Implication of an outer surface lipoprotein in adhesion of Bifidobacterium bifidum to Caco-2 cells
Implication of an outer surface lipoprotein in adhesion of Bifidobacterium bifidum to Caco-2 cells
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DOI：
10.1128/aem.00124-08
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发表时间：
2008-08-01
影响因子：
4.4
通讯作者：
Parini, Carlo
中科院分区：
文献类型：
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作者：
Guglielmetti, Simone;Tamagnini, Isabella;Parini, Carlo
我们发现人肠道分离株双歧双歧杆菌MIMBb75与Caco-2细胞有很强的粘附性。蛋白酶K和氯化锂处理表明，蛋白质在MIMBb75与Caco-2细胞的黏附中起关键作用。通过对细胞壁相关蛋白的研究，我们确定了一种表面蛋白，我们将其标记为BopA。我们对该蛋白进行了层析纯化，发现其具有促进Caco-2细胞黏附的功能。在对该蛋白和球霉素编码基因的电子分析中，实验表明BopA是一种半胱氨酸锚定的脂蛋白，表达为前体多肽。数据库搜索表明，BopA在生物学上似乎是ABC运输系统中的寡肽/三肽-溶质结合蛋白。我们在另外8株两裂双歧杆菌高黏附性菌株中发现了一种与BopA及其基因相对应的蛋白质。最后，我们发现双歧杆菌MIMBb75和BopA对Caco-2上皮细胞产生IL-8有影响。BOPA是迄今为止第一个被描述为直接参与双歧杆菌与Caco-2细胞的黏附并显示免疫调节活性的蛋白质。
We found that the human intestinal isolate Bifidobacterium bifidum MIMBb75 strongly adhered to Caco-2 cells. Proteinase K and lithium chloride treatments showed that proteins play a key role in MIMBb75 adhesion to Caco-2 cells. By studying the cell wall-associated proteins, we identified a surface protein, which we labeled BopA. We purified the protein chromatographically and found that it functioned as an adhesion promoter on Caco-2 cells. In silico analysis of the gene coding for this protein and globomycin experiments showed that BopA is a cysteine-anchored lipoprotein expressed as a precursor polypeptide. A database search indicated that BopA appears to function biologically as an oligopeptide/tripeptide-solute-binding protein in the ABC transport system. We discovered a protein corresponding to BopA and its gene in eight other highly adherent B. bifidum strains. Finally, we found that B. bifidum MIMBb75 and BopA affected the production of interleukin-8 in Caco-2 epithelial cells. BopA is the first protein described to date to be directly involved in the adhesion of bifidobacteria to Caco-2 cells and to show immunomodulatory activity.