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首页> 外文期刊>Infection and immunity >Molecular cloning and characterization of a 35.5-kilodalton lipoprotein of Treponema pallidum.
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Molecular cloning and characterization of a 35.5-kilodalton lipoprotein of Treponema pallidum.

机译：梅毒螺旋体35.5-千达尔顿脂蛋白的分子克隆和表征

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摘要

A clone expressing a 35.5-kDa recombinant treponemal protein was isolated from a genomic DNA library constructed from Treponema pallidum street strain 14. Polyclonal antiserum raised against the recombinant protein reacted with a corresponding native protein of comparable size in T. pallidum that is specific to the pathogenic treponemes. Radiolabeling of the recombinant protein with [3H]palmitate demonstrated that it is lipid modified. Like other recently characterized T. pallidum lipoproteins, the 35.5-kDa lipoprotein partitioned into the detergent phase from T. pallidum cells fractionated with Triton X-114, suggesting that it is an integral membrane protein. Processing of the recombinant 35.5-kDa lipoprotein from a precursor form to a smaller mature form was not evident in pulse-chase experiments. However, pretreatment of Escherichia coli cells expressing the 35.5-kDa lipoprotein with inhibitors of protein processing or translocation revealed the existence of a higher-molecular-mass precursor. Gene fusion studies with the transposon TnphoA demonstrated the presence of an export signal in the 35.5-kDa lipoprotein that promotes the extracytoplasmic localization of a 35.5-kDa lipoprotein-PhoA hybrid.
机译：从梅毒螺旋体街菌株14构建的基因组DNA文库中分离出表达35.5-kDa重组蛋白的克隆。针对重组蛋白产生的多克隆抗血清与梅毒螺旋体中具有相当大小的相应天然蛋白反应，该天然蛋白特异于致病性色氨酸。用[3H]棕榈酸酯对重组蛋白进行放射性标记，表明该蛋白经脂质修饰。像其他最近鉴定过的梅毒螺旋体脂蛋白一样，35.5 kDa脂蛋白从用Triton X-114分离的梅毒螺旋体细胞分配到去污剂相中，表明它是一种完整的膜蛋白。在脉冲追逐实验中，重组35.5-kDa脂蛋白从前体形式加工成较小的成熟形式的过程并不明显。但是，用蛋白质加工或易位抑制剂对表达35.5-kDa脂蛋白的大肠杆菌细胞进行预处理，发现存在较高分子量的前体。转座子TnphoA的基因融合研究表明，在35.5-kDa脂蛋白中存在一个输出信号，该信号促进了35.5-kDa脂蛋白-PhoA杂种的胞外定位。

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