Sweet potato (Ipomoea batatas) trypsin inhibitors expressed in transgenic tobacco plants confer resistance against Spodoptera litura

Yeh, Kai‐Wun; Lin, Meng-Ting; Tuan, S.-J.; Chen, Y.-M.; Lin, Chien-Ching; Kao, Suey-Sheng

doi:10.1007/s002990050304

Cited by 118 publications

(63 citation statements)

References 14 publications

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“…When the trypsin PI MTI-2 was expressed at the highest level in tobacco and Arabidopsis transgenic plants, deleterious effects were observed on insect larvae, together with a reduction of leaf damage, thus providing effective pest resistance to the plant. These results are in agreement with those obtained by Yeh et al (1997) on the closely related pest, Spodoptera litura F, when expressing a sweet potato trypsin inhibitor in tobacco. On the contrary, when MTI-2 was expressed at lower levels in tobacco plants, larvae developed faster, were bigger than on control plants, and caused more damage to the leaves.…”

Section: Discussionsupporting

confidence: 82%

“…et al, 1996;Xu et al, 1996;Gatehouse et al, 1997;Yeh et al, 1997) resulted in dramatic changes in the reaction of S. littoralis larvae to transgenic leaf consumption. When the trypsin PI MTI-2 was expressed at the highest level in tobacco and Arabidopsis transgenic plants, deleterious effects were observed on insect larvae, together with a reduction of leaf damage, thus providing effective pest resistance to the plant.…”

Section: Discussionmentioning

confidence: 99%

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Opposite Effects on Spodoptera littoralis Larvae of High Expression Level of a Trypsin Proteinase Inhibitor in Transgenic Plants

et al. 1998

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This work illustrates potential adverse effects linked with the expression of proteinase inhibitor (PI) in plants used as a strategy to enhance pest resistance. Tobacco (Nicotiana tabacum L. cv Xanthi) and Arabidopsis [Heynh.] ecotype Wassilewskija) transgenic plants expressing the mustard trypsin PI 2 (MTI-2) at different levels were obtained. First-instar larvae of the Egyptian cotton worm (Spodoptera littoralis Boisd.) were fed on detached leaves of these plants. The high level of MTI-2 expression in leaves had deleterious effects on larvae, causing mortality and decreasing mean larval weight, and was correlated with a decrease in the leaf surface eaten. However, larvae fed leaves from plants expressing MTI-2 at the low expression level did not show increased mortality, but a net gain in weight and a faster development compared with control larvae. The low MTI-2 expression level also resulted in increased leaf damage. These observations are correlated with the differential expression of digestive proteinases in the larval gut; overexpression of existing proteinases on low-MTI-2-expression level plants and induction of new proteinases on high-MTI-2-expression level plants. These results emphasize the critical need for the development of a PI-based defense strategy for plants obtaining the appropriate PI-expression level relative to the pest's sensitivity threshold to that PI.

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Section: Discussionsupporting

confidence: 82%

Section: Discussionmentioning

confidence: 99%

Opposite Effects on Spodoptera littoralis Larvae of High Expression Level of a Trypsin Proteinase Inhibitor in Transgenic Plants

et al. 1998

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“…The use of proteinaceous inhibitors in insect control strategies has good potential, because insect digestive proteinases are promising targets in the control of various insects, including lepidopterans such as Manduca sexta [3], Heliothis zea [4], Spodoptera litura [5], and Lucilia cuprina [6], and also various coleopterans [7][8][9][10][11]. Despite several suggested physiological functions in plants [12][13][14], the inhibitors are known for their role in response to abiotic [15,16] biotic stresses, especially in plant defense processes against insect pest attack [9,[17][18][19][20].…”

Section: Introductionmentioning

confidence: 99%

Effect of trypsin inhibitor from Crotalaria pallida seeds on Callosobruchus maculatus (cowpea weevil) and Ceratitis capitata (fruit fly)

Gomes

Barbosa

Macedo

et al. 2005

Plant Physiology and Biochemistry

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“…Antitrypsin compounds are used in agriculture as pesticides, in food industry [32,33]. Therefore E. arvense extract can be used as a potential antitrypsin compound.…”

