MULTIPLE BETA-1-CHAIN INTEGRINS ARE RECEPTORS FOR INVASIN, A PROTEIN THAT PROMOTES BACTERIAL PENETRATION INTO MAMMALIAN-CELLS
MULTIPLE BETA-1-CHAIN INTEGRINS ARE RECEPTORS FOR INVASIN, A PROTEIN THAT PROMOTES BACTERIAL PENETRATION INTO MAMMALIAN-CELLS
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DOI：
10.1016/0092-8674(90)90099-z
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发表时间：
1990-03-09
期刊：
影响因子：
64.5
通讯作者：
LEONG, JM
中科院分区：
文献类型：
--
作者：
ISBERG, RR;LEONG, JM
促进细胞内细菌进入非吞噬细胞的哺乳动物细胞受体尚未确定。我们在此表明，细胞粘附受体整合素超家族的多个成员在细菌渗透到哺乳动物细胞之前与假结核耶尔森氏菌入侵蛋白结合。粗洗涤剂提取物的亲和层析证明含有亚基结构α3.β1、α4.β1、α5.β1和α6.β1的整联蛋白与固定化的侵袭素结合。此外，含有分离的整联蛋白的磷脂囊泡能够附着在侵袭素上。还证明了侵入素与已鉴定的整联蛋白受体结合的特异性，因为免疫探针和磷脂重构研究表明α2.β1整联蛋白、β2链整联蛋白和玻连蛋白受体(αv.β3)不参与细胞对侵入素的附着。
Mammalian cell receptors that promote entry of intracellular bacteria into nonphagocytic cells have not been identified. We show here that multiple members of the integrin superfamily of cell adhesion receptors bind the Yersinia pseudotuberculosis invasin protein prior to bacterial penetration into mammalian cells. Affinity chromatography of crude detergent extracts demonstrated that integrins containing the subunit structures .alpha.3.beta.1, .alpha.4.beta.1, .alpha.5.beta.1, and .alpha.6.beta.1 bound to immobilized invasin. Furthermore, phospholipid vesicles containing isolated integrin proteins were able to attach to invasin. Specificity for invasin binding to the identified integrin receptors was also demonstrated, as immunoprobing and phospholipid reconstitution studies showed that the .alpha.2.beta.1 integrin, .beta.2 chain integrins, and vitronectin receptor (.alpha.v.beta.3) were not involved in cellular attachment to invasin.