Location: Subtropical Insects and Horticulture Research
Title: Toxicity of the jaburetox peptide to the multi-host insect-pest Helicoverpa armigera (Lepidoptera: Noctuidae) larvaeAuthor
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DIDONE, DIELLI - University Of Passo Fundo |
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LOPES, FERNANDA - Federal University Of Rio Grande Do Sul |
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MARTINELLI, ANNE - Federal University Of Rio Grande |
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CECCON, CASSIA - University Of Passo Fundo |
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TEIXEIRA, TIAGO - University Of Passo Fundo |
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DE SILVA, MARILIA - University Of Passo Fundo |
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SALVADORI, JOSE - University Of Passo Fundo |
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CARLINI, CELIA - Federal University Of Rio Grande |
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Shatters, Robert |
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GRANDO, MAGALI - University Of Passo Fundo |
Submitted to: Journal of Economic Entomology
Publication Type: Peer Reviewed Journal Publication Acceptance Date: 9/1/2021 Publication Date: 9/23/2021 Citation: Didone, D.A., Lopes, F.C., Martinelli, A., Ceccon, C.C., Teixeira, T., De Silva, M.R., Salvadori, J.R., Carlini, C.R., Shatters, R.G., Grando, M.F. Toxicity of the jaburetox peptide to the multi-host insect-pest Helicoverpa armigera (Lepidoptera: Noctuidae) larvae. Journal of Economic Entomology. 104(3):230-238. 2021. https://doi.org/10.1653/024.104.0313. DOI: https://doi.org/10.1653/024.104.0313 Interpretive Summary: Helicoverpa armigera, the old world cotton bollworm stands out for the extensive damage it can cause to numerous crop types. Although this pest has not established in the U.S. it has established in South America and threatens the U.S. This paper presents the testing of a natural occurring peptide from Jack bean that could be used in a biologically-based control strategy for this aggressive pest. The peptide, called Jaburetox (JBTX), is a proteolytic fragment of a Jack bean enzyme called urease and has previously been shown to have entomotoxic activity against a number of insects. In one experiment, freshly hatched Helicoverpa armigera larvae were fed JBTX-peptide treated leaves (16 µg of JBTX per cm2 of leaf). The peptide induced higher mortality, abouy 70% mortality, than the controls. The peptide also caused a delay in the larvae development and reduction in feeding. In a second experiment, 3rd instar larvae were subjected to two treatments for nine days: (T1) 80 µg of JBTX per 5cm2 of leaf; and (T2) sodium phosphate buffer control. The JBTX treatment induced slower development and significantly higher mortality than the control at day six with 100% mortality by nine days. These results support further evaluation of the use of the JBTX peptide in control strategies for Helicoverpa armigera, including transgenic expression of this peptide in crops plants. Technical Abstract: Helicoverpa armigera (Hübner) (Lepidoptera: Noctuidae) stands out for the extensive damage it can cause to crops. The entomotoxic peptides fragments from Jack bean urease, Jaburetox (JBTX) and JBTX '-ß, present potential for controlling some insects species, and could provide an alternative for pest insect control in agricultural crops. This paper evaluated the effectiveness of these two peptides on behavior and survival of the Helicoverpa armigera larvae in two stages of development. Freshly hatched larvae were fed leaves for eight days with two peptide topical leaf treatments: (T1) 16 µg cm2 of JBTX; (T2) 16 µg cm2 of JBTX '-ß; and two control treatments: (T3) 20 mM pH7.5 of sodium phosphate buffer and (T4) distilled water. Both peptides induced higher mortality than the controls with the JBTX '-ß inducing greatest mortality during the first 6 days at which time both peptides were equally effective and caused ~70% mortality. Both peptide versions also cause a delay in the larvae development, but the larger peptide caused a greater reduction in feeding. In a second experiment, 3rd larvae were subjected to two treatments for nine days: (T1) 80 µg 5cm2 of JBTX; and (T2) sodium phosphate buffer control. The JBTX treatment induced slower development and significantly higher mortality than the control at day six with 100% mortality by nine days. These results support further evaluation of the use of the JBTX peptide in control strategies for Helicoverpa armigera, including transgenic expression of this peptide in crops plants. |