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首页> 外文期刊>Infection and immunity >Immunologic characterization of a cloned fragment containing the species-specific epitope from the major outer membrane protein of Chlamydia trachomatis.
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Immunologic characterization of a cloned fragment containing the species-specific epitope from the major outer membrane protein of Chlamydia trachomatis.

机译：包含沙眼衣原体主要外膜蛋白中物种特异性表位的克隆片段的免疫学表征。

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摘要

A 183-bp fragment encoding variable domain IV (VD IV) of Chlamydia trachomatis serovar B major outer membrane protein (MOMP) (amino acids 273 to 333) and containing the species-specific epitope was cloned and expressed in Escherichia coli as a fusion protein with Schistosoma japonicum glutathione S-transferase (GST-VD IV). The fusion protein was affinity purified under nondenaturing conditions and used to immunize rabbits. Antisera were characterized by microimmunofluorescence, immunoblot, dot blot, peptide enzyme-linked immunosorbent, and in vitro neutralization assays. Antisera recognized MOMP from all 12 tested serovars of C. trachomatis but not from Chlamydia psittaci. In a dot blot assay, antisera bound to elementary bodies of serovars B, D, E, L2, and K in a strong fashion and to elementary bodies of serovars F, G, A, and H in a weak fashion but not to elementary bodies of serovars C, J, and I. High-resolution peptide mapping with synthetic overlapping serovar B MOMP peptides in a solid-phase enzyme-linked immunosorbent assay showed that immunization with GST-VD IV produced a serologic response that closely mimicked the response produced with purified serovar B elementary bodies. Antipeptide antibodies with strong binding to species- and subspecies-specific epitopes were elicited. Antisera were able to neutralize only those C. trachomatis serovars that bound antibodies in the dot blot assay. These results suggest that antigenic fragments from VD IV containing the species-specific epitope may be useful in the construction of a chlamydial vaccine for some but not all C. trachomatis serovars.
机译：克隆了一个183bp的片段，该片段编码沙眼衣原体血清型B主要外膜蛋白（MOMP）的可变域IV（VD IV）（氨基酸273至333）并含有物种特异性表位，并作为融合蛋白在大肠杆菌中表达。日本血吸虫谷胱甘肽S-转移酶（GST-VD IV）。融合蛋白在非变性条件下被亲和纯化并用于免疫兔。通过微免疫荧光，免疫印迹，斑点印迹，肽酶联免疫吸附剂和体外中和测定来表征抗血清。抗血清从沙眼衣原体的所有12种测试血清中识别出MOMP，但在鹦鹉热衣原体中却没有。在斑点印迹分析中，抗血清以强效方式与血清型B，D，E，L2和K的基本体结合，并以弱方式与血清型F，G，A和H的基本体结合，但不与基本体结合。在固相酶联免疫吸附试验中使用合成的重叠血清型B MOMP肽进行高分辨率肽图分析，结果表明，用GST-VD IV免疫产生的血清学应答与模拟产生的应答密切相关。纯化的血清型B基本体。产生了与物种和亚种特异性表位具有强结合力的抗肽抗体。抗血清只能在斑点印迹分析中中和结合抗体的沙眼衣原体血清。这些结果表明，含有物种特异性表位的VD IV抗原片段可用于构建沙眼衣原体部分而非全部沙眼衣原体疫苗。

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