Volume 40, Issue 5 pp. 437-442

Stable high-level expression of truncated human papillomavirus type 16 L1 protein in Drosophila Schneider-2 cells

Jin Zheng

Jin Zheng

Key Laboratory of Biomedical Information Engineering, Ministry of Education, Center of Vaccine Development, School of Life Science and Technology, Xi'an Jiaotong University, Xi'an 710061, China

Search for more papers by this author
Xiaofeng Yang

Xiaofeng Yang

Key Laboratory of Biomedical Information Engineering, Ministry of Education, Center of Vaccine Development, School of Life Science and Technology, Xi'an Jiaotong University, Xi'an 710061, China

Department of Obstetrics and Gynecology, The First Affiliated Hospital, Medical School of Xi'an Jiaotong University, Xi'an 710061, China

Search for more papers by this author
Ying Sun

Ying Sun

Key Laboratory of Biomedical Information Engineering, Ministry of Education, Center of Vaccine Development, School of Life Science and Technology, Xi'an Jiaotong University, Xi'an 710061, China

Search for more papers by this author
Baochang Lai

Baochang Lai

Key Laboratory of Biomedical Information Engineering, Ministry of Education, Center of Vaccine Development, School of Life Science and Technology, Xi'an Jiaotong University, Xi'an 710061, China

Search for more papers by this author
Yili Wang

Corresponding Author

Yili Wang

Key Laboratory of Biomedical Information Engineering, Ministry of Education, Center of Vaccine Development, School of Life Science and Technology, Xi'an Jiaotong University, Xi'an 710061, China

*Corresponding author: Tel/Fax, 86-29-82655499; E-mail, [email protected]Search for more papers by this author

Abstract

To improve the existing human papillomavirus type 16 (HPV16) virus-like particle (VLP) preparation, the Drosophila inducible/secreted expression system, a highly efficient, economical method, was used to produce HPV16 VLPs. Drosophila Schneider-2 cells were cotransfected with pMT/BiP/V5-His expression vector containing the target gene encoding HPV16L1 protein without nucleus localization sequence and the selection vector pCoHygro plasmids at the ratio of 4:1. The stabled hygromycin-resistant cell line was obtained 1 month later, and the protein expression was induced by copper sulfate. The molecular mass of expressed HPV16L1 protein was 66 kDa, as revealed by SDS-PAGE, and confirmed by Western blot analysis. The yield of HPV16L1 protein was 0.554 mg per 1×107 cells. The characteristics of HPV16L1 protein were further analyzed by mouse erythrocyte hemagglutination assay, hemagglutination inhibition assay, and transmission electron microscopy. Results showed that the truncated protein was as biologically active as natural HPVL1 protein, inducing murine erythrocyte agglutination and VLP formation. These findings indicate that the Drosophila inducible/secreted expression system is promising as a convenient and economical method for the preparation of HPV16VLP vaccine.

The full text of this article hosted at iucr.org is unavailable due to technical difficulties.