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刘思静, 蒋明娟, 蒲启康等. 结核分枝杆菌clpP2抗原表位预测与分析[J]. 四川大学学报(医学版), 2017, 48(2): 244-247.
引用本文: 刘思静, 蒋明娟, 蒲启康等. 结核分枝杆菌clpP2抗原表位预测与分析[J]. 四川大学学报(医学版), 2017, 48(2): 244-247.
LIU Si-jing, JIANG Ming-juan, PU Qi-kang. et al. Prediction and Analysis of Epitopes in clpP2 of Mycobacterium tuberculosis[J]. Journal of Sichuan University (Medical Sciences), 2017, 48(2): 244-247.
Citation: LIU Si-jing, JIANG Ming-juan, PU Qi-kang. et al. Prediction and Analysis of Epitopes in clpP2 of Mycobacterium tuberculosis[J]. Journal of Sichuan University (Medical Sciences), 2017, 48(2): 244-247.

结核分枝杆菌clpP2抗原表位预测与分析

Prediction and Analysis of Epitopes in clpP2 of Mycobacterium tuberculosis

  • 摘要: 【摘要】 目的 预测结核分枝杆菌酪蛋白酶蛋白水解亚基单位2(clpP2)的抗原表位,为结核病疫苗、药物研制等提供新的靶点。方法 以clpP2蛋白的氨基酸序列为基础,采用生物信息软件DNA Star预测二级结构;运用SWISS-MODEL在线软件进行同源建模;运用VaxiPred软件综合预测T 细胞抗原表位,用ABCpred、COBEPro和BepiPredPred 软件综合预测其B 细胞抗原表位;采用DNA Star Protean、SignalP、TMHMM在线软件和NCBI数据库分析其免疫学相关信息。结果 clpP2蛋白结构丰富,含有较多潜在细胞毒性T细胞和辅助T细胞表位; 也含有较多的B细胞线性和构象优势表位,这些区域亲水性、表面可能性和柔韧性指数都较高。结论 clpP2蛋白具有诱导免疫应答的潜能,可以作为结核监测、治疗、预防的新靶点。

     

    Abstract: 【Abstract】 Objective To predict and analyze the antigenic epitopes in Mycobacterium tuberculosis protein caseinolytic protease P2 (clpP2), and explore its possibility to be applied as a new tuberculosis (TB) vaccine and drug development target. Methods Secondary structure of clpP2 based on nucleic sequence was predicted by DNA Star software. The homologous sequence conformation were analyzed by Swiss-Model online software. T cells antigenic epitopes were predicted through VaxiPred, and B cell epitopes were predicted by combining use of several different prediction programs, such as ABCpred, COBEPro and BepiPredPred. The immune characteristics of clpP2 were analyzed by DNA Star, SignalP, TMHMM online software and were searched through NCBI database. Results clpP2protein was diverse in structure, composing with a great deal of CTL and Th cell epitopes. clpP2 was also predicted to comprise rich potential liner and discontinuous B-cell epitopes. These epitopes were accessible on the protein surface, located in flexible and hydrophilic regions. Conclusion clpP2 is prompted to induce immune responses and developes a novel target in surveillance, treatment and vaccine.

     

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