摘要
通过生物信息学相关软件分析大豆过敏原Gly m 4蛋白理化性质(Prot Param)、信号肽(Signal P 4.1 Server)、跨膜区(TMHMM Server V 2.0)、B细胞表位(DNAStar)、MHC-Ⅱ类分子的结合能力(Net MHCⅡ2.2)。结果发现:Gly m4蛋白稳定性较好,无信号肽与跨膜区,转角结构丰富;B细胞抗原表位预测表明,Gly m 4蛋白61~64、93~94、122~125、127~130、134~137区域是潜在B细胞抗原表位;MHC-Ⅱ类分子的结合力分析表明Gly m 4蛋白144~153区域及82~96区域是潜在T细胞抗原表位,同时发现HLA-DRB10701、HLA-DRB10101等位基因型人群对Gly m 4蛋白较敏感。Gly m 4蛋白抗原表位分析为大豆过敏原的低过敏原性改造提供参考依据。
To analyze the physicochemical properties and structure of major Glycine max( Linn. ) Merr. allergen Gly m 4 pro- tein using bioinformatics software and provide a reference for modifying the allergen Gly m 4 protein experimentally. The amino acid sequence of Gly m 4 protein was searched from NCBI database. The physicochemicat properties were analyzed by Prot- Param, the signal peptide of Gly m 4 protein was analyzed by SignalP 4. 1 Server, the transmembrane helix was analyzed by TMHMM Server V 2. 0, the B cell epitopes were predicted with DNAStar. The binding affinity between Gly m 4 protein and MHC- II molecules was analyzed with NetMHCII 2. 2 Server to predict the T cell epitopes. The results showed that Gly m 4 protein was stable and doesn't possess any signal peptide and transmembrane helix, most secondary structures of Gly m 4 were turn regions. Prediction result suggested the potential B cell epitope of Gly m 4 were located in the region of 61-64, 93-94, 122-125, 127-130 and 134-137. Analysis of the binding affinity between Gly m 4 and MHC-II molecules suggested the regions of 144-153 and 82-96 were the potential T cell epitopes. Human with HLA-DRB10701 alleles and HLA-DRB10101 alleles maybe more sensitive to Gly m 4 protein. This study facilitates to understand the antigen epitope of Gly m 4 protein and provides a reference to reduce the allergenicity of Gly m 4.
出处
《大豆科学》
CAS
CSCD
北大核心
2017年第3期365-370,共6页
Soybean Science
基金
国家科技重大专项重点课题(2014ZX08011-05B)