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Cantharidin Impedes Activity of Glutathione S-Transferase in the Midgut of Helicoverpa armigera Hübner

by Rashid Ahmed Khan 1,†, Ji Yuan Liu 1,†, Maryam Rashid 1,†, Dun Wang 1,2,* and Ya Lin Zhang 1,*
1
Key Laboratory of Plant Protection Resources and Pest Management, Ministry of Education, College of Plant Protection, Northwest A&F University, Yangling 712100, Shaanxi, China
2
Institute of Entomology, Northwest A&F University, Yangling 712100, Shaanxi, China
*
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Int. J. Mol. Sci. 2013, 14(3), 5482-5500; https://doi.org/10.3390/ijms14035482
Received: 17 December 2012 / Revised: 16 February 2013 / Accepted: 26 February 2013 / Published: 8 March 2013
(This article belongs to the Section Biochemistry)
Previous investigations have implicated glutathione S-transferases (GSTs) as one of the major reasons for insecticide resistance. Therefore, effectiveness of new candidate compounds depends on their ability to inhibit GSTs to prevent metabolic detoxification by insects. Cantharidin, a terpenoid compound of insect origin, has been developed as a bio-pesticide in China, and proves highly toxic to a wide range of insects, especially lepidopteran. In the present study, we test cantharidin as a model compound for its toxicity, effects on the mRNA transcription of a model Helicoverpa armigera glutathione S-transferase gene (HaGST) and also for its putative inhibitory effect on the catalytic activity of GSTs, both in vivo and in vitro in Helicoverpa armigera, employing molecular and biochemical methods. Bioassay results showed that cantharidin was highly toxic to H. armigera. Real-time qPCR showed down-regulation of the HaGST at the mRNA transcript ranging from 2.5 to 12.5 folds while biochemical assays showed in vivo inhibition of GSTs in midgut and in vitro inhibition of rHaGST. Binding of cantharidin to HaGST was rationalized by homology and molecular docking simulations using a model GST (1PN9) as a template structure. Molecular docking simulations also confirmed accurate docking of the cantharidin molecule to the active site of HaGST impeding its catalytic activity. View Full-Text
Keywords: glutathione S-transferases; Helicoverpa armigera; cantharidin; mRNA; molecular docking simulations glutathione S-transferases; Helicoverpa armigera; cantharidin; mRNA; molecular docking simulations
MDPI and ACS Style

Khan, R.A.; Liu, J.Y.; Rashid, M.; Wang, D.; Zhang, Y.L. Cantharidin Impedes Activity of Glutathione S-Transferase in the Midgut of Helicoverpa armigera Hübner. Int. J. Mol. Sci. 2013, 14, 5482-5500.

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