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首页> 外文期刊>Journal of Clinical Microbiology >High-level expression of a 56-kilodalton protein gene (bor56) of Rickettsia tsutsugamushi Boryong and its application to enzyme-linked immunosorbent assays.
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High-level expression of a 56-kilodalton protein gene (bor56) of Rickettsia tsutsugamushi Boryong and its application to enzyme-linked immunosorbent assays.

机译：cket虫立克次体的56个千岛蛋白基因（bor56）的高水平表达及其在酶联免疫吸附测定中的应用。

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摘要

The 56-kDa protein of Rickettsia tsutsugamushi, which is located on the rickettsial surface, has been shown to be an immunodominant antigen. The gene that encodes the 56-kDa protein of R. tsutsugamushi Boryong (bor56) was cloned. Sequencing revealed an open reading frame of 1,602 bp encoding 534 amino acids with a molecular weight of 56,803. The 56-kDa protein of R. tsutsugamushi Boryong (Bor56) was expressed as a fusion protein with the maltose-binding protein of Escherichia coli by deleting 252 bp from the 5' end of the open reading frame and subcloning it into the StuI site of pIH821. The recombinant fusion protein was purified by amylose column chromatography for application in an enzyme-linked immunosorbent assay to evaluate the ability of the method to detect the antibody to R. tsutsugamushi in human patient sera. By using sera from 100 patients with scrub typhus and 70 patients with other febrile diseases, a high diagnostic sensitivity (95%) and a high diagnostic specificity (100%) were demonstrated, suggesting the suitability of the recombinant antigen for use as an immunodiagnostic tool.
机译：位于立克次体表面的立克氏菌的56 kDa蛋白已被证明是一种免疫显性抗原。克隆了编码gam虫支博毛虫（bor56）的56-kDa蛋白的基因。测序揭示了一个1,602 bp的开放阅读框，编码534个氨基酸，分子量为56,803。通过从开放阅读框的5'末端缺失252 bp并将其亚克隆到大肠杆菌的StuI位点，将虫R. tsutsugamushi Boryong（Bor56）的56 kDa蛋白表达为与大肠杆菌的麦芽糖结合蛋白的融合蛋白。 pIH821。通过直链淀粉柱色谱纯化重组融合蛋白，以用于酶联免疫吸附测定中，以评估该方法检测人患者血清中虫的抗体的能力。通过使用100例斑疹伤寒患者和70例其他发热性疾病患者的血清，证明了高诊断敏感性（95％）和高诊断特异性（100％），表明重组抗原适合用作免疫诊断工具。

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