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Strong hydrophobicity enables efficient purification of HBc VLPs displaying various antigen epitopes through hydrophobic interaction chromatography
Li, Zhengjun1,2; Wei, Jiangxue1,2; Yang, Yanli1; Ma, Xiaowei3; Hou, Baidong4; An, Wenqi3; Hua, Zhaolin4; Zhan, Jingjing3; Li, Yao5; Ma, Guanghui1; Zhang, Songping1; Su, Zhiguo1
2018-12-15
Source PublicationBIOCHEMICAL ENGINEERING JOURNAL
ISSN1369-703X
Volume140Pages:157-167
Abstract

Hepatitis B core virus -like particle (HBc-VLP) has become a carrier for expression and presentation of foreign epitopes as vaccine candidates. Efficient purification is necessary for preparation of HBc-VLP and its derivatives with various foreign epitopes. In previous reports, HBc-VLP was mainly purified with ion exchange chromatography. In this study, we developed a platform purification technique based on hydrophobic interaction chromatography (HIC). The underlying principle is the strong hydrophobicity on the surface of HBc-VLP, which was found by mathematical calculation and experimental measurement. Based on HIC, a complete downstream process, from feedstock supernatant to the final pure product, was developed involving a heat pretreatment, an HIC, an ultrafiltration concentration and a size exclusion chromatography. The total recovery of HBc-VLP was 41.92% with nearly 100% purity. HIC was also applicable to three HBc-based vaccine candidates displaying epitope from nuclear protein (NP) and matrix protein 2 (M2e) of the influenza A virus, as well as from ovalbumin (OVA). Optimal HIC condition for these three recombinant VLPs was rationally designed by analysis on their surface hydrophobicity, which was influenced upon insertion of the foreign epitope. By applying the same process developed for HBc-VLP, satisfactory results were achieved for product recovery, purity and host cell DNA removal, thus it is possible to become a platform technique for various HBc-VLP based vaccine candidates.

KeywordHbc-vlp Hydrophobic Interaction Chromatography Surface Hydrophobicity Properties Rational Design Vaccine Candidates
DOI10.1016/j.bej.2018.09.020
Language英语
WOS KeywordVirus-like Particles ; b Core Antigen ; Ion-exchange Chromatography ; Mouth-disease Virus ; Phase-i Trial ; Escherichia-coli ; Negative Chromatography ; Enhanced Immunogenicity ; Surface-antigen ; Influenza-virus
Funding ProjectNatural Sciences Foundation of China[21336010] ; National Key Scientific Instrument and Equipment Development Project[2013YQ14040508]
WOS Research AreaBiotechnology & Applied Microbiology ; Engineering
WOS SubjectBiotechnology & Applied Microbiology ; Engineering, Chemical
Funding OrganizationNatural Sciences Foundation of China ; National Key Scientific Instrument and Equipment Development Project
WOS IDWOS:000450375700018
PublisherELSEVIER SCIENCE BV
Citation statistics
Document Type期刊论文
Identifierhttp://ir.ipe.ac.cn/handle/122111/26568
Collection中国科学院过程工程研究所
Corresponding AuthorZhang, Songping; Su, Zhiguo
Affiliation1.Chinese Acad Sci, Inst Proc Engn, State Key Lab Biochem Engn, Beijing 100190, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
3.Hualan Biol Engn Inc, Xinxiang 453003, Peoples R China
4.Chinese Acad Sci, Inst Biophys, Key Lab Infect & Immun, Beijing 100101, Peoples R China
5.Chinese Acad Sci, Inst Proc Engn, State Key Lab Multiphase Complex Syst, CAS Key Lab Green Proc & Engn, Beijing 100190, Peoples R China
Recommended Citation
GB/T 7714
Li, Zhengjun,Wei, Jiangxue,Yang, Yanli,et al. Strong hydrophobicity enables efficient purification of HBc VLPs displaying various antigen epitopes through hydrophobic interaction chromatography[J]. BIOCHEMICAL ENGINEERING JOURNAL,2018,140:157-167.
APA Li, Zhengjun.,Wei, Jiangxue.,Yang, Yanli.,Ma, Xiaowei.,Hou, Baidong.,...&Su, Zhiguo.(2018).Strong hydrophobicity enables efficient purification of HBc VLPs displaying various antigen epitopes through hydrophobic interaction chromatography.BIOCHEMICAL ENGINEERING JOURNAL,140,157-167.
MLA Li, Zhengjun,et al."Strong hydrophobicity enables efficient purification of HBc VLPs displaying various antigen epitopes through hydrophobic interaction chromatography".BIOCHEMICAL ENGINEERING JOURNAL 140(2018):157-167.
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