Production of a Bacteria-like Particle Vaccine Targeting Rock Bream (Oplegnathus fasciatus) Iridovirus Using Nicotiana benthamiana
- Authors
- Ahn, Gyeongik; Cha, Joon-Yung; Lee, Jeong Won; Park, Gyeongran; Shin, Gyeong-Im; Song, Shi-Jian; Ryu, Gyeongryul; Hwang, Inhwan; Kim, Min Gab; Kim, Woe-Yeon
- Issue Date
- Feb-2022
- Publisher
- 한국식물학회
- Keywords
- Bacteria-like particle; Iridovirus; Major capsid protein; Nicotiana benthamiana; Plant-based vaccine
- Citation
- Journal of Plant Biology, v.65, no.1, pp 21 - 28
- Pages
- 8
- Indexed
- SCIE
SCOPUS
KCI
- Journal Title
- Journal of Plant Biology
- Volume
- 65
- Number
- 1
- Start Page
- 21
- End Page
- 28
- URI
- https://scholarworks.gnu.ac.kr/handle/sw.gnu/1650
- DOI
- 10.1007/s12374-021-09328-z
- ISSN
- 1226-9239
1867-0725
- Abstract
- Viral diseases are extremely widespread infections that change constantly through mutations. To produce vaccines against viral diseases, transient expression systems are employed, and Nicotiana benthamiana (tobacco) plants are a rapidly expanding platform. In this study, we developed a recombinant protein vaccine targeting the major capsid protein (MCP) of iridovirus fused with the lysine motif (LysM) and coiled-coil domain of coronin 1 (ccCor1) for surface display using Lactococcus lactis. The protein was abundantly produced in N. benthamiana in its N-glycosylated form. Total soluble proteins isolated from infiltrated N. benthamiana leaves were treated sequentially with increasing ammonium sulfate solution, and recombinant MCP mainly precipitated at 40-60%. Additionally, affinity chromatography using Ni-NTA resin was applied for further purification. Native structure analysis using size exclusion chromatography showed that recombinant MCP existed in a large oligomeric form. A minimum OD600 value of 0.4 trichloroacetic acid (TCA)-treated L. lactis was required for efficient recombinant MCP display. Immunogenicity of recombinant MCP was assessed in a mouse model through enzyme-linked immunosorbent assay (ELISA) with serum-injected recombinant MCP-displaying L. lactis. In summary, we developed a plant-based recombinant vaccine production system combined with surface display on L. lactis.
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