Section: Ftir Analysesmentioning

confidence: 99%

Kinetic and structural characterization of interaction between trypsin and Equisetum arvense extract

Uslu¹,

Bayraktar²,

Ceylan³

2014

Turk J Bioch

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Kinetic and structural characterization of interaction between trypsin and Equisetum arvense extract [Trypsin ve Equisetum arvense özütü arasındaki etkileşimin kinetik ve yapısal karakterizasyonu] ABSTRACT Objective: In this study the inhibitory effect of E. arvense extract on trypsin activity and the effect of trypsin on E. arvense extract were studied. In addition the nature of the interaction between the extract and trypsin was investigated. Methods: The inhibitory effect ethanol extract of E. arvense on trypsin activity was determined using trypsin enzyme assay. The structural effects of the extract-trypsin interaction for the extract were analyzed by FTIR. Finally, the HPLC analyses were carried out to analyze the individual components of the extract and the supernatant and soluble precipitate phases. Results: E. arvense extract was found to decrease total percent activity of trypsin to 5% in 24 hour at 24 °C. FTIR analyses indicated that the interaction between trypsin and E. arvense extract caused changes in the structure and hydrogen bonding behavior and composition of the extract proteins. These interactions also caused the extract lipids to accumulate in the insoluble precipitate phase. Most of the phenolics remained in the supernatant phase enhancing the inactivation of trypsin. However, the precipitated compounds were shown to be of apolar in nature as shown in the HPLC chromatograms. Conclusion:The methods that were used showed that the high phenolic content of E. arvense was the main reason for the inhibition of trypsin enzyme activity by denaturing the enzyme. of 1:20. The dry leafs particles were shaked in the solution for overnight at 300 rpm at 24 °C. After the centrifugation at 2000xg for 5 minutes the supernatant was collected into 50 ml falcon tubes. The alcohol in the liquid phase was evaporated with a rotary evaporator. The aqueous extract was frozen for 24 hours and then freeze dried in a lyophilizer (Telstar-Cryodos). Preparation of inhibition solutionE. arvense extract was dissolved in distilled water to a final concentration of 10 mg/ml. By serial dilutions of stock solution 2 mg/ml, 0.2 mg/ml and 0.02 mg/ml concentrations were prepared. Preparation of trypsin solutionBovine pancreatic trypsin was purchased from Fluka Analytical (cat.93610) and used without further purification. Lyophilized powder of bovine pancreatic trypsin (Fluka Analytical, USA) was dissolved in 1 mM HCl to a final concentration of 0.1 mg/ml. Determination of enzyme kineticsTrypsin catalyzes the hydrolysis of N-benzoyl-L-arginine ethyl ester (BAEE) to N-benzoyl-L-arginine (BA) and ethanol. The slope of the absorbance versus time graph was the production rate of BA at pH 7.6.The reaction was held in a total volume of 3.2 ml quartz cuvette at 25 °C. The unit of trypsin activity was previously determined as 1 µmol BA produced per minute at 253 nm, at pH 7.6 and 25 °C. The reaction was carried out in 100 mM Tris buffer solution. To determine absorption of blank solution, 3050 μl tris buffer and 150 μl of BAEE solution ...

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Sweet potato (Ipomoea batatas) trypsin inhibitors expressed in transgenic tobacco plants confer resistance against Spodoptera litura

Cited by 118 publications

References 14 publications

Opposite Effects on Spodoptera littoralis Larvae of High Expression Level of a Trypsin Proteinase Inhibitor in Transgenic Plants

Opposite Effects on Spodoptera littoralis Larvae of High Expression Level of a Trypsin Proteinase Inhibitor in Transgenic Plants

Effect of trypsin inhibitor from Crotalaria pallida seeds on Callosobruchus maculatus (cowpea weevil) and Ceratitis capitata (fruit fly)

Kinetic and structural characterization of interaction between trypsin and Equisetum arvense extract

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