Gene cloning of a sigma class glutathione S-transferase from abalone (Haliotis diversicolor) and expression analysis upon bacterial challenge

Abstract

National High Technology Research, Development Program of China [2007AA091406]; MEL Young Scientist Visiting Scholarship [MEL0905]Glutathione S-transferases (GSTs) are a multigene family of xenobiotic metabolizing phase II detoxification enzymes which take part in many pathological and physiological processes, and which can potentially be used as indicators and biomarkers for cancer diagnoses and organic or inorganic pollutant exposure. In this study, a full-length cDNA of a sigma class GST (abGSTsigma) (CenBank accession number EF546619) from variously colored abalone (Hatiotis diversicolor) was identified. It was 1328 bp containing an open reading frame of 624 bp, encoding 208 amino acid residues with a predicted protein molecular weight of 23.67 kDa and an estimated pI of 5.67. Sequence analysis showed that the predicted protein sequence of abGSTsigma cDNA contained the conserved domain of the GST_N_Sigma_like (PSSM: cd03039) and GST_C_Sigma_like (PSSM: cd03192). Alignment analysis demonstrated that the abGSTsigma of H. diversicolor was in a branch position with other known class sigma GSTs from different organisms. The abGSTsigma mRNA was distributed in multiple tissues tested and was highly demonstrated in the gill and mantle of normal abalones. In bacteria-challenged abalone, the abGSTsigma gene was significantly expressed in the hemocytes, gill, mantle and digestive gland and the total GSTs enzyme and SOD were also induced in the four tissues. The increased activities of SOD and GSTs can result in the elimination of reactive oxygen species (ROS) indicating antioxidant activities involved. The preliminary work revealed that the sigma class glutathione S-transferase gene abGSTsigma, a phase 11 detoxification enzyme, had a positive response to bacterial challenge, and that will lead to an insightful study on elucidating the interactions between immune responses and biotransformation exerted by abGSTsigma. (C) 2009 Elsevier Ltd. All rights reserved