Molecular characterisation and localisation of an Onchocerca volvulus pi-class glutathione S-transferase.

Abstract:

: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.

journal_name

Mol Biochem Parasitol

authors

Salinas G,Braun G,Taylor DW

doi

10.1016/0166-6851(94)90030-2

subject

Has Abstract

pub_date

1994-07-01 00:00:00

pages

1-9

issue

1

eissn

0166-6851

issn

1872-9428

pii

0166-6851(94)90030-2

journal_volume

66

pub_type

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