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首页> 外文期刊>Infection and immunity >Characterization of native and recombinant 75-kilodalton immunogens from Chlamydia trachomatis serovar L2.
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Characterization of native and recombinant 75-kilodalton immunogens from Chlamydia trachomatis serovar L2.

机译:沙眼衣原体血清型L2的天然和重组75-千达尔顿免疫原的表征。

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A 75-kilodalton (kDa) immunogen from Chlamydia trachomatis serovar L2 was characterized. The 75-kDa protein was localized in the cytoplasm of chlamydiae and was shown to be a protein synthesized early in the developmental cycle of chlamydiae. A gene library was made by the recombinant DNA technique, using the expression vectors pEX1, pEX2, and pEX3. From this library one clone was found which reacted with a monoclonal antibody against the 75-kDa immunogen of C. trachomatis. The 75-kDa protein produced by the recombinant Escherichia coli was expressed independently of the promoter for the hybrid protein cro-betagalactosidase. Thus it is not produced as a fusion protein. Epitope mapping of the 75-kDa protein from C. trachomatis L2 and from the recombinant E. coli performed by Staphylococcus aureus V8 protease digestion showed that the two proteins are identical. Furthermore, patient sera reacted with both proteins.
机译:表征了来自沙眼衣原体血清型L2的75千达尔顿(kDa)免疫原。 75-kDa蛋白定位于衣原体的细胞质中,并被证明是在衣原体发育周期的早期合成的蛋白。使用表达载体pEX1,pEX2和pEX3,通过重组DNA技术制备基因文库。从该文库中发现一个克隆,它与抗沙眼衣原体75-kDa免疫原的单克隆抗体反应。重组大肠杆菌产生的75 kDa蛋白的表达独立于杂合蛋白cro-β-半乳糖苷酶的启动子。因此,它不作为融合蛋白产生。金黄色葡萄球菌V8蛋白酶消化对沙眼衣原体L2和重组大肠杆菌中的75 kDa蛋白进行的表位作图表明,这两种蛋白是相同的。此外,患者血清与两种蛋白质反应。

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