结核分枝杆菌TB10.4蛋白的生物信息学分析

Bioinformatics Analysis of Mycobacterium Tuberculosis TB10.4 Protein

目的预测分析结核分枝杆菌Rv0288基因的编码蛋白TB10.4的结构和功能。方法采用生物信息学软件ORF Finder、ExPASy、PSORT、SOSUI、TMHMM、SOPMA等预测分析结核分枝杆菌TB10.4蛋白的结构和功能。结果TB10.4蛋白由96个氨基酸组成,分子式为C448H677N125O143S9,原子总数1402,编码基因全长291 bp,等电点4.58,不稳定性50.36,为不稳定性蛋白。ProtScale软件预测TB10.4蛋白的脂肪族氨基酸指数为59.38,平均疏水性-0.266。SOSUI和Signal IP软件预测该蛋白无信号肽无跨膜区。TMHMM、NerNGlyc、NetPhos软件预测TB10.4蛋白为可溶性蛋白,有8个磷酸化位点,无糖基化位点。TB10.4蛋白的二级结构以α-螺旋(86.46%)为主,亚细胞定位于细胞质。IEDB软件预测该蛋白有3个B细胞抗原表位;SYFPEITHI、RANKPEP、NetMHC软件预测该蛋白有多个CTL表位和Th表位。STRING预测TB10.4和esxS、esxB、esxH、esxG、PPE4、PPE 18、PE5等蛋白有相互作用,参与多种胞浆蛋白,其二级结构生物学过程。结论TB10.4蛋白为不稳定疏水性以α-螺旋结构为主,含有多个T、B细胞抗原位点,能够磷酸化并与多种蛋白相互作用,可作为抗结核疫苗的候选蛋白。

Objective To predict and analyze the structure and function of the protein TB10.4 encoded by Rv0288 gene of Mycobacterium tuberculosis.Methods The structure and function of TB10.4 protein of Mycobacterium tuberculosis were predicted and analyzed by bioinformatics software ORF Finder,ExPASy,PSORT,SOSUI,TMHMM and SOPMA.Results TB10.4 protein was composed of 96 amino acids,the molecular formula was C448H677N125O143S9,the total number of atoms was 1402,the coding gene was 291 bp,the isoelectric point was 4.58,and the instability was 50.36,which was an unstable protein.ProtScale software predicted that the aliphatic amino acid index of TB10.4 protein was 59.38,and the average hydrophobicity was-0.266.SOSUI and SignalIP software predicted that the protein had no signal peptide and no transmembrane region.TMHMM,NerNGlyc and NetPhos software predicted that TB10.4 protein was a soluble protein with 8 phosphorylation sites and no glycosylation sites.The secondary structure of TB10.4 protein was mainlyα-helix(86.46%),and subcellular localization was in the cytoplasm.The IEDB software predicted that the protein had three B-cell epitopes;SYFPEITHI,RANKPEP,and NetMHC software predicted that the protein had multiple CTL epitopes and Th epitopes.STRING predicted that TB10.4 interacted with proteins such as esxS,esxB,esxH,esxG,PPE4,PPE 18,PE5 and participated in a variety of cytoplasmic proteins and their secondary structure biological processes.Conclusion TB10.4 protein is unstable and hydrophobic,mainly withα-helix structure,containing multiple T and B cell antigen sites,which can be phosphorylated and interact with a variety of proteins,and can be used as a candidate protein for anti-tuberculosis vaccine.