Expanding the family of Mu-class glutathione transferases in the cestode parasite Echinococcus granulosus sensu lato

Glutathione transferases (GSTs) perform catalytic and non-catalytic activities, mostly involved in stress-response and cell detoxification. Helminth parasites express several GSTs of multiple classes that are involved in the neutralization of potentially harmful oxidants, and in the inactivation or removal of xenobiotics. Additionally, GSTs participate in immunomodulatory processes that facilitate the parasite establishment and survival within its host. In Echinococcus granulosus sensu lato (s.l.) -the cestode parasite responsible for cystic echinococcosis- only one Mu-class GST has been reported. In the present work, by using bioinformatic and proteomic approaches we searched for novel Mu-class GSTs potentially involved in the parasite oxidative-stress metabolism. In the genome of E. granulosus s.l., 6 GST-related sequences were found to constitute a strongly conserved phylogenetical clade with Mu-class members. Among them, 5 displayed conserved gene structure (exon/intron), as well as specific residues and motifs characteristic of Mu-class enzymes. By proteomic analysis, 3 Mu-GSTs were identified to be expressed in the protoscolex parasite stage, 2 of them being firstly described as Mu-class GSTs here. The existence of more than one productive Mu-GST gene expands the parasite xenobiotic phase II metabolism, which might have beneficial roles on E. granulosus s.l. ability to successfully infect its host.