A single amino acid substitution in Isozyme GST mu in Triclabendazole resistant Fasciola hepatica (SLIGO STRAIN) can substantially influence the manifestation of anthelmintic resistance

FERNANDEZ V; ESTEIN S.M; ORTIZ P; LUCHESSI P; SOLANA V; SOLANA H

EXPERIMENTAL PARASITOLOGY

ACADEMIC PRESS INC ELSEVIER SCIENCE

Lugar: Amsterdam; Año: 2015 vol. 159 p. 174 - 179

0014-4894

The helminth parasite Fasciola hepatica causes fascioliasis in human and domestic ruminants. Economic losses due to this infection are estimated in U$S 2000e3000 million yearly. The most common method of control is the use of anthelmintic drugs. However, there is an increased concern about the growingappearance of F. hepatica resistance to Triclabendazole (TCBZ), an anthelmintic with activity over adult and young flukes.F. hepatica has eight Glutathione S-Transferase (GST) isozymes, which are enzymes involved in the detoxification of a wide range of substrates through chemical conjugation with glutathione. In the present work we identified and characterized the GST mu gene isolated from the TCBZ-susceptible andTCBZ-resistant F. hepatica strains. Total RNA was transcribed into cDNA by reverse transcription and a 657 bp amplicon corresponding to the GST mu gene was obtained. The comparative genetic analysis ofthe GST mu gene of the TCBZ susceptible strain (Cullompton) and TCBZ resistant strain (Sligo) showed three nucleotide changes and one amino acid change at position 143 in the GST mu isozyme of the TCBZresistant strain.These results have potential relevance as they contribute better understand the mechanisms that generate resistance to anthelmintics