The expression and purification of VP8* core protein of the rotavirus P 6 Genotype LL4260
10.3760/cma.j.issn.1003-9279.2018.02.019
- VernacularTitle: 轮状病毒P[6]基因型毒株LL4260株的VP8*核心区蛋白的表达和纯化
- Author:
Luyao WANG
1
;
Dandi LI
2
;
Xiaoman SUN
2
;
Qing ZHANG
2
;
Hong WANG
;
Lili PANG
2
;
Jihong HU
1
;
Zhaojun DUAN
2
Author Information
1. School of Public Health, University of Chinese Medicine, Lanzhou 730000, China
2. National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Beijing 102206, China
- Publication Type:Journal Article
- Keywords:
Rotavirus;
P[6] genotype;
VP8*core protein;
Protein expression and purification
- From:
Chinese Journal of Experimental and Clinical Virology
2018;32(2):195-198
- CountryChina
- Language:Chinese
-
Abstract:
Objective:The VP8* core protein of rotavirus P[6] genotype LL4260 was purified by prokaryotic expression, which is important for further study of protein structure and function.
Methods:The P[6] genotype LL4260 strain was obtained by PCR.The recombinant plasmid pET30 a-LL4260VP8*core was inserted into pET30 a vector and transformed into BL21 (DE3) competent cells with the correct recombinant plasmid. The expressed protein is purified by affinity chromatography and molecular sieve chromatography.
Results:The pET30 a-LL4260VP8* core region protein is soluble in the supernatant and proteins of approximately 22 kDa are identified by electrophoresis using purified proteins.
Conclusions:In this study, LL4260 containing pET30 a-LL4260VP8* core plasmid was successfully constructed and LL4260 strain VP8* protein was expressed.
