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牛源结核分枝杆菌pknB基因生物信息学分析OA

Bioinformatics Analysis of pknB Gene of Mycobacterium tuberculosis var.bovis

中文摘要英文摘要

为了解牛源结核分枝杆菌关键蛋白的生物学功能,应用生物信息学方法对丝氨酸/苏氨酸蛋白激酶pknB蛋白的结构及生物学特性进行了预测.结果显示:牛源结核分枝杆菌pknB蛋白是一类Ⅱ型跨膜蛋白,其跨膜区位于蛋白中部,亲水性强但缺乏能够分泌表达的信号肽;高级结构中无规则卷曲和α螺旋占比较高,分别为 44.73%和 32.27%,延伸链和β转角含量较少;pknB蛋白定位在细胞内质网的可能性最高,其次为细胞质,而定位在细胞核、高尔基体和线粒体的可能性最低;存在多个优势抗原表位,其中B细胞抗原表位有 12 个,分值大于 25 分的T细胞表位有 8 个;存在 65 个潜在的磷酸化修饰位点,它们可能与MRA_3902、MRA_3400、cfp17 等多种蛋白发生相互作用.结果说明:pknB蛋白作为一种跨膜蛋白具有良好的免疫原性,并参与宿主的NF-κB信号通路进而影响细菌增殖,可以作为抗结核病疫苗研发及快速诊断试剂盒研制的候选靶标蛋白.

In order to verify the biological functions of key protein of Mycobacterium tuberculosis var.bovis(MTB),the structure and biological properties of serine/threonine protein kinase pknB protein were predicted using the bioinformatics method.The results showed that pknB protein belonged to type Ⅱ transmembrane protein with a transmembrane region located in the middle of the protein,which was strongly hydrophilic without a signal peptide for secretion expression;random coils and α-helixes accounted for high proportions in the high-level structure,which were 44.73%and 32.27%,respectively,little extension strands and β-turns were contained;pknB protein was most likely located in the endoplasmic reticulum of cells,then in cytoplasm,but least likely in nucleus,golgi apparatus and mitochondria;many dominant antigenic epitopes were available,including 12 B-cell antigenic epitopes and 8 T-cell epitopes with above 25 scores;there were 65 potential phosphorylation modification sites that might interact with a variety of proteins,such as MRA_3902,MRA_3400,cfp17,etc.In conclusion,as a transmembrane protein,pknB was with good immunogenicity and could affect bacterial proliferation as an actor in the NF-κB signaling pathway of hosts,hence could be used as a candidate target protein for the development of vaccines and rapid diagnostic kits of tuberculosis.

郑琛;郭明佳

龙口市七甲镇畜牧兽医站,山东龙口 265722龙口市动物疫病预防控制中心,山东龙口 265701

畜牧业

结核分枝杆菌pknB基因生物信息分析遗传进化

MTBpknB genebioinformatics analysisgenetic evolution

《中国动物检疫》 2024 (008)

28-33 / 6

10.3969/j.issn.1005-944X.2024.08.006

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