Phan-Thanh L, Gormon T
Laboratoire de Pathologie, Infectieuse et Immunologie, Institut National de la Recherche Agronomique, Nonzilly-Tours, France.
Electrophoresis. 1997 Aug;18(8):1464-71. doi: 10.1002/elps.1150180821.
The proteins induced by the different stress conditions in Listeria monocytogenes were analyzed by two-dimensional (2-D) electrophoresis with the aid of a computerized 2-D gel analysis system. The stress conditions imposed were pH 4, pH 10, 0.015% sodium, dodecyl sulfate (SDS), 0.03% sodium deoxycholate and 4% ethanol. As previously seen for heat shock and cold shock, more than half of the proteins normally synthesized by Listeria cells were repressed under these stress conditions. Conversely, the synthesis of a great number of proteins was increased and novel proteins appeared upon stress. Each stress factor induced a specific set of proteins. These stress proteins were characterized by their apparent molecular mass and isoelectric point. No universal stress proteins were found to be common to all the stresses studied, while some proteins were commonly induced by two or three stress conditions. The degree of dissimilarity in stress responses was best illustrated by the induction of only two proteins common to exposure to the two detergents SDS and sodium deoxycholate. This work together with that on heat and cold shock, constitutes the basic step for the identification of stress proteins in Listeria.
利用计算机二维凝胶分析系统，通过二维（2-D）电泳对不同应激条件下单核细胞增生李斯特菌诱导产生的蛋白质进行了分析。施加的应激条件为pH 4、pH 10、0.015%的十二烷基硫酸钠（SDS）、0.03%的脱氧胆酸钠和4%的乙醇。正如之前在热休克和冷休克中所观察到的，在这些应激条件下，李斯特菌细胞正常合成的蛋白质中有一半以上受到抑制。相反，大量蛋白质的合成增加，并且在应激时出现了新的蛋白质。每种应激因素都诱导产生一组特定的蛋白质。这些应激蛋白通过其表观分子量和等电点进行表征。在所研究的所有应激中，未发现通用的应激蛋白，而有些蛋白质是由两种或三种应激条件共同诱导产生的。应激反应的差异程度通过仅诱导出两种同时暴露于两种去污剂SDS和脱氧胆酸钠时共有的蛋白质得到了最佳体现。这项工作以及热休克和冷休克方面的工作，构成了鉴定李斯特菌应激蛋白的基本步骤。
