Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1251373 | Chemical Research in Chinese Universities | 2007 | 4 Pages |
Abstract
In this study, a recombinant Pichia pastoris expression system was developed to express HPV16 L1 protein that was driven by a strong AOX1 promoter. HPV16L1 gene was cloned into vector pPICZαB. HPV16 L1 protein expression induced by methanol was screened by using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blotting. The results indicate that the HPV16 L1 protein is secreted by the recombinant P. pastoris, and the purified HPV16 L1 protein can self-assemble into virus-like particles(VLPs), which show a good immunogenicity and induces high-titer antibody in mice.
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Physical Sciences and Engineering
Chemistry
Chemistry (General)
Authors
Da-wei LIU, Yu ZHANG, Xiang-hui YU, Chun-lai JIANG, Yue CHEN, Yong-ge WU, Ying-hua JIN, Jun NIU, Ning QU, Ming LIU, Wei KONG,