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Tytuł:
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Molecular characterization, immune and xenobiotic responses of glutathione S-transferase omega 1 from the big-belly seahorse: Novel insights into antiviral defense.
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Autorzy:
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Udayantha HMV; Department of Marine Life Sciences & Fish Vaccine Research Center, Jeju National University, Jeju Self-Governing Province, 63243, Republic of Korea.
Liyanage DS; Department of Marine Life Sciences & Fish Vaccine Research Center, Jeju National University, Jeju Self-Governing Province, 63243, Republic of Korea.
Nadarajapillai K; Department of Marine Life Sciences & Fish Vaccine Research Center, Jeju National University, Jeju Self-Governing Province, 63243, Republic of Korea.
Omeka WKM; Department of Marine Life Sciences & Fish Vaccine Research Center, Jeju National University, Jeju Self-Governing Province, 63243, Republic of Korea.
Yang H; Department of Marine Life Sciences & Fish Vaccine Research Center, Jeju National University, Jeju Self-Governing Province, 63243, Republic of Korea.
Jeong T; Department of Marine Life Sciences & Fish Vaccine Research Center, Jeju National University, Jeju Self-Governing Province, 63243, Republic of Korea; Marine Science Institute, Jeju National University, Jeju Self-Governing Province, 63333, Republic of Korea.
Lee J; Department of Marine Life Sciences & Fish Vaccine Research Center, Jeju National University, Jeju Self-Governing Province, 63243, Republic of Korea; Marine Science Institute, Jeju National University, Jeju Self-Governing Province, 63333, Republic of Korea. Electronic address: .
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Źródło:
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Fish & shellfish immunology [Fish Shellfish Immunol] 2021 Feb; Vol. 109, pp. 62-70. Date of Electronic Publication: 2020 Dec 19.
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Typ publikacji:
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Journal Article
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Język:
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English
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Imprint Name(s):
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Original Publication: London ; New York : Academic Press, c1991-
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MeSH Terms:
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Fish Diseases/*immunology
Gene Expression Regulation/*immunology
Glutathione Transferase/*genetics
Glutathione Transferase/*immunology
Immunity, Innate/*genetics
Smegmamorpha/*genetics
Smegmamorpha/*immunology
Amino Acid Sequence ; Animals ; Female ; Fish Diseases/virology ; Fish Proteins/chemistry ; Fish Proteins/genetics ; Fish Proteins/immunology ; Gene Expression Profiling/veterinary ; Glutathione Transferase/chemistry ; Male ; Novirhabdovirus/physiology ; Phylogeny ; Rhabdoviridae Infections/immunology ; Rhabdoviridae Infections/virology ; Sequence Alignment/veterinary
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Contributed Indexing:
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Keywords: Antiviral response; Detoxification; Glutathione S-Transferases omega 1; Immune response; Seahorse; Viral hemorrhagic septicemia virus infection
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Substance Nomenclature:
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0 (Fish Proteins)
EC 2.5.1.18 (Glutathione Transferase)
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Entry Date(s):
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Date Created: 20201221 Date Completed: 20210514 Latest Revision: 20210514
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Update Code:
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20240105
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DOI:
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10.1016/j.fsi.2020.12.010
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PMID:
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33348035
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Glutathione S-transferases (GSTs) are important enzymes involved in phase II detoxification and function by conjugating with the thiol group of glutathione. In this study, we isolated an omega class GST from the big-belly seahorse (Hippocampus abdominalis; HaGSTO1) to study the putative xenobiotic responses and defense ability against viral and bacterial infections in this animal. The isolated HaGSTO1 gene, with a cording sequence of 720 bp, encodes a peptide of 239 amino acids. The predicted molecular mass and theoretical isoelectric point of HaGSTO1 was 27.47 kDa and 8.13, respectively. In-silico analysis of HaGSTO1 revealed a characteristic N-terminal thioredoxin-like domain and a C-terminal domain. Unlike other GSTs, the C-terminal of HaGSTO1 reached up to the N-terminal, and the N-terminal functional group was cysteine rather than tyrosine or serine, as observed in other GSTs. Phylogenetic analysis showed the evolutionary proximity of HaGSTO1 with other identified vertebrate and invertebrate GST orthologs. For the first time, we demonstrated the viral defense capability of HaGSTO1 against viral hemorrhagic septicemia virus (VHSV) infection. All six nucleoproteins of VHSV were significantly downregulated in HaGSTO1-overexpressing FHM cells at 24 h after infection compared with those in the control. Moreover, arsenic toxicity was significantly reduced in HaGSTO1-overexpressing FHM cells, and cell viability increased. Real-time polymerase chain reaction analysis showed that HaGSTO1 transcripts were highly expressed in the pouch and gill when compared with those in other tissues. Blood HaGSTO1 transcripts were significantly upregulated after Edwardsiella tarda, Streptococcus iniae, lipopolysaccharide, and polyinosinic:polycytidylic acid challenge experiments. Collectively, these findings suggest the involvement of HaGSTO1 in the host defense mechanism of seahorses.
(Copyright © 2020 Elsevier Ltd. All rights reserved.)
