Insecticidal effects of canatoxin on the cotton stainer bug Dysdercus peruvianus (Hemiptera: Pyrrhocoridae)

Stanisçuaski, Fernanda; Ferreira-DaSilva, C.T.; Mulinari, Fernanda; Pires-Alves, Melissa; Carlini, Célia R.

doi:10.1016/j.toxicon.2005.01.014

Cited by 57 publications

(72 citation statements)

References 17 publications

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“…However, it has been reported that canatoxin, a variant form of urease isolated from jackbean seeds was shown to be proteolytically activated by insect cathepsin-like enzymes (mainly cathepsins B and D) to produce entomotoxic peptide(s). Canatoxin-derived peptide (MW 10 kDa) displays insecticidal activity against insects of Coleoptera (beetles) and Hemiptera (bugs) orders, such as the cowpea weevil, Callosobruchus maculatus, the kissing bug , Rhodnius prolixus, the cotton stainer bug, Dysdercus peruvianus and the green soybean stink bug, Nezara viridula (Carlini and Grossi-de-Sa, 2002;Staniscuaski et al, 2005). Also, ureases from soybean and jackbean plants exhibited an important insecticidal activity on the cotton stainer bug Dysdercus peruvianus independently of their ureolytic activity (Follmer et al, 2004).…”

Section: Other Entomopathogenic Factors: Zwittermicin a Urease And Hcnmentioning

confidence: 99%

Bacillus thuringiensis beyond insect biocontrol: plant growth promotion and biosafety of polyvalent strains

et al. 2007

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The entomopathogenic bacterium Bacillus thuringiensis is widely used for the control of many agricultural insect pests and vectors of human diseases. Several studies reported also on its antibacterial and antifungal activities. However, to our knowledge there were no studies dealing with its capacity to act as a plant growth promoting bacterium. This review surveys the potential of B. thuringiensis as a polyvalent biocontrol agent, a biostimulator and biofertiliser bacterium that could promote the plant growth. Also, discussed is the safety of B. thuringiensis as a bacterium phylogenetically closely related to Bacillus cereus the opportunistic human pathogen and Bacillus anthracis, the etiological agent of anthrax.

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Section: Other Entomopathogenic Factors: Zwittermicin a Urease And Hcnmentioning

confidence: 99%

Bacillus thuringiensis beyond insect biocontrol: plant growth promotion and biosafety of polyvalent strains

et al. 2007

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“…Calculation of the structure of Jaburetox using NMR spectroscopy NOE cross-peaks were identified, assigned and integrated in 15 N-edited and 13 C-edited 3D NOESY-HSQC spectra TD is the total number of real+imaginary points collected. SI is the total number of real+imaginary points before the Fourier transform.…”

Section: Differential Scanning Fluorimetrymentioning

confidence: 99%

“…This toxicity involves an internal polypeptide of 10 kDa (pepcanatox), released from the protein upon hydrolysis by cathepsin-like digestive enzymes of insects such as Callosobruchus maculatus, Rhodnius prolixus, Nezara viridula, Dysdercus peruvianus and Oncopeltus fasciatus [13][14][15][16] (Fig. 1A,B).…”

Section: Introductionmentioning

confidence: 99%

“…NMR signal assignment provided backbone secondary chemical shifts that indicated that Jaburetox has a low propensity to assume a stable secondary structure. 15 N relaxation studies revealed significant backbone mobility, especially in the N-terminal portion of the polypeptide. The solution structure of Jaburetox shows the presence of an a-helical motif close to the N terminus, together with two turn-like structures situated in the central portion of the protein and close to the C terminus.…”

