Biochemical characterization and gene structure analysis of the 24‐kDa glutathione transferase sigma from Taenia solium

Taenia solium can cause human taeniasis and/or cysticercosis. The latter can in some instances cause human neurocysticercosis which is considered a priority in disease‐control strategies and the prevention of mental health problems. Glutathione transferases are crucial for the establishment and long‐term survival of T. solium; therefore, we structurally analyzed the 24‐kDa glutathione transferase gene (Ts24gst) of T. solium and biochemically characterized its product. The gene promoter showed potential binding sites for transcription factors and xenobiotic regulatory elements. The gene consists of a transcription start site, four exons split by three introns, and a polyadenylation site. The gene architecture is conserved in cestodes. Recombinant Ts24GST (rTs24GST) was active and dimeric. Anti‐rTs24GST serum showed slight cross‐reactivity with human sigma‐class GST. A 3D model of Ts24GST enabled identification of putative residues involved in interactions of the G‐site with GSH and of the H‐site with CDNB and prostaglandin D2. Furthermore, rTs24GST showed optimal activity at 45 °C and pH 9, as well as high structural stability in a wide range of temperatures and pHs. These results contribute to the better understanding of this parasite and the efforts directed to fight taeniasis/cysticercosis. Glutathione transferases (GST) are involved in detoxification and immunomodulation, allowing the establishment and development of cestodes in the host. Taenia solium has a 24‐kDa GST sigma class inducible gene that encodes a stable enzyme in a wide range of pHs and temperatures. Its enzymatic activity differs from other GSTs in the parasite, suggesting a different role to detoxification.