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。
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.
出处
《中国病毒学》
CSCD
2005年第5期519-521,共3页
Virologica Sinica
基金
国家自然科学基金30471288
30270990
教育部博士点基金项目2003030712
新世纪优秀人才支持计划(NCET-04-0502)
