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首页> 外文期刊>Infection and immunity >Molecular cloning and expression of Chlamydia trachomatis major outer membrane protein antigens in Escherichia coli.
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Molecular cloning and expression of Chlamydia trachomatis major outer membrane protein antigens in Escherichia coli.

机译：沙眼衣原体主要外膜蛋白抗原的分子克隆和表达。

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DNA obtained from Chlamydia trachomatis (serovar L2) was partially digested with DNase I and inserted into the beta-galactosidase gene of bacteriophage lambda gt11. Seven recombinants were selected that produced immunoreactive fusion proteins which were detected with anti-C. trachomatis rabbit serum. One recombinant, designated lambda gt11/L2/33, reacted with various monoclonal antibodies that recognize species-, subspecies-, and type-specific determinants on the chlamydial major outer membrane protein (MOMP). Immunoblot analysis of a lambda gt11/L2/33 lysogen revealed a fusion protein that expressed a approximately 15,000-dalton carboxyl-terminal peptide of the chlamydial MOMP. This moiety of the MOMP possesses epitopes responsible for each of the unique reactivities demonstrated by anti-MOMP monoclonal antibodies. The lambda gt11/L2/33 recombinant contained a 1.1-kilobase DNA insert which hybridized to DNA isolated from each of the 15 C. trachomatis serovars.
机译：从沙眼衣原体（血清型L2）获得的DNA用DNase I进行部分消化，并插入到λ噬菌体gt11的β-半乳糖苷酶基因中。选择了七个产生免疫反应性融合蛋白的重组体，所述融合蛋白用抗C检测。沙眼兔血清。一种重组体称为gt11 / L2 / 33，与各种单克隆抗体反应，这些抗体识别衣原体主要外膜蛋白（MOMP）上的物种，亚种和类型特异性决定簇。 λgt11/ L2 / 33溶原菌的免疫印迹分析显示融合蛋白表达了衣原体MOMP的大约15,000道尔顿的羧基末端肽。 MOMP的此部分具有表位，这些表位负责抗MOMP单克隆抗体证明的每个独特的反应性。 λgt11 / L2 / 33重组体包含一个1.1碱基碱基的DNA插入片段，该插入片段与从15个沙眼衣原体血清型中的每一个分离的DNA杂交。

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