Characterization of a recombinant mu-class glutathione S-transferase from Taenia solium

被引：1

作者：

N. Vibanco-Pérez

L. Jiménez

G. Mendoza-Hernández

A. Landa

机构：

[1] Depto. Microbiología y Parasitología,

[2] Facultad de Medicina,undefined

[3] Edificio A,undefined

[4] 2do piso. Universidad Nacional Autónoma de México,undefined

[5] Ciudad Universitaria,undefined

[6] Mexico D.F 04510,undefined

[7] Mexico,undefined

[8] Depto. Bioquímica,undefined

[9] Facultad de Medicina Universidad Nacional Autónoma de México,undefined

[10] Ciudad Universitaria,undefined

[11] Mexico D.F 04510,undefined

[12] Mexico,undefined

来源：

Parasitology Research | 2002年 / 88卷

关键词：

Glutathione; Sequence Analysis; cDNA Clone; High Identity; Enzymatic Property;

D O I：

暂无

中图分类号：

学科分类号：

摘要：

A Taenia solium larval glutathione S-transferase fraction (SGSTF), composed of two proteins with Mr 25,500 (SGSTM1) and 26,500 (SGSTM2), was purified by GSH-sepharose. Its N-terminal sequence analysis revealed that both proteins are related to mammalian mu-class GST enzymes. A cDNA clone coding for SGSTM1 was isolated and the amino acid sequence analysis showed close identity with two Echinococcus GSTs and also high identity with several mu-class GSTs that have been reported. In addition, SGSTM1 presents a similar structure to mu-class GSTs, including the mu loop. The recombinant SGSTM1 is a dimeric protein with enzymatic properties clearly related to mammalian mu-class GSTs. Western blot studies indicated that SGSTM1 is not antigenically related to SGSTM2 or mammalian GSTs from rabbit, pig and rat livers. Immunization with SGSTF and SGSTM2 was highly effective in reducing cysticerci load in murine cysticercosis. In contrast, no protection was obtained using native SGSTM1 and recombinant SGSTM1 as immunogens.

引用

页码：398 / 404

页数：6