柯萨奇病毒A组19型VP1蛋白生物信息学分析  

Bioinformatics analysis of coxsackievirus A19 VP1 protein

作　　者：杨亚文 冯琳琳 陶玲[1] 徐银兰 徐鹏卫[1] 晋乐飞 吴卫东[1] YANG Yawen;FENG Linlin;TAO Ling;XU Yinlan;XU Pengwei;JIN Yuefei;WU Weidong(School of Public Health,Xinxiang Medical University,Xinxiang 453003,Henan,China;School of Medical Laboratory,Sanquan College of Xinxiang Medical University;School of Public Health,Zhengzhou University)

机构地区：[1]新乡医学院公共卫生学院,河南新乡453003 [2]新乡医学院三全学院医学检验学院 [3]郑州大学公共卫生学院

出　　处：《中国病原生物学杂志》2024年第3期249-256,262,共9页Journal of Pathogen Biology

基　　金：河南省科技攻关项目(No.222102310641)。

摘　　要：目的分析柯萨奇病毒A组19型(coxsackievirus A19,CVA-19)VP1蛋白的理化性质、结构功能并预测其线性B细胞表位和T细胞表位。方法应用ProtParam分析CVA-19 VP1蛋白的理化性质;ProtScale预测其亲疏水性;使用SignalP 6.0、DeepTMHMM、NetPhos-3.1和Motif Scan分别预测CVA-19 VP1蛋白的信号肽、跨膜结构域、磷酸化位点和脂酰化位点;利用NetCGlyc-1.0、NetNGlyc-1.0和NetOGlyc-4.0分别预测CVA-19 VP1蛋白的C-甘露糖基化位点、N-糖基化位点和O-N-乙酰半乳糖胺(N-acetylgalactosamine,GalNAc)(粘蛋白型)糖基化位点;通过SOPMA和SWISS-MODEL在线工具分别预测CVA-19 VP1蛋白的二级结构和三级结构;使用网络服务器IEDB、Bepipred 3.0、ABCpred和SVTMrip联合预测其线性B细胞表位;应用IEDB和SYFPEITHI综合预测其T细胞表位。结果CVA-19 VP1蛋白的分子质量为33.099 ku,等电点为5.84,不稳定系数为37.50,总平均亲水性为-0.185,是一种稳定的亲水性蛋白,无信号肽、跨膜区和脂酰化位点。预测该蛋白含有30个可能的磷酸化位点、1个N-糖基化位点和7个O-GalNAc(粘蛋白型)糖基化位点,但无C-甘露糖基化位点。CVA-19 VP1蛋白的二级结构中,α-螺旋、延伸链、β-转角和无规则卷曲分别占24.66%、24.32%、2.70%和48.31%,以无规则卷曲为主。预测出该蛋白有6个潜在优势线性B细胞表位、3个潜在优势细胞毒性T淋巴细胞表位和9个潜在优势辅助性T细胞表位。结论用生物信息学方法预测CVA-19 VP1蛋白为稳定的亲水性蛋白,含有多个潜在的优势线性B细胞表位和T细胞表位,为进一步鉴定其线性表位奠定了基础,有助于CVA-19的抗体制备和疫苗研发。Objective To analyze the physicochemical properties,structure,and function of coxsackievirus A19(CVA-19)VP1 protein and predict the linear B cell epitopes and T cell epitopes.Methods ProtParam was used to analyze the physicochemical properties of CVA-19 VP1 protein.ProtScale was used to predict the hydrophilicity and hydrophobicity.The signal peptide,transmembrane domain,phosphorylation sites,and fatty acylation sites of CVA-19 VP1 protein were predicted by SignalP 6.0,DeepTMHMM,NetPhos-3.1,and Motif Scan,respectively.Using NetCGlyc-1.0,NetNGlyc-1.0,and NetOGlyc-4.0,the C-mannosylation sites,N-glycosylation sites,and O-N-acetylgalactosamine(GalNAc,mucin type)glycosylation sites of CVA-19 VP1 protein were respectively predicted.The secondary and tertiary structures of CVA-19 VP1 protein were separately predicted using the SOPMA and SWISS-MODEL online tools.The web servers IEDB,Bepipred 3.0,ABCpred,and SVTMrip were used to jointly predict the linear B cell epitopes.IEDB and SYFPEITHI were employed to comprehensively predict the T cell epitopes.Results The molecular weight of CVA-19 VP1 protein was 33.099 ku,the isoelectric point was 5.84,the instability coefficient was 37.50,and the grand average of hydropathicity was-0.185,so CVA-19 VP1 protein was a stable hydrophilic protein.In addition,the protein had no signal peptide,transmembrane domain,or fatty acylation site.It was predicted to contain 30 possible phosphorylation sites,1 Nglycosylation site,and 7 O-GalNAc(mucin type)glycosylation sites,but there was no C-mannosylation site.In the secondary structure of CVA-19 VP1 protein,there were 24.66%ofα-helix,24.32%of extended strand,2.70%ofβ-turn,and 48.31%of random curl,among which random curls accounted for the majority.As predicted,there were 6 potential dominant linear B cell epitopes,3 potential dominant cytotoxic T lymphocyte epitopes,and 9 potential dominant helper T cell epitopes of this protein.Conclusion Predicted by bioinformatics methods,CVA-19 VP1 protein is a stable hydrophilic protein and contains mu

关 键 词：柯萨奇病毒A组19型 VP1蛋白 抗原表位 生物信息学 

分 类 号：R373[医药卫生—病原生物学]