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| Main Authors: | , , , , , , , , , , , , , , , |
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| Format: | Artículo científico |
| Language: | en |
| Published: |
International journal of molecular sciences
2026
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| Subjects: | |
| Online Access: | https://pubmed.ncbi.nlm.nih.gov/41596326/ |
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Table of Contents:
- Development of a High-Hydrostatic-Pressure-Treated Recombinant Vaccine Targeting the Major Capsid Protein of Red Sea Bream Iridovirus. Sawasaki, Yuta Harakawa, Shogo Kitamura, Shin-Ichi Terawaki, Naomi Zhu, Zhangliang Yamada, Kohdai Fujisaki, Hinako Hirano, Suzuno Hamada, Mana Miyakawa, Takuya Matsuyama, Tomomasa Matsuura, Yuta Ozawa, Tatsuhiko Itano, Tomokazu Sawasaki, Tatsuya Nozawa, Akira Animals Capsid Proteins Viral Vaccines Hydrostatic Pressure Iridovirus Vaccines, Synthetic Sea Bream Antibodies, Viral Fish Diseases Immunoglobulin M Protein Subunit Vaccines Recombinant Proteins DNA Virus Infections Red sea bream () aquaculture represents one of the most economically important marine aquaculture industries in Japan and East Asia. However, viral diseases, particularly those caused by red sea bream iridovirus (RSIV), pose a serious threat to aquaculture production in this region. In this study, we applied high-hydrostatic-pressure (HHP) refolding technology to develop a recombinant vaccine targeting the RSIV major capsid protein (MCP). The recombinant MCP (RSIV-rMCP) expressed in was insoluble; however, HHP treatment under alkaline (pH 10) conditions in the presence of arginine successfully solubilised the protein while preserving its structural integrity. The solubilised protein (HHP-RSIV-rMCP) induced strong RSIV-specific IgM responses and enhanced disease resistance in red sea bream. In contrast, sera from fish immunised with a commercial formalin-inactivated vaccine exhibited minimal reactivity to HHP-RSIV-rMCP but reacted significantly to formalin-treated HHP-RSIV-rMCP. These results indicate that the HHP-RSIV-rMCP vaccine induces conformation-specific IgM antibodies and that structural preservation is crucial for maintaining antigenicity. Collectively, our findings demonstrate that HHP refolding technology is an effective strategy for preparing structurally preserved antigens.