Anchorless cell surface proteins function as laminin-binding adhesins in Lactobacillus rhamnosus FSMM22
Anchorless cell surface proteins function as laminin-binding adhesins in Lactobacillus rhamnosus FSMM22
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DOI：
10.1093/femsle/fnx056
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发表时间：
2017-03-01
影响因子：
2.1
通讯作者：
Fukuda, Kenji
中科院分区：
文献类型：
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作者：
Aryantini, Ni Putu Desy;Kondoh, Daisuke;Fukuda, Kenji
用1M氯化锂溶液从鼠李糖乳杆菌FSMM22中提取无锚细胞表面蛋白。在体外，失去无锚定的CSP导致与构成细胞外基质糖蛋白-层粘连蛋白结合的FSMM22细胞减少2倍。提取液中DNA结合蛋白HU、3-磷酸甘油醛脱氢酶、乳酸脱氢酶和30S核糖体蛋白S19(RPSS)经质谱鉴定为层粘连蛋白结合粘附素。免疫组织化学证实RPSS存在于细胞表面。我们的发现有力地表明，无锚CSP可以增强细菌对宿主的黏附。
Anchorless cell surface proteins (CSPs) were extracted with 1 M lithium chloride solution from Lactobacillus rhamnosus FSMM22. Loss of the anchorless CSPs resulted in a 2-fold decrease in FSMM22 cells bound to a constitutive extracellular matrix glycoprotein, laminin, in vitro. DNA-binding protein HU, glyceraldehyde-3-phosphate dehydrogenase, lactate dehydrogenase and 30S ribosomal protein S19 (RpsS) were identified by mass spectrometry in the extract as laminin-binding adhesins. Among the four proteins, RpsS was immunohistochemically confirmed to exist on the cell surface. Our findings strongly suggest that anchorless CSPs can enhance bacterial adhesion to the host.