摘要
为了对流产布鲁菌BP26蛋白进行抗原表位研究,设计了3个相互重叠15个氨基酸、覆盖整个BP26蛋白的重叠短肽,经克隆并在大肠杆菌中实现了融合表达。用流产型布鲁菌感染血清对3个融合蛋白进行免疫印迹分析,结果初步鉴定出BP26蛋白B细胞线性抗原表位位于第51-165氨基酸区域。在此基础上,针对BP26 2(51-165aa)短肽,设计了5个相互重叠10个氨基酸的短肽片段,进一步鉴定出了BP26蛋白B细胞线性表位位于第109-141氨基酸区域。该结果为进一步探索BP26蛋白的结构和功能以及建立诊断方法奠定了基础。
In order to identify the linear B-cell epitope of structural protein BP26 of Brucella abor- tus, the BP26 protein was dissected into three overlapping fragments,and expressed in Escherich- ia coli, respectively. Western blot analysis of the three fused proteins was carried out with sera from Brucella infected cattle. The results showed that the linear B-cell epitope of BP26 protein was located in the 51-165 aa. Based on these, the short peptide protein BP26 2 was dissected into five overlapping fragments further. Finally, we identified that the linear B cell epitope on BP26 is located in the 109-141 amino acid. It was concluded that the MAbs against the protein BP26 could be useful tools for further studying on the structure and function of BP26, as well as for develop- ment of diagnostic methods.
出处
《畜牧兽医学报》
CAS
CSCD
北大核心
2012年第9期1444-1448,共5页
ACTA VETERINARIA ET ZOOTECHNICA SINICA
基金
国家科技支撑计划课题(2007BAD60B02)
现代农业产业技术体系建设专项资金(CARS-37)
