文献类型： 外文期刊

作者： Du, L. ¹ ; Liu, F. ³ ; Ju, X. ² ; Huo, G. ¹ ;

作者机构： 1.NE Agr Univ, Minist Educ, Key Lab Dairy Sci, Harbin 150030, Peoples R China

2.Nanjing Univ Finance & Econ, Coll Food Sci & Engn, Nanjing, Peoples R China

3.Jiangsu Acad Agr Sci, Inst Agr Prod Proc, Nanjing, Peoples R China

关键词： adhesion;lactic acid bacteria;ligand fishing;protein domain;Western blot

期刊名称：LETTERS IN APPLIED MICROBIOLOGY （ 影响因子：2.858； 五年影响因子：2.776 ）

ISSN： 0266-8254

年卷期： 2010 年 51 卷 4 期

页码：

收录情况： SCI

摘要： Aims: This work aims to investigate the binding capability of certain domains at N terminus of the protein NP_785232 of Lactobacillus plantarum to Caco-2 cells and to test the usage of affinity chromatography to isolate the human mucus component that interacts with them. Methods and Results: Recombinant proteins containing the first and both the first and second domains at N terminus of NP_785232 fused to a His tag were constructed and used to bind the Caco-2 cells. The interacting molecule from human mucus was isolated by affinity chromatography through immobilizing the recombinant proteins onto a Sepharose matrix. It was found both recombinant proteins could block the adhesion of Lact. plantarum to Caco-2 cells and bind to a human mucus component. Conclusions: The first and both the first and second domains at N terminus of the protein NP_785232 have the capability to adhere Caco-2 cells and by affinity chromatography, an interacting UV-absorbing component from human mucus was isolated. Significance and Impact of the Study: The protein domains characterized in this study may be displayed on probiotics to promote adhesion, and further characterization of the human mucus component might be helpful to identify host factors required for prolonging probiotics persistence in the gastrointestinal tract.