Fröman G, Switalski L M, Faris A, Wadström T, Höök M
J Biol Chem. 1984 Dec 10;259(23):14899-905.
Four out of 17 enterotoxigenic strains of Escherichia coli isolated from infantile diarrhea bound 125I-fibronectin. This binding, which was inhibited by unlabeled fibronectin but not by other proteins, appears to involve two classes of receptors, one of which binds the ligand reversibly. Consistent with the presence of two classes of receptors the bacteria bound to at least two distinct sites of the fibronectin molecule, one being the amino-terminal domain which also contains the binding sites for Gram-positive bacteria and the other located outside this domain. The E. coli strain expressing fibronectin receptors adhered to fibroblasts and to fibronectin but not to ovalbumin-coated coverslips. Bacteria grown at 40 degrees C did not express fibronectin receptors and did not adhere to either substrate. Saturation of receptors with fibronectin blocked adhesion to both fibronectin-coated coverslips and to cultured fibroblasts. These data suggest that binding to fibronectin represents a mechanism of tissue adherence of E. coli.
从婴儿腹泻中分离出的17株产肠毒素大肠杆菌中，有4株能结合125I-纤连蛋白。这种结合可被未标记的纤连蛋白抑制，但不能被其他蛋白质抑制，似乎涉及两类受体，其中一类可逆地结合配体。与两类受体的存在相一致，细菌与纤连蛋白分子的至少两个不同位点结合，一个是氨基末端结构域，它也包含革兰氏阳性菌的结合位点，另一个位于该结构域之外。表达纤连蛋白受体的大肠杆菌菌株能黏附于成纤维细胞和纤连蛋白，但不能黏附于卵清蛋白包被的盖玻片。在40℃培养的细菌不表达纤连蛋白受体，也不黏附于任何一种底物。用纤连蛋白使受体饱和可阻断对纤连蛋白包被盖玻片和培养成纤维细胞的黏附。这些数据表明，与纤连蛋白的结合代表了大肠杆菌的一种组织黏附机制。
