BACTERIAL INTERNALIZATION MEDIATED BY BETA-1 CHAIN INTEGRINS IS DETERMINED BY LIGAND AFFINITY AND RECEPTOR DENSITY
BACTERIAL INTERNALIZATION MEDIATED BY BETA-1 CHAIN INTEGRINS IS DETERMINED BY LIGAND AFFINITY AND RECEPTOR DENSITY
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DOI：
10.1002/j.1460-2075.1993.tb05837.x
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发表时间：
1993-05-01
期刊：
影响因子：
11.4
通讯作者：
ISBERG, RR
中科院分区：
文献类型：
--
作者：
VANNHIEU, GT;ISBERG, RR
细菌与β1链整合素受体的结合导致细菌黏附或被培养细胞摄取(Isberg，1991)。在这份报告中，我们发现涂有高亲和力的β1链整合素家族配体的金黄色葡萄球菌可以有效地内化，而包被低亲和力配体的细菌内化能力很差。α5beta1整合素的过量生产提高了细菌内化的效率，表明摄取效率与受体的表达水平直接相关。通过使用胶乳小球或涂有针对α5beta1整合素的单抗的金黄色葡萄球菌，观察到受体-配体相互作用的亲和力与细菌内化速度之间大致呈半对数关系。有证据表明，细菌的高亲和力结合使微生物能够有效地与细胞基侧表面的受体-配体相互作用竞争。
Binding of bacteria to beta1 chain integrin receptors results in either bacterial adherence or uptake by cultured cells (Isberg, 1991). In this report we show that Staphylococcus aureus coated with high affinity ligands for the beta1 chain integrin family can be internalized efficiently, whereas bacteria coated with low affinity ligands are poorly internalized. Overproduction of the alpha5beta1 integrin increased the efficiency of bacterial internalization, indicating that the uptake efficiency is directly related to the level of expression of the receptor. By using latex beads or S.aureus coated with mAbs directed against the alpha5beta1 integrin, a roughly semi-logarithmic correlation was observed between the affinity of the receptor - ligand interaction and the rate of bacterial internalization. Evidence is presented that high affinity binding of the bacterium allows the microorganism to compete efficiently with receptor-ligand interactions at the basolateral surface of the cell.