,伊正君.结核分枝杆菌CarD蛋白结构与功能的生物信息学分析[J].中国病原生物学杂志,2017,12(7):605-8.
[6] Petersen TN,Brunak S,von Heijne G.et al.SignalP 4.0:discriminating signal peptides from transmembrane regions[J].Nature Methods,2011,8(10):785-6.
[7] 李晋涛,陈正琼,梁志清,等.Eppin抗原的二级结构分析B细胞表位预测[J].第三军医大学学报,2008,30(24):2254-7.
[8] 刘洪波,阳广菲,欧维琳,等.柯萨奇病毒A6型VP1蛋白的生物信息学分析[J].中国免疫学杂志,2016,32(4):536-40.
[9] Penin F,Combet C,Germanidis G,et al.Conservation of the conformation and positive charges of hepatitis C virus E2 envelope glycoprotein hypervariable region 1 points to a role in cell attachment[J].J Virol,2001,75(12):5703-10.
[10] Kong L,Giang E,Nieusma T,et al.Structure of hepatitis C virus envelope glycoprotein E2 antigenic site 412 to 423 in complex with antibody AP33[J].J Mol Biol,2015,427(16):2617-28.
[11] 成军,李克,陆荫,等.丙型肝炎病毒核心蛋白结合蛋白6基因和蛋白的生物信息学分析[J].世界华人消化杂志,2003,11(4):378-84.
[12] Albecka A,Montserret R,Krey T,et al.Identification of new functional regions in hepatitis C virus envelope glycoprotein E2[J].J Virolog,2011,85(4):1777.
[13] Wang Y,Wang J,Wu S,et al.The unexpected structures of hepatitis C virus envelope proteins[J].Exp Ther Med,2017,14(3):1859-65.
[14] Tian ZF,Shen H,Fu XH,et al.Interaction of hepatitis C virus envelope glycoprotein E2 with the large extracellular loop of tupaia CD81[J].World J Gastroenterol,2009,15(2):240.
[15] Higginbottom A,Quinn ER,Kuo CC,et al.Identification of amino acid residues in CD81 critical for interaction with hepatitis C virus envelope glycoprotein E2[J].J Virol,2000,74(8):3642-9.
[16] Freedman H,Logan MR,Law JLM,et al.Structure and function of the hepatitis C virus envelope glycoproteins E1 and E2:antiviral and vaccine targets[J].ACS Infect Dis,2016,2(11):749-62.
[2] Yagnik AT,Lahm A,Meola A,et al.A model for the hepatitis C virus envelope glycoprotein E2 [J].Prot Struce Fun Bio,2015,40(3):355-66.
[3] 卫敏,高文军,邓向红,等.丙型肝炎病毒E1、E2蛋白的表达及初步用于丙型肝炎患儿血清学诊断的临床研究[J].临床肝胆病杂志,2006,22(4):286-7.
[4] 何素梅,周见远,肖建华,等.丙型肝炎病毒E2蛋白的研究进展[J].微生物学免疫学进展,2010,38(4):79-82.
[5] 张德峰,付玉荣,伊正君.结核分枝杆菌CarD蛋白结构与功能的生物信息学分析[J].中国病原生物学杂志,2017,12(7):605-8.
[6] Petersen TN,Brunak S,von Heijne G.et al.SignalP 4.0:discriminating signal peptides from transmembrane regions[J].Nature Methods,2011,8(10):785-6.
[7] 李晋涛,陈正琼,梁志清,等.Eppin抗原的二级结构分析B细胞表位预测[J].第三军医大学学报,2008,30(24):2254-7.
[8] 刘洪波,阳广菲,欧维琳,等.柯萨奇病毒A6型VP1蛋白的生物信息学分析[J].中国免疫学杂志,2016,32(4):536-40.
[9] Penin F,Combet C,Germanidis G,et al.Conservation of the conformation and positive charges of hepatitis C virus E2 envelope glycoprotein hypervariable region 1 points to a role in cell attachment[J].J Virol,2001,75(12):5703-10.
[10] Kong L,Giang E,Nieusma T,et al.Structure of hepatitis C virus envelope glycoprotein E2 antigenic site 412 to 423 in complex with antibody AP33[J].J Mol Biol,2015,427(16):2617-28.
[11] 成军,李克,陆荫,等.丙型肝炎病毒核心蛋白结合蛋白6基因和蛋白的生物信息学分析[J].世界华人消化杂志,2003,11(4):378-84.
[12] Albecka A,Montserret R,Krey T,et al.Identification of new functional regions in hepatitis C virus envelope glycoprotein E2[J].J Virolog,2011,85(4):1777.
[13] Wang Y,Wang J,Wu S,et al.The unexpected structures of hepatitis C virus envelope proteins[J].Exp Ther Med,2017,14(3):1859-65.
[14] Tian ZF,Shen H,Fu XH,et al.Interaction of hepatitis C virus envelope glycoprotein E2 with the large extracellular loop of tupaia CD81[J].World J Gastroenterol,2009,15(2):240.
[15] Higginbottom A,Quinn ER,Kuo CC,et al.Identification of amino acid residues in CD81 critical for interaction with hepatitis C virus envelope glycoprotein E2[J].J Virol,2000,74(8):3642-9.
[16] Freedman H,Logan MR,Law JLM,et al.Structure and function of the hepatitis C virus envelope glycoproteins E1 and E2:antiviral and vaccine targets[J].ACS Infect Dis,2016,2(11):749-62.