Ishibashi Y, Claus S, Relman D A
Department of Microbiology and Immunology, Stanford University School of Medicine, California 94305.
J Exp Med. 1994 Oct 1;180(4):1225-33. doi: 10.1084/jem.180.4.1225.
Bordetella pertussis, the causative agent of whooping cough, adheres to human monocytes/macrophages by means of a bacterial surface-associated protein, filamentous hemagglutinin (FHA) and the leukocyte integrin, complement receptor 3 (CR3, alpha M beta 2, CD11b/CD18). We show that an FHA Arg-Gly-Asp site induces enhanced B. pertussis binding to monocytes, and that this enhancement is blocked by antibodies directed against CR3. Enhancement requires a monocyte signal transduction complex, composed of leukocyte response integrin (alpha? beta 3) and integrin-associated protein (CD47). This complex is known to upregulate CR3 binding activity. Thus, a bacterial pathogen enhances its own attachment to host cells by coopting a host cell signaling pathway.
百日咳博德特氏菌是百日咳的病原体，它借助一种细菌表面相关蛋白丝状血凝素（FHA）以及白细胞整合素补体受体3（CR3，αMβ2，CD11b/CD18）黏附于人类单核细胞/巨噬细胞。我们发现，FHA的精氨酸-甘氨酸-天冬氨酸位点可增强百日咳博德特氏菌与单核细胞的结合，并且这种增强作用可被针对CR3的抗体阻断。增强作用需要一个由白细胞反应整合素（αⅡbβ3）和整合素相关蛋白（CD47）组成的单核细胞信号转导复合物。已知该复合物可上调CR3的结合活性。因此，一种细菌病原体通过利用宿主细胞信号通路来增强自身与宿主细胞的附着。
