Echinococcus granulosus: Evidence of a heterodimeric glutathione transferase built up by phylogenetically distant subunits

被引:7
作者
Arbildi, Paula [1 ]
La-Rocca, Silvana [1 ]
Lopez, Veronica [1 ]
Da-Costa, Natalia [1 ]
Fernandez, Veronica [1 ]
机构
[1] UdelaR, Fac Quim, Catedra Inmunol, Av Alfredo Navarro 3051,Piso 2, Montevideo 11600, Uruguay
关键词
Echinococcus granulosus; Glutathione transferase; Heterodimer; Enzyme activity; OMEGA-CLASS; S-TRANSFERASES; IDENTIFICATION; INFECTION; P1-1;
D O I
10.1016/j.molbiopara.2016.12.006
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 2016 Elsevier B.V. All rights reserved.
引用
收藏
页码:26 / 30
页数:5
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