Expression and purification of Tp0751 recombinant protein of Treponema pallidum and its immuno-competence analysis
10.3760/cma.j.issn.0254-5101.2009.07.008
- VernacularTitle:梅毒螺旋体Tp0751黏附蛋白的表达、纯化及免疫活性研究
- Author:
Shuangquan LIU
;
Feijun ZHAO
;
Qiugui ZHANG
;
Xiangjun YAN
;
Lanfang LIU
;
Yimou WU
- Publication Type:Journal Article
- Keywords:
Treponema pallidum;
Laminin-binding adhesin;
Tp0751;
Recombinant protein;
Im-munocompetence
- From:
Chinese Journal of Microbiology and Immunology
2009;29(7):612-615
- CountryChina
- Language:Chinese
-
Abstract:
Objective To express Tp0751 laminin-binding adhesion of Treponema pallidum (T. pallidum) ,and assess the immunocompetence. Methods The Tp0751 ORF without upstream non-cod-ing region was ligated into the expression vector pET-28a( + ), and expressed in E. coli R2566. Its immuno-gen was analyzed by Western blot and ELISA. Results A fusion protein with molecular weight about 26×103 was attained after expression and purification. Western blot proved that the recombinant protein can specifically react with T. palliclum IgG positive sera. Specific humoral response were elicited after introducing recombinant protein in Zealand rabbit and the specific antibody titer was above 1:10 2400 detected by indi-rect ELISA. Conclusion The expressed recombinant protein showed excellent immunoeompetence, and the results lay the foundation for the research on its function to T. paUidum infection.
