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Gene cloning and prokaryotic expression of recombinant outer membrane protein from Vibrio parahaemolyticus

机译:副溶血性弧菌重组外膜蛋白的基因克隆和原核表达

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摘要

Gram-negative Vibrio parahaemolyticus is a common pathogen in humans and marine animals. The outer membrane protein of bacteria plays an important role in the infection and pathogenicity to the host. Thus, the outer membrane proteins are an ideal target for vaccines. We amplified a complete outer membrane protein gene (ompW) from V. parahaemolyticus ATCC 17802. We then cloned and expressed the gene into Escherichia coli BL21 (DE3) cells. The gene coded for a protein that was 42.78 kDa. We purified the protein using Ni-NTA affinity chromatography and Anti-His antibody Western blotting, respectively. Our results provide a basis for future application of the OmpW protein as a vaccine candidate against infection by V. parahaemolyticus. In addition, the purified OmpW protein can be used for further functional and structural studies.
机译:革兰氏阴性副溶血性弧菌是人类和海洋动物的常见病原体。细菌的外膜蛋白在宿主的感染和致病性中起重要作用。因此,外膜蛋白是疫苗的理想靶标。我们从副溶血弧菌ATCC 17802扩增了一个完整的外膜蛋白基因(ompW)。然后,我们克隆了该基因并将其表达到大肠杆菌BL21(DE3)细胞中。该基因编码的蛋白质为42.78 kDa。我们分别使用Ni-NTA亲和色谱法和Anti-His抗体Western印迹法纯化了蛋白质。我们的结果为将来将OmpW蛋白用作抗副溶血性弧菌感染的候选疫苗提供了基础。此外,纯化的OmpW蛋白可用于进一步的功能和结构研究。

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