医学分子生物学杂志2011，Vol.8Issue(2)：118-122,5.DOI:10.3870/j.issn.1672-8009.2011.02.006
巴尔通体(Bartonella tribocorum)P26蛋白原核重组表达研究
Expression of Recombinant p26 Protein of Bartonella tribocorum
摘要
Abstract
Objective To generate prokaryotic expression vector for Bartonella surface protein p26 gene, express and purify the recombinant p26, and characterize its antigenicity. Methods p26 gene was amplified from the genomic DNA of B. tribocorum isolated from Xiamen region through PCR assay. The coding region of p26 was cloned into pGEX-4T-1 vector to generate the prokaryotic vector expressing recombinant fusion protein GST-p26. The expression vector was transformed into E. coli DH5α to express GST-p26. GST-p26 was purified through affinity chromatography assay. The antigenicity of GST-p26 was investigated with Western-blot and indirect ELISA assay. Results We successfully generated the recombinant p26 protein prokaryotic expression vector. The expression vector was induced to produce GST-p26 efficiently. Western-blot experiment indicated that the expressed prokaryotic GST-p26 immunologically reacted with the blood samples from the infected animal. Coriclusion The results demonstrated that the expressed recombinant GST-p26 is a potential antigen for serological detection of Bartonella.关键词
巴尔通体/巴尔通体表面蛋白/基因表达与调控分类
生物科学引用本文复制引用
叶曦,伍小春,李国伟,罗炜,王团老..巴尔通体(Bartonella tribocorum)P26蛋白原核重组表达研究[J].医学分子生物学杂志,2011,8(2):118-122,5.基金项目
厦门市医学科技计划(No.WZK-0629) （No.WZK-0629）
