Wildenburg G, Liebau E, Henkle-Dührsen K
Department of Helminthology and Entomology, Bernhard Nocht Institute for Tropical Medicine, Hamburg, Germany.
Exp Parasitol. 1998 Jan;88(1):34-42. doi: 10.1006/expr.1998.4189.
Glutathione S-transferases (GSTs) are essential detoxification enzymes for virtually all cells and may additionally aid in parasite survival by counteracting host-induced damage. GSTs from parasitic nematodes have been identified as potential targets for both immuno- and chemotherapy. To more closely characterize a 31-kDa (OvGST1) and a 24.5-kDa (OvGST2) GST from the pathogenic human filarial parasite Onchocerca volvulus, immunolocalization by electron microscopy was performed using two distinct affinity-purified polyclonal antisera raised against the recombinant OvGST1 and OvGST2. The strongest immunogold staining for OvGST1 was identified in the body wall of adult worms, especially in protuberances of the cuticle which lie in pouches of the hypodermis and in the outer zone of the syncytial hypodermis, where the external plasma membrane forms series of lamellae. Gold particles were also observed on the epicuticle of the adults and in the region of the border between the cuticle and hypodermis of microfilariae. The larval stages L1, L2, and infective L3 were also immunopositive for OvGST1. There was no specific labeling in the longitudinal musculature, the intestine, or the uterine wall of the adult worm. In contrast to the results for OvGST1, immunogold labeling for OvGST2 was observed throughout the whole hypodermal cytoplasm. The epithelial cells of the uterine wall showed moderate labeling. These ultrastructural immunolocalization results are consistent with the molecular characterization of both enzymes, indicating that OvGST1 is secreted out of the hypodermis into the cuticle and is acting at the host-parasite interface, while OvGST2 functions as an intracellular cytosolic housekeeping enzyme.
