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首页> 外文期刊>Journal of Clinical Microbiology >Characterization of a tick isolate of Borrelia burgdorferi that possesses a major low-molecular-weight surface protein.
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Characterization of a tick isolate of Borrelia burgdorferi that possesses a major low-molecular-weight surface protein.

机译：伯氏疏螺旋体的壁虱分离株的特征，该分离株具有主要的低分子量表面蛋白。

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摘要

An unusual strain of Borrelia burgdorferi (DN 127 cl 9-2) that was isolated from an Ixodes pacificus tick did not react with monoclonal antibodies (MAbs) to OspA and OspB surface proteins, which are found in most U.S. strains. The strain exhibited an abundant protein with an apparent molecular weight of 25,000 (25K protein). A MAb, 86 DN-1, that was prepared to the 25K protein was used in studies on the effect of proteases on the intact spirochetes, immune electron microscopy, and Western blot (immunoblot) analyses; the results indicated that the low-molecular-weight protein was an apparent surface protein that was loosely attached to the spirochete. Five tick isolates from California possessed low-molecular-weight proteins in the 20,000- to 25,000-molecular-weight range that reacted with the 86 DN-1 MAb. The 25K protein of DN 127 cl 9-2 was unaffected by prolonged in vitro passage of cultures in BSK II medium, while the low-molecular-weight proteins of the other strains of B. burgdorferi from California either decreased in quantity or became undetectable on long-term in vitro passage.
机译：从太平洋小tick中分离出的不寻常的伯氏疏螺旋体（Borrelia burgdorferi）（DN 127 cl 9-2）不会与针对OspA和OspB表面蛋白的单克隆抗体（MAb）反应，而大多数美国菌株中都存在这种抗体。该菌株显示出丰富的蛋白质，其表观分子量为25,000（25K蛋白质）。针对25K蛋白制备的MAb（86 DN-1）用于研究蛋白酶对完整螺旋体的影响，免疫电子显微镜和Western blot（免疫印迹）分析。结果表明，低分子量蛋白是一种明显的表面蛋白，松散地附着在螺旋体上。来自加利福尼亚的五个壁虱分离株具有在20000至25,000分子量范围内的低分子量蛋白质，可与86 DN-1 MAb反应。 DN 127 cl 9-2的25K蛋白不受BSK II培养基中体外培养时间的延长的影响，而来自加利福尼亚州的其他B. burgdorferi菌株的低分子量蛋白要么数量减少，要么在检测不到长期体外传代。

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