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Updated: Mar 9, 2026

Spectrophotometric Screening for Potential Inhibitors of Cytosolic Glutathione S-Transferases
Published on: October 10, 2020
Echinococcus granulosus: Evidence of a heterodimeric glutathione transferase built up by phylogenetically distant
Paula Arbildi1, Silvana La-Rocca1, Veronica Lopez1
1Cátedra de Inmunología, Facultad de Química, UdelaR, Av. Alfredo Navarro 3051, piso 2, Montevideo, CP 11600, Uruguay.
Abstract:
In the cestode parasite Echinococcus granulosus, three phylogenetically distant cytosolic glutathione transferases (GSTs) (EgGST1, 2 and 3) were identified. Interestingly, the C-terminal domains of EgGST3 and EgGST2 but not EgGST1, exhibit all amino acids involved in Sigma-class GST dimerization. Here, we provide evidence indicating that EgGST2 and EgGST3 naturally form a heterodimeric structure (EgGST2-3), and also we report the enzymatic activity of the recombinant heterodimer. EgGST2-3 might display novel properties able to influence the infection establishment. This is the first report of a stable heterodimeric GST built up by phylogenetically distant subunits.
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