摘要
目的分析新疆细粒棘球蚴AgB1、AgB2、AgB4蛋白的氨基酸序列,了解其蛋白二级结构特点,预测抗原表位,为包虫病的进一步免疫学诊断和研究提供理论支持。方法利用生物信息分析软件DNAstar分析3种抗原的蛋白二级结构特点,运用在线软件IEDB对3种抗原各参数进行综合分析并预测其抗原表位。结果EgAgB1、EgAgB2和EgAgB4分别是由78、90、91个氨基酸残基组成的不同多肽。其蛋白质二级结构中均有α-螺旋、β-折叠、转角区域和卷曲区域。综合分析各参数推测EgAgB1具有2个抗原表位,分别是14～23位氨基酸残基（DDGLTSTSRS）、37～42位氨基酸残基（RDPLGQ）。推测EgAgB2的2个抗原表位分别为41～49位氨基酸残基（DFFRNDPLG）、83～90位氨基酸残基（EEKDDDSk）。EgAgB4可能含有的2个抗原表位分别是43～50位氨基酸残基（RSDPLGQR）、84～89位氨基酸残基（EEEDDS）。结论采用生物信息技术对新疆细粒棘球蚴AgB1、AgB2、AgB4进行B细胞表位特点的研究和分析,对更准确诊断包虫病具有重要意义。
Objective To analyze EgAgB1,EgAgB2 and EgAgB4 amino acid sequence of the recombinant protein to understand their protein secondary structure prediction epitope to provide theoretical support for further immunological diagnosis and research on hydatid disease. Methods Bioinformatics analysis software DNAstar was used to analyze the protein secondary structure features of three antigens,and the online software IEDB was applied for analyze each of the three antigens parameters and predict their epitopes. Results EgAgB1,EgAgB2 and EgAgB4 are polypeptide consisting of 78,90 and 91 amino acid residues respectively,all which possess α-helix,β-folded corner area and curling area in Protein secondary structure. Comprehensive analysis presumed EgAgB1 parameter contains two epitopes： amino acid fragment of 14-23（ DDGLTSTSRS） and 37-42（ RDPLGQ）,EgAgB2 contains two epitopes： amino acid fragment of 41-49（ DFFRNDPLG） and 83-90（ EEKDDDSk）,and EgAgB4 contains two epitopes： amino acid fragment of 43~50（ RSDPLGQR） and 84~89（ EEEDDS）. Conclusion It is meaningful for more accurate diagnosis of hydatid disease that B cell epitopes feasures of EgAgB1,EgAgB2 and EgAgB4 were analyzed.
出处
《新疆医科大学学报》
CAS
2016年第12期1541-1546,1553,共7页
Journal of Xinjiang Medical University
基金
国家自然科学基金(81160202
81460307
81660343)
新疆维吾尔自治区包虫病重点实验室基金项目(XJDX0202-2010-04)
