Cantharidin is a highly potent toxin produced by insects belonging to the order Coleoptera and family Meloidae. The insecticidal activity of cantharidin against different orders of insects has been well documented. Although it is highly effective, its extraction and synthesis is very tedious. Consequently, much work is underway to synthesize the bioactive analogs of norcantharidin and study their relative structures. In this study, we investigate the acute and chronic toxicological effects of cantharidin and endothall, an analog of norcantharidin, using an age-stage-based two-sex life table methodology. Results reveal the acute toxicity of these compounds to Spodoptera litura Fabricius (Lepidoptera: Noctuidae), with the LC50 of cantharidin being 2.10 and endothall being 3.72 ppm, after 72 h posttreatment. Although both the compounds negatively affected the intrinsic rate of population increase (r), finite rate of increase (λ), net reproduction rate (R0), mean generation time (T), doubling time (DT), relative fitness (Rf), biotic potential, and longevity, cantharidin was slightly more effective. Among the reproductive parameters, fecundity was severely affected by cantharidin, which reduced offspring to 42 compared to 528 per female in the control cohort. Both cantharidin and endothall caused similar physiological changes such as weight reduction, wing malformation, and pupal deformities. These findings demonstrate that both cantharidin and endothall are highly toxic to S. litura, particularly in their chronic effects on population parameters. This will help us to understand the biological and ecological interactions in agricultural cropping systems and how their application will modify insect herbivory.
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Int J Parasitol
August 2019
Department of Immunology, College of Basic Medical Science, China Medical University, Shenyang, Liaoning 110122, China; Department of Internal Medicine, Morsani College of Medicine, University of South Florida, 3720 Spectrum Boulevard, Suite 304, Tampa, FL 33612-9415, USA. Electronic address:
Sexual development in malaria parasites involves multiple signal transduction pathways mediated by reversible protein phosphorylation. Here, we functionally characterised a protein phosphatase, Ser/Thr protein phosphatase 5 (PbPP5), during sexual development of the rodent malaria parasite Plasmodium berghei. The recombinant protein phosphatase domain displayed obvious protein phosphatase activity and was sensitive to PP1/PP2A inhibitors including cantharidic acid (IC = 122.
View Article and Find Full Text PDFJ Econ Entomol
December 2018
Key Laboratory of Plant Protection Resources and Pest Management, Ministry of Education, College of Plant Protection, Northwest A&F University, Yangling, Shaanxi, China.
Cantharidin is a highly potent toxin produced by insects belonging to the order Coleoptera and family Meloidae. The insecticidal activity of cantharidin against different orders of insects has been well documented. Although it is highly effective, its extraction and synthesis is very tedious.
View Article and Find Full Text PDFSci Rep
July 2015
Key Laboratory of Plant Protection Resources &Pest Management of the Ministry of Education, Northwest A&F University, Yangling 712100, Shaanxi, China.
Serine/threonine protein phosphatase 5 (PP5) is a promising novel target for anticancer therapies. This work aims to uncover the key interactions at the atomic level between PP5 and three inhibitors (cantharidin, norcantharidin and endothall). We found that, unlike previous report, Arg 100 contributes less to PP5-inhibitor binding, and the residues His 69, Asn 128, His 129, Arg 225, His 252 and Arg 250 are of importance to PP5-inhibitor binding.
View Article and Find Full Text PDFPLoS One
June 2015
Key Laboratory of Plant Protection Resources & Pest Management of the Ministry of Education, Northwest A&F University, Yangling, Shaanxi, China.
Protein phosphatase 5 (PP5), a unique member of serine/threonine phosphatases, regulates a variety of biological processes. We obtained full-length PP5 cDNAs from three lepidopteran insects, Helicoverpa armigera, Mythimna separata and Plutella xylostella, encoding predicted proteins of 490 (55.98 kDa), 490 (55.
View Article and Find Full Text PDFInt J Mol Sci
December 2013
Key Laboratory of Plant Protection Resources and Pest Management of Ministry of Education, Northwest A&F University, Yangling 712100, China.
Protein phosphatase 5 (PP5) is a unique member of serine/threonine phosphatases which has been recognized in regulation of diverse cellular processes. A cDNA fragment encoding PP5 (EcPP5) was cloned and characterized from the cantharidin-producing blister beetle, E. chinensis.
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