期刊
JOURNAL OF BIOTECHNOLOGY
卷 223, 期 -, 页码 8-12出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jbiotec.2016.02.025
关键词
Porcine circovirus type 2; Escherichia coli expression; Virus-like particle; Cryo-EM structure; Vaccine efficacy
资金
- Major Science and Technology Program in Henan Province [131100110200]
- SIP, Suzhou city
- Jiangsu Province
We report the strategies leading to the large-production of soluble non-tag full-length porcine circovirus type 2 (PCV2) Cap protein in Escherichia coll. Under neutral pH condition, the purified recombinant Cap protein derived from E. coli expression self-assembles into homogenous round virus-like particle at the similar size of that of the intact PCV2 virus, which is further characterized by Cryo-EM single particle structure determined at 4.5 angstrom. The engineered PCV2 rCap VLP was tested as a subunit vaccine for the protective efficacy against PCV2 challenge on 3-week old piglets. Similar to commercial available PCV2 vaccine, the Cap VLP-immunized piglets developed specific antibody-mediated response and were protected from the virulent SH PCV2 strain challenge. Hence, the production of E. coli based PCV2Cap-VLP could be applied as a cost-friendly and effective subunit vaccine to control PCV2 spreading in developing countries. (C) 2016 Elsevier B.V. All rights reserved.
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