Binding of Escherichia coli to fibronectin. A mechanism of tissue adherence.
Binding of Escherichia coli to fibronectin. A mechanism of tissue adherence.
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DOI：
10.1016/s0021-9258(17)42689-5
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发表时间：
1984-12
期刊：
影响因子：
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通讯作者：
G. Froman;L. Switalski;A. Faris;Torkel Wadström;M. Höök
中科院分区：
文献类型：
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作者：
G. Froman;L. Switalski;A. Faris;Torkel Wadström;M. Höök
17株产肠毒素大肠杆菌中有4株与125 I-纤维连接蛋白结合。这种结合，这是抑制未标记的纤连蛋白，但不是由其他蛋白质，似乎涉及两类受体，其中之一可逆地结合配体。与两类受体的存在一致，细菌结合到纤连蛋白分子的至少两个不同位点，一个是氨基末端结构域，其也含有革兰氏阳性细菌的结合位点，另一个位于该结构域之外。急诊表达纤连蛋白受体的大肠杆菌菌株粘附于成纤维细胞和纤连蛋白，但不粘附于卵清蛋白包被的盖玻片。在40 ℃下生长的细菌不表达纤连蛋白受体，也不粘附于任何一种基质。受体与纤连蛋白的饱和阻断了与纤连蛋白包被的盖玻片和培养的成纤维细胞的粘附。这些数据表明，与纤连蛋白的结合代表了E.杆菌
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.