Expression and purification of human papillomavirus type16 L1 protein in a prokaryotic expression system.
- Author:
Guangyu BAO
1
;
Hongxi GU
;
Daohong LIN
;
Min ZHUANG
;
Lihua SHUI
;
Jing WANG
Author Information
1. Department of Microbiology, Harbin Medical University, Harbin 150086.
- Publication Type:Journal Article
- MeSH:
Capsid Proteins;
biosynthesis;
Escherichia coli;
metabolism;
Genetic Vectors;
Human papillomavirus 16;
Oncogene Proteins, Viral;
biosynthesis
- From:
Journal of Biomedical Engineering
2002;19(2):280-283
- CountryChina
- Language:Chinese
-
Abstract:
This study was intended to establish a method of purification of HPV16 L1 protein expressed in a prokaryotic system and to obtain the purified protein. The prokaryotic expression vector pGEX-4T-1-HPV16 L1 was constructed and transformed into E. coli BL21 cell, and induced by 1 mM IPTG to express HPV16L1 protein. The inclusion bodies were isolated and solubilized with 8 M urea. After the urea was removed by gradual dialysis, the denatured L1 protein were renatured and then were purified by affinity chromatography. The results showed that HPV16L1 protein formed inclusion bodies in bacterial expression system, suggesting that this assay can be used to purify HPV16L1 protein and hence provide a basis for studying the applications of HPV16 L1 protein.