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confidence: 99%

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Pliable natural biocide: Jaburetox is an intrinsically disordered insecticidal and fungicidal polypeptide derived from jack bean urease

et al. 2015

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Jaburetox is a polypeptide derived from jack bean (Canavalia ensiformis) urease and toxic to a broad spectrum of insects, phytopathogenic filamentous fungi and yeasts of medical importance. The elucidation of the structural basis for the mode of action of Jaburetox is the focus of this multifaceted study. Jaburetox in solution is a monomer of 11.0 kDa featuring a large hydrodynamic radius, suggestive of a disordered polypeptide. The intrinsically disordered nature of Jaburetox was theoretically predicted by a comprehensive bioinformatics analysis and experimentally confirmed by light scattering as well as by circular dichroism and NMR spectroscopy. NMR signal assignment provided backbone secondary chemical shifts that indicated that Jaburetox has a low propensity to assume a stable secondary structure. 15N relaxation studies revealed significant backbone mobility, especially in the N-terminal portion of the polypeptide. The solution structure of Jaburetox shows the presence of an a-helical motif close to the N terminus, together with two turn-like structures situated in the central portion of the protein and close to the C terminus. Similar regions were predicted as potential protein-protein interaction sites using computational tools. The knowledge of the structural properties of Jaburetox in solution is a key step to correlate its structural and biological activities.Abbreviations HSQC, heteronuclear single quantum coherence; IDP, intrinsically disordered protein; JBU, jack bean urease; LUV, large unilamellar vesicle;

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“…The kissing bug Rhodnius prolixus, and three economically important crop pests, the cowpea weevil Callosobruchus maculatus, the green stinkbug Nezara viridula and the cotton stainer bug Dysdercus peruvianus, are susceptible to the lethal effect of these proteins when they are added to their diets at 0.02 to 0.1% (w/w) levels (14,15). Susceptible insects have cathepsins of type B and D as their main digestive enzymes.…”

Section: Insecticidal Properties Of Plant Ureasesmentioning

confidence: 99%

Ureases display biological effects independent of enzymatic activity: Is there a connection to diseases caused by urease-producing bacteria?

Olivera‐Severo

Wassermann

Carlini

2006

Braz J Med Biol Res

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Ureases are enzymes from plants, fungi and bacteria that catalyze the hydrolysis of urea to form ammonia and carbon dioxide. While fungal and plant ureases are homo-oligomers of 90-kDa subunits, bacterial ureases are multimers of two or three subunit complexes. We showed that some isoforms of jack bean urease, canatoxin and the classical urease, bind to glycoconjugates and induce platelet aggregation. Canatoxin also promotes release of histamine from mast cells, insulin from pancreatic cells and neurotransmitters from brain synaptosomes. In vivo it induces rat paw edema and neutrophil chemotaxis. These effects are independent of ureolytic activity and require activation of eicosanoid metabolism and calcium channels. Helicobacter pylori, a Gram-negative bacterium that colonizes the human stomach mucosa, causes gastric ulcers and cancer by a mechanism that is not understood. H. pylori produces factors that damage gastric epithelial cells, such as the vacuolating cytotoxin VacA, the cytotoxin-associated protein CagA, and a urease (up to 10% of bacterial protein) that neutralizes the acidic medium permitting its survival in the stomach. H. pylori whole cells or extracts of its water-soluble proteins promote inflammation, activate neutrophils and induce the release of cytokines. In this paper we review data from the literature suggesting that H. pylori urease displays many of the biological activities observed for jack bean ureases and show that bacterial ureases have a secretagogue effect modulated by eicosanoid metabolites through lipoxygenase pathways. These findings could be relevant to the elucidation of the role of urease in the pathogenesis of the gastrointestinal disease caused by H. pylori.

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Insecticidal effects of canatoxin on the cotton stainer bug Dysdercus peruvianus (Hemiptera: Pyrrhocoridae)

Cited by 57 publications

References 17 publications

Bacillus thuringiensis beyond insect biocontrol: plant growth promotion and biosafety of polyvalent strains

Bacillus thuringiensis beyond insect biocontrol: plant growth promotion and biosafety of polyvalent strains

Pliable natural biocide: Jaburetox is an intrinsically disordered insecticidal and fungicidal polypeptide derived from jack bean urease

Ureases display biological effects independent of enzymatic activity: Is there a connection to diseases caused by urease-producing bacteria?

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