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目的提取和鉴定干酪乳杆菌LC2W表面黏附相关蛋白,初步探索LC2W对胃癌细胞MKN-45细胞的黏附机制。方法LiCl处理、Sephadex G-75柱层析分离提取LC2W的表面蛋白,用黏附试验、电镜观察和SDS-PAGE电泳进行黏附相关蛋白的鉴定。结果LC2W经LiCl处理后,扫描电镜结果发现菌体表面粗糙但仍完整,黏附试验表明其对MKN-45细胞的黏附能力显著降低。提取到的表面蛋白的分子量分别为41.6、63.5、66.2 kDa。粗提物经柱层析后发现分子量为41.6 kDa的组分可以明显增强经LiCl处理过的菌体的黏附,而与未经处理的菌体黏附情况类似。结论表面蛋白参与了LC2W对MKN-45细胞的黏附,其主要活性成分的分子量为41.6 kDa。
Objective To extract and identify the surface adhesion proteins of Lactobacillus casei LC2W and to explore the mechanism of LC2W adhesion to gastric cancer cell line MKN-45. Methods The surface protein of LC2W was isolated by Sephadex G-75 column chromatography with LiCl and identified by adhesion test, electron microscope and SDS-PAGE electrophoresis. Results LC2W treated with LiCl showed that the cell surface was rough but still intact after scanning electron microscopy. The adhesion test showed that the adhesion of MK2 cells to MKN-45 cells was significantly reduced. The molecular weights of the extracted surface proteins were 41.6, 63.5 and 66.2 kDa, respectively. After the crude extract was subjected to column chromatography, it was found that the molecular weight of 41.6 kDa could significantly enhance the adhesion of LiCl-treated cells, which was similar to that of untreated cells. Conclusions Surface proteins are involved in the adhesion of LC2W to MKN-45 cells. The molecular weight of the major active ingredient is 41.6 kDa.