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结核分枝杆菌mpt53蛋白的生物信息学分析 被引量:2

Bioinformatics analysis of Mycobacterium tuberculosis mpt53 protein
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摘要 目的应用生物学软件预测结核分枝杆菌Rv2878c基因编码蛋白mpt53的结构和功能。方法从NCBI中获得Rv2878c基因及其编码序列,通过ORF Finder、ProtParam、ProtScaleon Expasy、TMHMM Server v.2.0、SignalP 4.1 Server、TargetP 1.1 Server、NetPhos 3.1 Server、BLAST、SOPMA、SWISS-MODEL、ABCpred、SYFPEITHI、STRING等工具预测分析mpt53蛋白的相关生物学信息。结果Rv2878c基因全长为922 bp,有8个开放阅读框架,其编码蛋白mpt53由172个氨基酸组成,等电点5.19,为含有信号肽的非跨膜蛋白;该蛋白含有21个磷酸化位点,1个保守域,18个(得分≥0.80)B细胞抗原表位和8个(得分≥15)T细胞抗原表位;二级结构预测mpt53中α-螺旋占32.56%,β-折叠占23.84%,β-转角占7.56%,无规则卷曲占36.05%。富集分析显示该蛋白与氧化还原反应有关。讨论生物学信息分析mpt53蛋白为分泌蛋白,可用于研发结核病血清学诊断试剂。蛋白的二级结构助于氧化折叠,是抗结核药物的潜在靶点;该蛋白含有有大量潜在的T、B细胞抗原表位,是结核病疫苗的候选蛋白。 Objective Prediction of structure and function of mpt53 protein encoded by Rv2878 c gene of Mycobacterium tuberculosis by biological software.Methods The Rv2878 c gene and its coding sequence were obtained from NCBI database.The open reading framework of Rv2878 c gene was analyzed by ORF Finder tool.The physical and chemical properties and hydrophobicity of mpt53 protein were predicted by ProtParam and ProtScaleon Expash.The transmembrane region of mpt53 protein was analyzed by TMHMM Server v.2.0.Signal P 4.1 Server and TargetP 1.1 Server tools were used to predict mpt53 signal peptide and subcellular localization.Netphos 3.1 server was used to predict mpt53 phosphorylation sites.The conserved domain and homology of mpt53 protein were analyzed by blast.Secondary structure and tertiary structure of proteins were analyzed by Sopma and Swans model tools.Protein epitopes were predicted by ABCpred and SYFPEITHI to find the best B and T cell epitopes.Interaction protein and Go analyse of mpt53 protein were predicted by STRING.Results Rv2878 c gene has a total length of 922 bp and 8 open reading frames,and its coding protein is mpt53.The protein is composed of 172 amino acids with an isoelectric point of 5.19 and is a non transmembrane protein containing signal peptide;It has 21 phosphorylation sites,1 conserved domain,18 B cell epitopes(Score≥0.80)and 9 T cell epitopes(Score≥15);The prediction of protein secondary structure shows that alpha helix accounts for 32.56%,beta bridge for 23.84%,beta turn for 7.56%,and random coil for 36.05%;The protein is related to redox reaction.It is discussed that mpt53 is a secretory protein,which contributes to the oxidative folding of proteins.It has a large number of potential T and B cell epitopes,and can be used as a candidate protein for the development of tuberculosis diagnostic reagents,anti tuberculosis drugs and tuberculosis vaccines.Conclusion Protein mpt53 is a secretory protein,which is helpful for protein oxidative folding.It has a large number of potential T and B cell epitopes,and can be used as a candidate protein for the development of tuberculosis diagnostic reagents,anti tuberculosis drugs and tuberculosis vaccines.
作者 杨雨昕 付玉荣 伊正君 YANG Yu-xin;FU Yu-rong;YI Zheng-jun(Department of Mededical Laboratory Science,Weifang Medical University,Weifang 261031,Shandong,China;Department of Pathogen Biology,Weifang Medical University)
出处 《中国病原生物学杂志》 CSCD 北大核心 2020年第7期768-773,共6页 Journal of Pathogen Biology
基金 山东省自然科学基金重大基础研究项目(No.ZR2018ZC1054) 山东省自然科学基金面上项目(No.ZR2018MH001)。
关键词 mpt53蛋白 结核分枝杆菌 Rv2878c 生物信息学分析 mpt53 protein Mycobacterium tuberculosis Rv2878c bioinformatics analysis
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