Salinas G, Braun G, Taylor D W
Department of Pathology, University of Cambridge, UK.
Mol Biochem Parasitol. 1994 Jul;66(1):1-9. doi: 10.1016/0166-6851(94)90030-2.
Glutathione S-transferases (GSTs) constitute a major detoxification mechanism in helminth organisms and are regarded vaccine candidates against helminth infections. Onchocerca volvulus glutathione-binding proteins were purified from the aqueous soluble fraction of homogenised adult females by affinity chromatography on glutathione-agarose. The eluted proteins had a specific GST activity of 1.6 mumol min-1 mg-1. Immunohistochemical studies localised these antigens in the hypodermis, the wall of the seminal receptacle and spermatozoa of adult worms. A lambda gt11 clone was isolated from an expression library of O. volvulus by immunoscreening. Sequence analysis revealed that it encoded a pi-class GST with 60% identity with Caenorhabditis elegans and up to 45% identity with mammalian pi-class GSTs. Antibodies affinity selected with recombinant GST demonstrated cross-reactivity between Litomosoides sigmodontis and O. volvulus GSTs.
谷胱甘肽S-转移酶（GSTs）是蠕虫生物体中的一种主要解毒机制，被视为抗蠕虫感染的候选疫苗。通过谷胱甘肽琼脂糖亲和层析从匀浆成年雌性虫体的水溶性部分纯化盘尾丝虫谷胱甘肽结合蛋白。洗脱的蛋白具有1.6 μmol min⁻¹ mg⁻¹的特异性GST活性。免疫组织化学研究将这些抗原定位在成虫的皮下组织、受精囊壁和精子中。通过免疫筛选从盘尾丝虫的表达文库中分离出一个λgt11克隆。序列分析表明，它编码一种π类GST，与秀丽隐杆线虫的同一性为60%，与哺乳动物π类GST的同一性高达45%。用重组GST亲和选择的抗体显示，链尾丝虫和盘尾丝虫GST之间存在交叉反应性。
