np0c00480_si_001.pdf (283.45 kB)
Glutathione Transferases: Surrogate Targets for Discovering Biologically Active Compounds
journal contributionposted on 2020-10-01, 17:14 authored by Muriel Barbier, Thomas Perrot, Guillaume Salzet, Nadine Amusant, Stéphane Dumarçay, Philippe Gérardin, Mélanie Morel-Rouhier, Rodnay Sormani, Eric Gelhaye
Glutathione transferases comprise a large class of multifunctional enzymes, some involved in detoxification pathways. Since these enzymes are able to interact with potentially toxic molecules, they could be used as targets to screen for compounds with biological activity. To test this hypothesis, glutathione transferases (GSTs) from the white-rot fungus Trametes versicolor have been used to screen for antifungal molecules from a library of tropical wood extracts. The interactions between a set of six GSTs from the omega class and 116 extracts from 21 tropical species were quantified using a high-throughput thermal shift assay. A correlation between these interactions and the antifungal properties of the tested extracts was demonstrated. This approach has been extended to the fractionation of an Andira coriacea extract and led to the detection of maackiain and lapachol in this wood. Altogether, the present results supported the hypothesis that such detoxification enzymes could be used to detect biologically active molecules.
GSTglutathione transferasesantifungal propertiesantifungal moleculesAndira coriaceaCompounds Glutathione transferaseswood extractsdetoxification enzymesdetoxification pathwaysGlutathione Transferaseswhite-rot fungus Trametes versicoloromega classinteractionhypothesisshift assay116 extractsmultifunctional enzymes