RECOGNITION OF A BACTERIAL ADHESIN BY AN INTEGRIN - MACROPHAGE CR3 (ALPHA-M-BETA-2, CD11B CD18) BINDS FILAMENTOUS HEMAGGLUTININ OF BORDETELLA-PERTUSSIS
RECOGNITION OF A BACTERIAL ADHESIN BY AN INTEGRIN - MACROPHAGE CR3 (ALPHA-M-BETA-2, CD11B CD18) BINDS FILAMENTOUS HEMAGGLUTININ OF BORDETELLA-PERTUSSIS
复制标题
DOI：
10.1016/0092-8674(90)90701-f
复制
发表时间：
1990-06-29
期刊：
影响因子：
64.5
通讯作者：
WRIGHT, SD
中科院分区：
文献类型：
--
作者：
RELMAN, D;TUOMANEN, E;WRIGHT, SD
在百日咳过程中，百日咳杆菌与肺泡巨噬细胞和呼吸道上皮细胞上的其他白细胞相互作用。我们在这里报告的机制，这些细菌粘附在体外人类巨噬细胞。整个细菌通过两种蛋白质粘附，即丝状血凝素（FHA）和百日咳毒素，其中任何一种都足以介导粘附。FHA与巨噬细胞上的两类分子、含半乳糖的糖缀合物和整联蛋白CR 3（α M β 2，CD 11b/CD 18）相互作用。CR 3和FHA之间的相互作用涉及识别FHA中1097-1099位的Arg-Gly-Asp（RGD）序列。这项研究表明，细菌粘附可以基于细菌粘附素RGD序列与整合素的相互作用，并且细菌粘附素可以具有真核细胞外基质蛋白的多个结合位点特征。
During the course of whooping cough, Bordetella pertussis interacts with alveolar macrophages and other leukocytes on the respiratory epithelium. We report here mechanisms by which these bacteria adhere to human macrophages in vitro. Whole bacteria adhere by means of two proteins, filamentous hemagglutinin (FHA) and pertussis toxin, either of which is sufficient to mediate adherence. FHA interacts with two classes of molecules on macrophages, galactose-containing glycoconjugates and the integrin CR3 (.alpha.M.beta.2, CD11b/CD18). The interaction between CR3 and FHA involves recognition of the Arg-Gly-Asp (RGD) sequence at positions 1097-1099 in FHA. This study demonstrates that bacterial adherence can be based on the interaction of a bacterial adhesin RGD sequence with an integrin and that bacterial adhesins can have multiple binding sites characteristic of eukaryotic extracellular matrix proteins.