Department of Infection Biology, Leibniz Institute for Natural Product Research and Infection Biology, Jena, Germany.
J Infect Dis. 2010 Aug 15;202(3):490-8. doi: 10.1086/653825.
Lyme disease-causing Borrelia burgdorferi spirochetes express up to 5 complement regulator-acquiring surface proteins (CRASPs). To better define how CRASP-1 contributes to infection, we aimed to identify novel CRASP-1-binding host proteins. Here, we identified a number of novel human CRASP-1-binding proteins, including bone morphogenic protein 2, collagen I, collagen III, collagen IV, fibronectin, laminin, and plasminogen. The plasminogen-binding regions were located in 2 separate regions of CRASP-1. Our results demonstrated that plasminogen-bound CRASP-1 can be converted to plasmin by the urokinase-type plasminogen activator and that proteolytically active plasmin cleaves the synthetic chromogenic substrate S-2251 and the natural substrate fibrinogen. In conclusion, CRASP-1 is a multifunctional protein of B. burgdorferi that binds to several human extracellular matrix proteins and plasminogen. These interactions may contribute to adhesion, bacterial colonization, and organ tropism and may allow dissemination of B. burgdorferi in the host.
莱姆病病原体伯氏疏螺旋体表达多达 5 种补体调控蛋白获取表面蛋白（CRASPs）。为了更好地定义 CRASP-1 如何促进感染，我们旨在鉴定新的 CRASP-1 结合宿主蛋白。在这里，我们鉴定了一些新的人类 CRASP-1 结合蛋白，包括骨形态发生蛋白 2、胶原蛋白 I、胶原蛋白 III、胶原蛋白 IV、纤连蛋白、层粘连蛋白和纤溶酶原。纤溶酶原结合区域位于 CRASP-1 的 2 个不同区域。我们的结果表明，纤溶酶原结合的 CRASP-1 可以被尿激酶型纤溶酶原激活物转化为纤溶酶，并且具有蛋白水解活性的纤溶酶可切割合成显色底物 S-2251 和天然底物纤维蛋白原。总之，CRASP-1 是伯氏疏螺旋体的一种多功能蛋白，可与几种人类细胞外基质蛋白和纤溶酶原结合。这些相互作用可能有助于黏附、细菌定植和器官趋向性，并可能允许伯氏疏螺旋体在宿主中传播。
