SM22-α蛋白结构与功能的生物信息学分析  

Bioinformatics analysis of the structure and function of SM22-αprotein

作　　者：门杰[1] 李昊 许婷 姚思羽 刘致宇 邹双玲 马佳 相晨敏 王文娟 MEN Jie;LI Hao;XU Ting;YAO Si-yu;LIU Zhi-yu;ZOU Shuang-ling;MA Jia;XIANG Chen-min;WANG Wen-juan(Fenyang College of Shanxi Medical University,Fenyang 032200,China)

机构地区：[1]山西医科大学汾阳学院,山西汾阳032200

出　　处：《生物技术》2022年第6期684-692,共9页Biotechnology

基　　金：山西省高等学校科技创新计划创新项目(2020L0750);山西医科大学汾阳学院科技扶持基金(2020C08);山西医科大学汾阳学院大学生创新创业计划项目(FDC202101,FDC202103,FDC202104,FDC202113,FDC202124);山西省高等学校大学生创新创业计划项目(S202117114011)。

摘　　要：[目的]通过生物信息学分析手段对SM22-α蛋白结构与作用进行系统性分析。[方法]从NCBI数据库中获取SM22-α蛋白的基本信息,应用NCBI GenBank、ExPAsy、TMHMM Server v.2.0、NetPhos 3.1 Server、IEDB、SIGNALP 5.0 Server等生物信息学分析软件对SM22-α蛋白的氨基酸序列、理化性质、跨膜结构、亲水/疏水性、功能位点、信号肽、序列同源性、糖基化和磷酸化位点、空间结构以及抗原表位进行分析。[结果]SM22-α蛋白编码201个氨基酸,为碱性蛋白,其等电点为8.85,不稳定指数为31.85,并将其归为稳定蛋白。其平均亲水系数为-0.607,为亲水性蛋白。根据IEDB在线软件发现SM22-α蛋白序列的第4-31、39-50、70-89、105-111、116-122、138-197存在B细胞抗原表位。利用HLA-A*0.2:0.1算法预测SM22-α蛋白序列第61和130位序列表面存在2个T细胞抗原表位;若利用HLA-DRBI*0401算法预测则第142位序列存在1个T细胞抗原表位。SM22-α蛋白的二级结构中α螺旋占46.77%,延伸链占6.47%,β-转角占4.48%,无规则卷曲占42.29%。且通过生物信息学分析可知SM22-α蛋白在不同物种之间的同源性为97.0%~68.7%。[结论]SM22-α为碱性、稳定、亲水性胞外蛋白,且蛋白表面含有T、B细胞抗原表位,可为其抗原性药物研究提供理论参考。[Objective]The structure and function of SM22-αprotein were systematically analyzed by bioinformatics analysis.[Method]The basic information of SM22-αprotein was obtained from NCBI database,bioinformatics analysis software,such as NCBI GenBank,ExPAsy,TMHMM Server v.2.0,NetPhos 3.1 Server,IEDB,SIGNALP 5.0 SERVER and so on,were used in order to analyze the amino acid sequence,physicochemical properties,transmembrane domain,hydrophilic/hydrophobic,functional site,signal peptide,sequence homology,glycosylation site,phosphorylation site,spatial structure and cell epitope of SM22-αprotein.[Result]It can be seen from the analysis that SM22-αprotein is a basic protein encodes 201 amino acids and Its isoelectric point is 8.85,and we classified it as a stable protein because its instability index is 31.85.It is also a hydrophilic protein with average hydrophilic coefficient is-0.607.B cell epitopes of SM22-αprotein sequence 4-31,39-50,70-89,105-111,116-122,138-197 were found according to IEDB online software.HLA-A*0.2:0.1 algorithm was used to predict the presence of two T cell epitopes on the surface of position 61 and 130 of SM22-αprotein.If HLA-DRBI*0401 algorithm was used to predict the presence of a T cell epitope in the 142 th sequence.In the secondary structure of SM22-α,alpha helix accounts for 46.77%,extended strand accounts for 6.47%,beta turn accounts for 4.48%and random coil accounts for 42.29%.And bioinformatics analysis showed that the homology of SM22-αprotein among different species was 97.0%-68.7%.[Conclusion]SM22-αprotein is an alkaline,unstable,hydrophilic extracellular protein,and its surface contains T and B cell epitopes,which can provide theoretical reference for antigenicity study.

关 键 词：SM22-α蛋白 动脉粥样硬化 生物信息学分析 理化性质 

分 类 号：R543.3[医药卫生—心血管疾病]