摘要
目的:预测欧猥迭宫绦虫成虫谷胱甘肽转移酶1(Glutathione S-Transferase1,GST1)基因及其编码蛋白的结构和功能。方法:应用生物信息学方法对从欧猥迭宫绦虫成虫cDNA文库中所获基因的氨基酸组成、基本性质进行分析,同时构建其编码蛋白的系统进化树并对其抗原表位进行预测及定位;建立其编码蛋白的三级空间结构模型。结果:GST1基因编码221个氨基酸,理论分子量为25767.39Da,理论等电点为5.98,理论分子式为C1188H1786N304O330S5,具有2个完整的保守功能域;在细胞内可能发挥基因表达调控及信号转导功能,与猪带绦虫的同源一致性达53%。在进化的过程中与绦虫类亲缘较近,而与脊椎类亲缘较远。预测最有可能的3个潜在抗原表位分别位于35-46aa、87-94aa、215-221aa之间。结论:GST1基因编码的蛋白为胞质型蛋白,可能是理想的药物作用靶点及新型免疫诊断的分子靶标,为对进一步研究奠定理论基础。
Objective: To analyze the structural characteristics of glutathione S transferase 1 gene from adult Spirometra erinaceieuropaei, and to predict the function of its encoded protein by applying the bioinformatics. Methods: Nucleic acid sequences of GST1 gene was obtained from cDNA library of Spirometra erinaceieuropaei adult worm, bioinformatics approach were applied to analyze GST gene's composition, the basic physical and chemical properties, multi-sequence .homological alignment, tertiary structure of GST protein was established on its homology modeling. Results: GST1 gene encoded 221 amino acids, the theoretical molecular mass is 25767.39 Da, the theoretical isoelectrie was 5.98, the theoretical formula is C1188 H1786 N304 0330 S5. There were two complete conservative domains, maybe play a role in the regulation of gene expression and signal transduction within the cell. Consistency of the screened gene with that of Taenia solium GST was 53%. In the process of evolution, it was close relative to the tape-worms but distant relative to the vertebrate. The three most likely potential antigenic epitopes are 35- 46aa, 87-94aa, 215-221aa, which located out side of GST spatial structure and were far away from each other. Conclusions: It suggests that glutathione S transferase 1 of Spirometra erinaceieuropaei is predicted to be a cytoplasmic protein and may be have good application prospect for new immunodiagnostic mo- lecular target, which provides the theoretical basis for further research.
出处
《海南医学院学报》
CAS
2013年第5期577-581,共5页
Journal of Hainan Medical University
基金
国家自然科学基金课题(81260254)~~