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大豆花叶病毒外壳蛋白基因的克隆及其在大肠杆菌中的表达。

Cloning of coat protein gene of soybean mosaic virus and its expression in Escherichia coli.

作者信息

Liu J, Peng X, Li L, Mang K

机构信息

Institute of Microbiology, Chinese Academy of Sciences, Beijing.

出版信息

Chin J Biotechnol. 1993;9(3):143-9.

PMID:8049345
Abstract

The 3'-terminal genomic region of the Beijing isolate of soybean mosaic virus (SMV-BJ) has been cloned through technique of polymerase chain reaction (PCR). We have analyzed the nucleotide sequence of 3' region of SMV-BJ genome. Comparisons of the nucleotide and deduced amino acid sequence of SMV-BJ coat protein gene with those of SMV-N strain show 93.4% and 98.5% identity between them, respectively. Alignments of the 3' non-coding sequence in pairs with that of SMV-N strain show homology of 88.8%. It has been found that the SMV coat protein gene is expressed in E. coli by western blot analysis. The coat protein produced in E. coli has the same electrophoretic mobility as the authentic coat protein.

摘要

通过聚合酶链反应(PCR)技术克隆了大豆花叶病毒北京分离株(SMV-BJ)的3'末端基因组区域。我们分析了SMV-BJ基因组3'区域的核苷酸序列。将SMV-BJ外壳蛋白基因的核苷酸和推导的氨基酸序列与SMV-N株的相应序列进行比较,结果显示它们之间的同一性分别为93.4%和98.5%。将3'非编码序列与SMV-N株的相应序列进行比对,同源性为88.8%。通过蛋白质免疫印迹分析发现,SMV外壳蛋白基因在大肠杆菌中表达。在大肠杆菌中产生的外壳蛋白与天然外壳蛋白具有相同的电泳迁移率。

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