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为获得纯化的重组SARS病毒S1蛋白C端 ,研究其刺激机体产生针对SARS病毒免疫应答的规律和机制 ,将编码SARS病毒S1蛋白C端 311个氨基酸残基的基因克隆 ,并在原核表达系统中表达 ,纯化获得了的重组蛋白。利用SARS患者恢复期的血清 ,对纯化的重组S1蛋白进行血清学分析。结果表明 ,本研究中克隆表达的重组蛋白序列与公布的SARS病毒S1蛋白C端的序列相同 ,其编码的重组蛋白相对分子质量约为 5 90 0 0Mr。SARS患者恢复期的血清均与重组蛋白反应 ,在5 9 0 0 0Mr处形成特异性的反应条带 ,而来自SARS流行前的正常人对照血清则不能与重组蛋白反应。在本研究中获得的重组蛋白可以为研究SARS病毒识别宿主细胞受体的过程及其机制提供条件。
In order to obtain the purified C terminus of S1 protein of recombinant SARS virus, we studied the mechanism and mechanism of stimulating the body to produce immune response against SARS virus. Cloned the gene encoding 311 amino acids at the C terminal of S1 protein of SARS virus and expressed in prokaryotic expression system Expression, purification of the obtained recombinant protein. Purified recombinant S1 protein was serologically analyzed using serum from convalescent SARS patients. The results showed that the recombinant protein cloned in this study has the same sequence as the C-terminus of S1 protein of SARS virus, and the relative molecular mass of recombinant protein encoded by this protein is about 59000Mr. The serum of convalescent SARS patients reacted with the recombinant protein, forming a specific reaction band at 5900Mr, whereas the normal human control sera from pre-SARS patients did not react with the recombinant protein. The recombinant protein obtained in this study can provide conditions for studying the process of SARS virus recognition of host cell receptor and its mechanism.