Fungitoxic and insecticidal plant polypeptides

Becker-Ritt, Arlete Beatriz; Carlini, Célia R.

doi:10.1002/bip.22097

Cited by 33 publications

(13 citation statements)

References 274 publications

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“…Almost one-third of world agricultural production would be lost due to pathogens or insects in the absence of chemical treatment, and even up to 80% in some areas 1 . Due to their efficiency and low cost, chemical pesticides are widely used around the world, but their extensive use leads to significant damage to ecosystems, for example by targeting different groups of beneficial insects or by impairing animal and human health 2 .…”

Section: Introductionmentioning

confidence: 99%

The interaction of the bioinsecticide PA1b (Pea Albumin 1 subunit b) with the insect V-ATPase triggers apoptosis

Eyraud

Balmand

Karaki

et al. 2017

Sci Rep

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PA1b (Pea Albumin 1, subunit b) peptide is an entomotoxin, extracted from Legume seeds, with a lethal activity towards several insect pests, such as mosquitoes, some aphids and cereal weevils. This toxin acts by binding to the subunits c and e of the plasma membrane H+-ATPase (V-ATPase) in the insect midgut. In this study, two cereal weevils, the sensitive Sitophilus oryzae strain WAA42, the resistance Sitophilus oryzae strain ISOR3 and the insensitive red flour beetle Tribolium castaneum, were used in biochemical and histological experiments to demonstrate that a PA1b/V-ATPase interaction triggers the apoptosis mechanism, resulting in insect death. Upon intoxication with PA1b, apoptotic bodies are formed in the cells of the insect midgut. In addition, caspase-3 enzyme activity occurs in the midgut of sensitive weevils after intoxication with active PA1b, but not in the midgut of resistant weevils. These biochemical data were confirmed by immuno-histochemical detection of the caspase-3 active form in the midgut of sensitive weevils. Immuno-labelling experiments also revealed that the caspase-3 active form and V-ATPase are close-localized in the insect midgut. The results concerning this unique peptidic V-ATPase inhibitor pave the way for the utilization of PA1b as a promising, more selective and eco-friendly insecticide.

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Section: Introductionmentioning

confidence: 99%

The interaction of the bioinsecticide PA1b (Pea Albumin 1 subunit b) with the insect V-ATPase triggers apoptosis

Eyraud

Balmand

Karaki

et al. 2017

Sci Rep

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“…Ureases and derived peptides show several biological activities including membrane disruption and permeabilization, fungicidal and insecticidal properties [9]. Jaburetox2Ec and jaburetox (JBTX) are the two first versions of a recombinant peptide with 91 amino acids, based on jack bean urease sequence, with a potent effect against insects, yeasts and filamentous fungi [10–12].…”

Section: Introductionmentioning

confidence: 99%

Jaburetox: update on a urease-derived peptide

Becker-Ritt

Portugal

Carlini

2017

J Venom Anim Toxins Incl Trop Dis

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Urease from Canavalia ensiformis seeds was the first enzyme ever to be crystallized, in 1926. These proteins, found in plants, bacteria and fungi, present different biological properties including catalytic hydrolysis of urea, and also enzyme-independent activities, such as induction of exocytosis, pro-inflammatory effects, neurotoxicity, antifungal and insecticidal properties. Urease is toxic to insects and fungi per se but part of this toxicity relies on an internal peptide (~11 kDa), which is released upon digestion of the protein by insect enzymes. A recombinant form of this peptide, called jaburetox (JBTX), was constructed using jbureII gene as a template. The peptide exhibits liposome disruption properties, and insecticidal and fungicidal activities. Here we review the known biological properties activities of JBTX, and comment on new ones not yet fully characterized. JBTX was able to cause mortality of Aedes aegypti larvae in a feeding assay whereas in a dose as low as of 0.1 μg it provoked death of Triatoma infestans bugs. JBTX (10−5–10−6 M) inhibits the growth of E. coli, P. aeruginosa and B. cereus after 24 h incubation. Multilamellar liposomes interacting with JBTX undergo reorganization of the membrane’s lipids as detected by small angle X-ray scattering (SAXS) studies. Encapsulating JBTX into lipid nanoparticles led to an increase of the peptide’s antifungal activity. Transgenic tobacco and sugarcane plants expressing the insecticidal peptide JBTX, showed increased resistance to attack of the insect pests Spodoptera frugiperda, Diatraea saccharalis and Telchin licus licus. Many questions remain unanswered; however, so far, JBTX has shown to be a versatile peptide that can be used against various insect and fungus species, and in new bacterial control strategies.

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“…Although fall armyworm feeds primarily on corn, this insect pest is also capable of feeding on many crops, including alfalfa, cotton, peanuts, grasses, tobacco and several others (Oakeshott et al, 2013). On the other hand, several insecticidal compounds have been isolated from plant sources (Becker-Ritt & Carlini, 2012;Coots, Lambdin, Grant, & Rhea, 2013). Plants are able to synthesize numerous compounds that include secondary metabolites and proteinaceous compounds, and many of these compounds may be synthesized in the plant's defense system.…”

Section: Introductionmentioning

confidence: 99%

Identification of a Novel 2S Albumin with Antitryptic Activity from Caryocar brasiliense Seeds

Costa¹,

Franco²,

Migliolo³

et al. 2015

JAS

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Proteinaceous and non-proteinaceous compounds with insecticidal activities have been isolated from plant sources. Here, protein extracts from Pequi seeds (Caryocar brasiliense) showed in vitro activity against trypsin-like enzymes. However, no activity was obtained against cancer cells, phytopathogenic fungi or human pathogenic bacteria. Further purification was performed by using trypsin-Sepharose affinity chromatography. Electrophoretic analysis revealed a single protein compound with molecular mass of approximately 14 kDa. Under reducing conditions, two peptides with smaller molecular masses were observed in SDS-PAGE, showing the presence of a heterodimeric peptide. MALDI-ToF/ToF sequencing was performed with a protein band removed from SDS-PAGE, and the sequence revealed high identity with the 2S albumin family. Purified peptide was challenged in vitro against bovine trypsin and Spodoptera frugiperda digestive enzymes by using BApNA as a substrate, showing high inhibitory activity in both cases. Data here reported suggest that a 2S albumin dimeric peptide could show biotechnological potential for S. frugiperda control. In summary, Cb2SA could be useful in controlling insect pests of agricultural interest.

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Fungitoxic and insecticidal plant polypeptides

Cited by 33 publications

References 274 publications

The interaction of the bioinsecticide PA1b (Pea Albumin 1 subunit b) with the insect V-ATPase triggers apoptosis

The interaction of the bioinsecticide PA1b (Pea Albumin 1 subunit b) with the insect V-ATPase triggers apoptosis

Jaburetox: update on a urease-derived peptide

Identification of a Novel 2S Albumin with Antitryptic Activity from Caryocar brasiliense Seeds

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