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首页> 外文期刊>Infection and immunity >The Enolase of Borrelia burgdorferi Is a Plasminogen Receptor Released in Outer Membrane Vesicles
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The Enolase of Borrelia burgdorferi Is a Plasminogen Receptor Released in Outer Membrane Vesicles

机译：伯氏疏螺旋体的烯醇酶是在外膜囊泡中释放的纤溶酶原受体。

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The agent of Lyme disease, Borrelia burgdorferi, has a number of outer membrane proteins that are differentially regulated during its life cycle. In addition to their physiological functions in the organism, these proteins also likely serve different functions in invasiveness and immune evasion. In borreliae, as well as in other bacteria, a number of membrane proteins have been implicated in binding plasminogen. The activation and transformation of plasminogen into its proteolytically active form, plasmin, enhances the ability of the bacteria to disseminate in the host. Outer membrane vesicles of B. burgdorferi contain enolase, a glycolytic-cycle enzyme that catalyzes 2-phosphoglycerate to form phosphoenolpyruvate, which is also a known plasminogen receptor in Gram-positive bacteria. The enolase was cloned, expressed, purified, and used to generate rabbit antienolase serum. The enolase binds plasminogen in a lysine-dependent manner but not through ionic interactions. Although it is present in the outer membrane, microscopy and proteinase K treatment showed that enolase does not appear to be exposed on the surface. However, enolase in the outer membrane vesicles is accessible to proteolytic degradation by proteinase K. Samples from experimentally and tick-infected mice and rabbits as well as from Lyme disease patients exhibit recognition of enolase in serologic assays. Thus, this immunogenic plasminogen receptor released in outer membrane vesicles could be responsible for external proteolysis in the pericellular environment and have roles in nutrition and in enhancing dissemination.
机译：莱姆病的病原体伯氏疏螺旋体具有许多在其生命周期中受到不同调节的外膜蛋白。除了它们在生物体中的生理功能外，这些蛋白质还可能在侵袭性和免疫逃避中发挥不同的功能。在疏螺旋体以及其他细菌中，许多膜蛋白已牵涉结合纤溶酶原。纤溶酶原的活化和转化成其蛋白水解活性形式的纤溶酶可增强细菌在宿主中的传播能力。伯氏疏螺旋体的外膜囊泡含有烯醇酶，一种糖酵解循环酶，催化2-磷酸甘油酸酯形成磷酸烯醇丙酮酸，这也是革兰氏阳性细菌中已知的纤溶酶原受体。将该烯醇酶克隆，表达，纯化，并用于产生兔抗烯醇酶血清。烯醇化酶以赖氨酸依赖性方式结合纤溶酶原，但不通过离子相互作用结合。尽管它存在于外膜中，但显微镜检查和蛋白酶K处理显示烯醇酶似乎未暴露于表面。但是，外膜囊泡中的烯醇化酶可通过蛋白酶K进行蛋白水解降解。在血清学检测中，实验性和tick感染的小鼠和兔子以及莱姆病患者的样品均显示出烯醇化酶的识别。因此，这种释放在外膜囊泡中的免疫原性纤溶酶原受体可能负责细胞周围环境中的外部蛋白水解，并在营养和增强传播方面具有作用。

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