yinyuhe
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- Associate professor
- Supervisor of Doctorate Candidates
- Supervisor of Master's Candidates
- Name (English):carter
- Name (Pinyin):yinyuhe
- Date of Birth:1972-05-27
- E-Mail:
- Date of Employment:2007-07-01
- School/Department:长春工业大学化学与生命科学学院
- Education Level:Postgraduate (Doctoral)
- Degree:Doctoral degree
- Professional Title:Associate professor
- Status:Employed
- Alma Mater:吉林大学
- Teacher College:化学与生命科学学院
Contact Information
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- Paper Publications
Characterization of NoV P particle-based chimeric protein vaccines developed from two different expression systems
Release time:2021-04-12 Hits:
- Affiliation of Author(s):化学与生命科学学院
- Teaching and Research Group:化学与生命科学学院
- Journal:Protein Expression and Purification
- Funded by:省、市、自治区科技项目
- Key Words:P particle Inclusion body expression system
- Abstract:The Norovirus (NoV) P domain, with three surface loops for foreign antigen insertion, has been demonstrated as an excellent platform for antigen presentation and novel vaccine development. The P domain alone can self-assemble into a P dimer, 12-mer small particle or 24-mer P particle, and vaccines based on those particles may elicit different levels of immunogenicity. Currently, P particles are generally produced in soluble expression systems in Escherichia coli, mainly in the 24-mer form. However, the low yield of the soluble protein has hindered further clinical applications of P particle-based protein vaccines. In this study, we inserted the Alzheimer's disease (AD) immunogen A b 1-6 into the three loops of the P particle to generate an AD protein vaccine. To increase the yield of this chimeric protein, we tested the generation of proteins in a soluble expression system and an inclusion body expression system sepa- rately in E. coli. The result showed that the inclusion body expression system could greatly enhance the product yield of the chimeric protein compared with the soluble expression system. The refolded protein from the inclusion bodies was mainly in the 12-mer form, while the protein generated from the soluble supernatant was mainly in the 24-mer form. Moreover, the immunogenicity of soluble proteins was significantly stronger than that of the refolded proteins. Thus, comparisons between the two expression methods suggested that the soluble expression system generated chimeric P particles with better immunogenicity, while inclusion body expression system yielded more P particle proteins.
- First Author:carter
- Indexed by:Journal paper
- Page Number:1
- Translation or Not:no
- Date of Publication:2016-09-28