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author 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
author_facet 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
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
collection PubMed - marine biology
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.
format Artículo científico
id pubmed_41596326
institution PubMed
language en
publishDate 2026
publisher International journal of molecular sciences
record_format pubmed
spellingShingle 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
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.
title Development of a High-Hydrostatic-Pressure-Treated Recombinant Vaccine Targeting the Major Capsid Protein of Red Sea Bream Iridovirus.
topic 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
url https://pubmed.ncbi.nlm.nih.gov/41596326/