A sigma-class glutathione S-transferase from Solen grandis that responded to microorganism glycan and organic contaminants.

Glutathione S-transferases (GSTs) are a superfamily of antioxidant enzymes, which play crucial roles in detoxification and protection of tissues from oxidative damage caused by reactive oxygen species (ROS). In this study, a sigma-class GST was identified from razor clam Solen grandis (designated as SgGST-S1), and its expression patterns, both in tissues and toward microorganism glycan as well as organic contaminants stimulation, were then characterized. The full-length cDNA of SgGST-S1 was of 1291 bp, containing a 5' untranslated region (UTR) of 27 bp, and a 3' UTR of 619 bp with a poly (A) tail. The open reading frame (ORF) was of 645 bp, encoding a polypeptide of 214 amino acids with the predicted molecular weight of 24.8 kDa, which shared 47% identity with GST from Ruditapes philippinarum. The analysis of conserved domain and phylogenetic relationship strongly suggested that SgGST-S1 was a member of sigma-class GST. The mRNA of SgGST-S1 was constitutively expressed in all tested tissues of healthy razor clam, including mantle, gill, gonad, hemocytes, muscle, and hepatopancreas, and it was highly expressed in hepatopancreas. The mRNA expression of SgGST-S1 in hemocytes was significantly up-regulated (P < 0.01) after razor clam was stimulated by peptidoglycan (PGN) or β-1, 3-glucan, but not LPS. In addition, the SgGST-S1 transcript level was also significantly (P < 0.01) induced by exposure of benzo[a]pyrene (B[a]P) or Polybrominated Diphenyl Ethers (PBDE). All the results indicated that SgGST-S1 might serve as an antioxidant enzyme involving in the detoxification cause by both microorganism glycan and organic contaminants.