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

Abstract 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...

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Autores principales: Vanessa Eyraud, Séverine Balmand, Lamis Karaki, Isabelle Rahioui, Catherine Sivignon, Agnès F. Delmas, Corinne Royer, Yvan Rahbé, Pedro Da Silva, Frédéric Gressent
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spelling oai:doaj.org-article:7193b3596f33475aa472de278324cf702021-12-02T15:05:38ZThe interaction of the bioinsecticide PA1b (Pea Albumin 1 subunit b) with the insect V-ATPase triggers apoptosis10.1038/s41598-017-05315-y2045-2322https://doaj.org/article/7193b3596f33475aa472de278324cf702017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-05315-yhttps://doaj.org/toc/2045-2322Abstract 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.Vanessa EyraudSéverine BalmandLamis KarakiIsabelle RahiouiCatherine SivignonAgnès F. DelmasCorinne RoyerYvan RahbéPedro Da SilvaFrédéric GressentNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-10 (2017)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Vanessa Eyraud
Séverine Balmand
Lamis Karaki
Isabelle Rahioui
Catherine Sivignon
Agnès F. Delmas
Corinne Royer
Yvan Rahbé
Pedro Da Silva
Frédéric Gressent
The interaction of the bioinsecticide PA1b (Pea Albumin 1 subunit b) with the insect V-ATPase triggers apoptosis
description Abstract 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.
format article
author Vanessa Eyraud
Séverine Balmand
Lamis Karaki
Isabelle Rahioui
Catherine Sivignon
Agnès F. Delmas
Corinne Royer
Yvan Rahbé
Pedro Da Silva
Frédéric Gressent
author_facet Vanessa Eyraud
Séverine Balmand
Lamis Karaki
Isabelle Rahioui
Catherine Sivignon
Agnès F. Delmas
Corinne Royer
Yvan Rahbé
Pedro Da Silva
Frédéric Gressent
author_sort Vanessa Eyraud
title The interaction of the bioinsecticide PA1b (Pea Albumin 1 subunit b) with the insect V-ATPase triggers apoptosis
title_short The interaction of the bioinsecticide PA1b (Pea Albumin 1 subunit b) with the insect V-ATPase triggers apoptosis
title_full The interaction of the bioinsecticide PA1b (Pea Albumin 1 subunit b) with the insect V-ATPase triggers apoptosis
title_fullStr The interaction of the bioinsecticide PA1b (Pea Albumin 1 subunit b) with the insect V-ATPase triggers apoptosis
title_full_unstemmed The interaction of the bioinsecticide PA1b (Pea Albumin 1 subunit b) with the insect V-ATPase triggers apoptosis
title_sort interaction of the bioinsecticide pa1b (pea albumin 1 subunit b) with the insect v-atpase triggers apoptosis
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/7193b3596f33475aa472de278324cf70
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