Insecticidal effect of Canavalia ensiformis major urease on nymphs of the milkweed bug Oncopeltus fasciatus and characterization of digestive peptidases

Defferrari, Marina S.; Demartini, Diogo Ribeiro; Marcelino, Thiago Beltram; Pinto, Paulo Marcos; Carlini, Célia R.

doi:10.1016/j.ibmb.2011.02.008

Cited by 37 publications

(23 citation statements)

References 63 publications

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“…The activity of cathepsin D-like peptidase(s) was assayed using the specific synthetic fluorogenic substrate Abz-AIAFFSRQ-EDDnp (Sorgine et al, 2000;Piovesan et al, 2008;Defferrari et al, 2011).…”

Section: First Blood Mealmentioning

confidence: 99%

Biochemical changes in the transition from vitellogenesis to follicular atresia in the hematophagous Dipetalogaster maxima (Hemiptera: Reduviidae)

Aguirre

Fruttero

Leyria

et al. 2011

Insect Biochemistry and Molecular Biology

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Section: First Blood Mealmentioning

confidence: 99%

Biochemical changes in the transition from vitellogenesis to follicular atresia in the hematophagous Dipetalogaster maxima (Hemiptera: Reduviidae)

Aguirre

Fruttero

Leyria

et al. 2011

Insect Biochemistry and Molecular Biology

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“…It is resistant to insects and microorganisms and suppresses the growth of nematodes [10, 11]. In agriculture, C. ensiformis is used as a green cover for the nutritional enrichment of soils, because it fixes nitrogen efficiently.…”

Section: Introductionmentioning

confidence: 99%

Proteases fromCanavalia ensiformis: Active and Thermostable Enzymes with Potential of Application in Biotechnology

Gonçalves

Barbosa

Silva-López

2016

Biotechnology Research International

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Extracts of leaves, seeds, roots, and stem from a tropical legume, C. ensiformis, were prepared employing buffers and detergent in aqueous solution. Leaf extracts had the highest protein content and the most pronounced peptidase activity with optimal pH in the neutral to alkaline range. All extracts exhibited peaks of activity at various pH values, suggesting the presence of distinctive classes of proteases. N-α-Tosyl-L-arginine methyl ester hydrolysis was maximal at 30°C to 60°C and peptidase activity from all extracts presented very good thermal stability after 24 h incubation at 70°C. C. ensiformis proteases exhibited molecular masses of about 200–57, 40–37, and 20–15 kDa by SDS-PAGE analysis. These enzymes cleaved hemoglobin, bovine serum albumin, casein, and gelatin at different levels. Serine and metalloproteases are the major proteases in C. ensiformis extracts, modulated by divalent cations, stable at 1% of surfactant Triton X-100 and at different concentrations of the reducing agent β-mercaptoethanol. Thus, C. ensiformis expresses a particular set of proteases in distinctive organs with high activity and stability, making this legume an important source of proteases with biotechnological potential.

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“…On the other hand, additional data suggested that in nymphs of D. peruvianus , a metalloprotease is involved in the limited proteolysis of ureases and release of the entomotoxic peptide. The in vitro hydrolysis of JBURE-I by midgut homogenates of nymphs of Oncopeltus fasciatus also produces a peptide of ~10 kDa that is recognized by Jaburetox-2Ec antibodies [37]. Since no metalloprotease activity was detected in midgut homogenates of this insect, it is possible that another class of enzyme is involved in O. fasciatus in the limited proteolysis of ureases.…”

Section: Urease Processing By Insect Digestive Enzymesmentioning

confidence: 99%

Plant Ureases and Related Peptides: Understanding Their Entomotoxic Properties

Stanisçuaski

Carlini

2012

Toxins

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Recently, ureases were included in the arsenal of plant defense proteins, alongside many other proteins with biotechnological potential such as insecticides. Isoforms of Canavalia ensiformis urease (canatoxin—CNTX and jack bean urease—JBURE-I) are toxic to insects of different orders. This toxicity is due in part to the release of a 10 kDa peptide from the native protein, by cathepsin-like enzymes present in the insect digestive tract. The entomotoxic peptide, Jaburetox-2Ec, exhibits potent insecticidal activity against several insects, including many resistant to the native ureases. JBURE-I and Jaburetox-2Ec cause major alterations of post-feeding physiological processes in insects, which contribute to, or can be the cause of, their entomotoxic effect. An overview of the current knowledge on plant urease processing and mechanisms of action in insects is presented in this review.

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Insecticidal effect of Canavalia ensiformis major urease on nymphs of the milkweed bug Oncopeltus fasciatus and characterization of digestive peptidases

Cited by 37 publications

References 63 publications

Biochemical changes in the transition from vitellogenesis to follicular atresia in the hematophagous Dipetalogaster maxima (Hemiptera: Reduviidae)

Biochemical changes in the transition from vitellogenesis to follicular atresia in the hematophagous Dipetalogaster maxima (Hemiptera: Reduviidae)

Proteases fromCanavalia ensiformis: Active and Thermostable Enzymes with Potential of Application in Biotechnology

Plant Ureases and Related Peptides: Understanding Their Entomotoxic Properties

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