Prokaryotic Expression of the GP3 Protein of Porcine Reproductive and Respiratory Syndrome Virus S1 Strain

JIANG Wen-ming; JIANG Ping*; LI Yu-feng

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October 2005

JIANG Wen-ming, JIANG Ping* and LI Yu-feng. Prokaryotic Expression of the GP3 Protein of Porcine Reproductive and Respiratory Syndrome Virus S1 Strain[J]. Virologica Sinica, 2005, 20(5): 519-521.

Citation: JIANG Wen-ming, JIANG Ping*, LI Yu-feng. Prokaryotic Expression of the GP3 Protein of Porcine Reproductive and Respiratory Syndrome Virus S1 Strain .VIROLOGICA SINICA, 2005, 20(5) : 519-521.

猪繁殖与呼吸综合征病毒S1株GP3蛋白的原核表达与纯化

1.
南京农业大学农业部动物疫病诊断与免疫重点开放实验室江苏南京

摘要

利用限制性酶切从重组质粒pRSET-GP3中得到缺失N端疏水序列的基因片段tGP3(truncated GP3)。将tGP3克隆至原核高效表达载体pRSET,在E.coliBL21细胞中用IPTG诱导表达了猪繁殖与呼吸综合征病毒(PRRSV)重组蛋白(His)6-GP3,并用亲和层析法获得了纯化蛋白。Western-Blotting结果表明重组蛋白可被PRRSV阳性血清所识别,从而为进一步研究PRRSV GP3结构蛋白的免疫特性和功能奠定了基础。
- 猪繁殖与呼吸综合征病毒
- , GP3
- , 原核表达

Prokaryotic Expression of the GP3 Protein of Porcine Reproductive and Respiratory Syndrome Virus S1 Strain

Abstract

The GP3 deleted hydrophobic N-terminal sequence(tGP3) of Porcine reproductive and respiratory syndrome virus(PRRSV) was cloned into prokaryotic expression vector pRSET.The recombinant protein(His)_6-GP3 was highly expressed in E.coli BL21 and could amount to 41% of the total proteins.It could be purified efficiently with affinity chromatography.Western-blotting analysis showed that the recombinant protein was able to react with PRRSV polyclonal antiserum.It can be used for the further investigation on immunogenicity and function of GP3 of PRRSV.
- PRRSV
- , GP3'Prokaryotic expression

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通讯作者: 陈斌, bchen63@163.com

1.
沈阳化工大学材料科学与工程学院沈阳 110142

Prokaryotic Expression of the GP3 Protein of Porcine Reproductive and Respiratory Syndrome Virus S1 Strain

Abstract: The GP3 deleted hydrophobic N-terminal sequence(tGP3) of Porcine reproductive and respiratory syndrome virus(PRRSV) was cloned into prokaryotic expression vector pRSET.The recombinant protein(His)_6-GP3 was highly expressed in E.coli BL21 and could amount to 41% of the total proteins.It could be purified efficiently with affinity chromatography.Western-blotting analysis showed that the recombinant protein was able to react with PRRSV polyclonal antiserum.It can be used for the further investigation on immunogenicity and function of GP3 of PRRSV.