Interaction of Escherichia coli heat-stable enterotoxin B with rat intestinal epithelial cells and membrane lipids.
Interaction of Escherichia coli heat-stable enterotoxin B with rat intestinal epithelial cells and membrane lipids.
复制标题
大肠杆菌热稳定肠毒素 B 与大鼠肠上皮细胞和膜脂的相互作用。
DOI：
10.1111/j.1574-6968.1999.tb13455.x
复制
发表时间：
1999
影响因子：
2.1
通讯作者：
Dreyfus,LA
中科院分区：
文献类型：
--
作者：
Chao,KL;Dreyfus,LA
125 I标记的大肠杆菌热稳定性肠毒素B与大鼠肠上皮细胞的结合是不饱和的和非特异性的，其浓度远高于介导生物事件所需的浓度。在与肠细胞相互作用后，约 50-80% 的热稳定性肠毒素 B 仍与细胞稳定结合，这意味着它被分配到膜中和/或被细胞内化。该毒素以不同的亲和力与从肠上皮细胞分离的脂质、磷脂、糖脂、中性脂质结合，并与含有带负电荷的脂质的模型膜囊泡结合。这些结果表明，热稳定性肠毒素 B 利用膜双层，而不是表面蛋白或糖蛋白来调节毒素诱导的肠毒性。
The binding of125I-labeledEscherichia coliheat-stable enterotoxin B to rat intestinal epithelial cells was unsaturable and nonspecific, at concentrations well above that required to mediate biological events. Following its interaction with intestinal cells, ~50–80% of heat-stable enterotoxin B remained stably associated with the cells, implying that it was partitioned into the membrane and/or internalized by the cell. The toxin bound with different affinities to lipids isolated from intestinal epithelial cells, phospholipids, glycolipids, neutral lipids and to model membrane vesicles containing negatively charged lipids. These results indicate that heat-stable enterotoxin B utilizes the membrane bilayer, rather than a surface protein or glycoprotein in modulating toxin-induced enterotoxicity.