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Title 

Bacterial expression and purification of human papillomavirus type 18 L1

 

인유두종 바이러스 18타입 L1의 박테리아내 발현 및 정제

Authors 

P S SeoSun-Yeon HeoE J HanJeong Woo SeoS J GhimChul Ho Kim

Publisher 

Springer Verlag (Germany)

Issue Date 

2009

Citation 

Biotechnology and Bioprocess Engineering, vol. 14, no. 2, pp. 168-174

Keywords 

bacterial expressionHPV type 18human papillomavirusL1 major capsid proteinpurification

Abstract 

The human papillomavirus (HPV) 18 L1 gene, which encodes the L1 major capsid protein, was isolated from a female patient in Pusan, Korea Republic and was cloned into pGEX-4T-1 vector. The HPV-18L1 gene was expressed in Escherichia coli as a fusion protein with a glutathione-S-transferase (GST) tag. The soluble recombinant fusion protein, GST-18 L1 fusion, was isolated to high purity. HPV-18 L1 was purified from the GST-18 L1 fusant after biotinylated thrombin cleavage, and then the treated thrombin was removed serially using streptavidin conjugated resin. The purified HPV-18 L1 was confirmed by western blotting using a rabbit anti-denatured papillomavirus polyclonal antibody. The virus-like particles (VLP) from the purified full-length 18 L1 protein without any extra amino acid sequences was observed through the analysis of the electron microscope. This is the first study to report the expression and purification of HPV-18 L1 in E. coli. This expression and purification system offers a simple method of expressing and purifying HPV L1 protein, and could potentially be an effective route for the development and manufacturing of highly purified HPV-18 L1-based cervical cancer vaccines.

ISSN 

1226-8372

Link 

http://dx.doi.org/10.1007/s12257-008-0122-4

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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