【摘要】 为了筛选出牛源致脑炎大肠杆菌S9922 FimD、PilN蛋白的优势B细胞表位，本试验采用生物信息学分析工具ProtParam、TMHMM、NetPhos、DNASTAR软件、SOPMA、SWISS-MODEL、BepiPred、Immunomedicine Group等对FimD、PilN蛋白进行理化性质、跨膜区、信号肽、糖基化位点、磷酸化位点、二级结构、三级结构和B细胞表位预测，并进行综合分析，最终得出优势B细胞表位。结果显示，FimD、PilN蛋白都为亲水、稳定蛋白，无规则卷曲在二级结构中所占比例最高；FimD蛋白共有48个磷酸化位点，不存在跨膜区和信号肽；PilN蛋白共有85个磷酸化位点，PilN蛋白在1～50位氨基酸上可能出现跨膜区，26～27位氨基酸上出现信号肽；多种参数综合分析最终得到潜在的优势B细胞表位，FimD蛋白：7～18、144～152、307～315、365～373;PilN蛋白：77～86、138～149、516～524。通过对FimD、PilN蛋白进行综合分析，最终得出潜在的优势B细胞表位，为牛源致脑炎大肠杆菌多表位疫苗的进一步研究提供参考依据。更多还原

【Abstract】 In order to identify the dominant B cell epitopes in FimD and PilN proteins from bovineEscherichia coliS9922, this study employed bioinformatics analysis tools such as ProtParam, TMHMM, NetPhos, DNASTAR, SOPMA, SWISS-MODEL,BepiPred and Immunomedicine Group to predict the physicochemical properties, transmembrane regions, signal peptides, glycosylation sites, phosphorylation sites, secondary structures, tertiary structures and B cell epitopes in FimD and PilN proteins. The results showed that both FimD and PilN were hydrophilic and stable proteins, and irregular curling accounted for the highest proportion in the secondary structure; 48 phosphorylation sites were present in FimD protein, and no transmembrane region and signal peptide in FimD protein were found; 85 phosphorylation sites existed in PilN protein, and transmembrane region might appear in PilN protein at 1-50amino acid position, and signal peptide appeared at 26-27 amino acid position. Comprehensive analysis of various parameters identified dominant B cell epitopes in FimD protein at 7-18, 144-152, 307-315, 365-373, and in PilN protein at 77-86, 138-149, 516-524. Thus, comprehensive analysis of FimD and PilN proteins and identification of the dominant B cell epitopes laid the foundation for further development of multi-epitope vaccine againstEscherichia colicausing bovine encephalitis.更多还原