Molecular characterization of kappa class glutathione S‐transferase from the disk abalone (Haliotis discus discus) and changes in expression following immune and stress challenges

ABSTRACT Glutathione S‐transferase (GST; EC 2.5.1.18) isoenzymes represent a complex group of proteins that are involved in phase II detoxification in several organisms. In this study, GST kappa (GST&kgr;) from the disk abalone (Haliotis discus discus; AbGST&kgr;) was characterized at both the transcriptional and functional levels to determine its potential capacity to perform as a detoxification agent under conditions of different stress. The predicted AbGST&kgr; protein consists of 227 amino acids, with a predicted molecular weight of 25.6 kDa and a theoretical isoelectric point (pI) of 7.78. In silico analysis reveals that AbGST&kgr; is a disulfide bond formation protein A (DsbA), consisting of a thioredoxin domain, GSH binding sites (G‐sites), and a catalytic residue. In contrast, no hydrophobic ligand binding site (H‐site), or signal peptides, were detected. AbGST&kgr; showed the highest sequence identity with the orthologue from pufferfish (Takifugu obscurus) (60.0%). In a phylogenetic tree, AbGST&kgr; clustered closely together with other fish GST&kgr;s, and was evolutionarily distanced from other cytosolic GSTs. The predicted three‐dimensional structure clearly demonstrates that the dimer adopts a butterfly‐like shape. A tissue distribution analysis revealed that GST&kgr; was highly expressed in the digestive tract, suggesting it has detoxification ability. Depending on the tissue and time, AbGST&kgr; showed different expression patterns, and levels of expression, following challenge of the abalone with immune stimulants. Enzyme kinetics of the purified recombinant proteins demonstrated its conjugating ability using 1‐Chloro‐2,4‐dinitrobenzene (CDNB) and glutathione (GSH) as substrates, and suggested it has a low affinity for both substrates. The optimum temperature and pH for the rAbGST&kgr; GSH: CDNB conjugating activity were found to be 35 °C and pH 8, respectively indicating that the abalone is well adapted to a wide range of environmental conditions. Cibacron blue (100 &mgr;M) was capable of completely inhibiting rAbGST&kgr; (100%) with an IC50 (half maximal inhibitory concentration) of 0.05 &mgr;M. A disk diffusion assay revealed that rAbGST&kgr; could significantly protect cells from H2O2, CdCl2, and ZnCl2. Altogether, this current study suggests that AbGST&kgr; is involved in detoxification and immunological host defense mechanisms and allows abalones to overcome stresses in order for them to have an increased chance of survival. HighlightsThe full‐length coding sequence of AbGST&kgr; was identified in disk abalone.AbGST&kgr; is a disulfide bond formation protein A (DsbA) with a thioredoxin domain.Highest mRNA expression of AbGST&kgr; was observed in digestive tract.Immunological responses of AbGST&kgr; has evaluated.Enzyme kinetics, optimum conditions and heavy metal stress responses were measured.

• Publication year

  2018

• Venue

  Fish and Shellfish Immunology

• Publication date

  2018-06-01

• Fields of study

  Biology, Medicine, Environmental Science

• Identifiers
  DOI 10.1016/j.fsi.2018.03.058PMID 29621633
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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