Search results for "Insecticidal proteins"

showing 7 items of 7 documents

Studies on the insecticidal mechanism of Bacillus thuringiensis Vip3A and Cry proteins

2022

El control de plagas y patógenos ha tenido un efecto importante en la mejora del rendimiento de los sistemas agrícolas a nivel mundial. Diferentes tipos de insecticidas químicos se han usado extensivamente durante mucho tiempo para el control de plagas de insectos. Debido a la aparición de resistencias, problemas de contaminación de aguas y problemas de salud humana causados por dichos insecticidas de síntesis, la agricultura moderna necesita una estrategia de gestión integrada de plagas más saludable, respetuosa con el medio ambiente y sostenible. El uso de Bacillus thuringiensis (Bt) y sus proteínas insecticidas para el control de plagas es una de las estrategias biotecnológicas más impor…

pest managementinsecticidal proteinsvip3 proteinsUNESCO::CIENCIAS DE LA VIDAbacillus thuringiensisBt:CIENCIAS DE LA VIDA [UNESCO]
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Reduced membrane-bound alkaline phosphatase does not affect binding of Vip3Aa in a Heliothis virescens resistant colony

2020

The Vip3Aa insecticidal protein from Bacillus thuringiensis (Bt) is produced by specific transgenic corn and cotton varieties for efficient control of target lepidopteran pests. The main threat to this technology is the evolution of resistance in targeted insect pests and understanding the mechanistic basis of resistance is crucial to deploy the most appropriate strategies for resistance management. In this work, we tested whether alteration of membrane receptors in the insect midgut might explain the &gt

HELIOTHIS-VIRESCENSInsecticidesHealth Toxicology and Mutagenesislcsh:MedicinePROTEIN0601 Biochemistry and Cell BiologyToxicologyBiotecnologiaInsecticide ResistanceBacillus thuringiensisSITES0303 health sciencesbiologyChemistryfood and beveragesPlants Genetically ModifiedLepidopteraBiochemistryFood Science & TechnologyInsect ProteinsAlkaline phosphatase1115 Pharmacology and Pharmaceutical Sciencestobacco budwormLife Sciences & BiomedicineSPODOPTERA-FRUGIPERDA MIDGUTProtein BindingEXPRESSIONBrush borderBacillus thuringiensisCRY1ACArticleVESICLES03 medical and health sciencesBACILLUS-THURINGIENSISBacterial ProteinsDownregulation and upregulationinsecticidal proteinsCell surface receptor<i>Bacillus thuringiensis</i>AnimalsCROPS030304 developmental biologyScience & TechnologyGenetically modified maizeHeliothis virescens030306 microbiologylcsh:RfungiMembrane ProteinsMidgutAlkaline Phosphatasebiology.organism_classificationTOXIN RESISTANCEinsect resistanceProteïnes
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Structural Domains of the Bacillus thuringiensis Vip3Af Protein Unraveled by Tryptic Digestion of Alanine Mutants

2019

Vip3 proteins are increasingly used in insect control in transgenic crops. To shed light on the structure of these proteins, we used the approach of the trypsin fragmentation of mutants altering the conformation of the Vip3Af protein. From an alanine scanning of Vip3Af, we selected mutants with an altered proteolytic pattern. Based on protease digestion patterns, their effect on oligomer formation, and theoretical cleavage sites, we generated a map of the Vip3Af protein with five domains which match some of the domains proposed independently by two in silico models. Domain I ranges amino acids (aa) 12&ndash

Health Toxicology and MutagenesisIn silicoMutantlcsh:MedicineToxicologyCleavage (embryo)03 medical and health sciencesagricultural_sciences_agronomytetrameric proteinsTetramerinsecticidal proteinsmedicineBt toxins030304 developmental biologychemistry.chemical_classificationAlanine0303 health sciences030306 microbiologyChemistrylcsh:RAlanine scanningtrypsin cleavageTrypsinAmino acidBiochemistrydomain mapmedicine.drugToxins
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Insecticidal spectrum and mode of action of the Bacillus thuringiensis Vip3Ca insecticidal protein.

2016

The Vip3Ca protein, discovered in a screening of Spanish collections of Bacillus thuringiensis, was known to be toxic to Chrysodeixis chalcites, Mamestra brassicae and Trichoplusia ni. In the present study, its activity has been tested with additional insect species and we found that Cydia pomonella is moderately susceptible to this protein. Vip3Ca (of approximately 90 kDa) was processed to an approximately 70 kDa protein when incubated with midgut juice in all tested species. The kinetics of proteolysis correlated with the susceptibility of the insect species to Vip3Ca. The activation was faster to slower in the following order: M. brassicae (susceptible), Spodoptera littoralis (moderately…

0301 basic medicineInsecticides030106 microbiologyInsect pest controlAgrotis ipsilonVegetative insecticidal proteinsMothsmedicine.disease_causeMicrobiologyCiencias BiológicasInsecticide Resistance03 medical and health sciencesBiología Celular MicrobiologíaBacterial ProteinsBacillus thuringiensisBotanyTrichoplusiamedicineAnimalsSpodoptera littoralisPest Control BiologicalEcology Evolution Behavior and SystematicsHistological localizationbiologyToxinfungiVEGETATIVE INSECTICIDAL PROTEINSMidgutBioinsecticidesApical membranebiology.organism_classificationCROP PROTECTIONChrysodeixis chalcitesBIOINSECTICIDES030104 developmental biologyCrop protectionINSECT PEST CONTROLHISTOLOGICAL LOCALIZATIONCIENCIAS NATURALES Y EXACTASJournal of invertebrate pathology
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Unshared binding sites for Bacillus thuringiensis Cry3Aa and Cry3Ca proteins in the weevil Cylas puncticollis (Brentidae)

2016

Bacillus thuringiensis Cry3Aa and Cry3Ca proteins have been reported to be toxic against the African sweetpotato pest Cylas puncticollis. In the present work, the binding sites of these proteins in C. puncticollis brush border vesicles suggest the occurrence of different binding sites, but only one of them is shared. Our results suggest that pest resistance mediated by alteration of the shared Cry-receptor binding site might not render both Cry proteins ineffective.

endocrine systemAfrican sweetpotato weevilBacillus thuringiensis ToxinsShort CommunicationBinding sitesInsect controlfungiBacillus thuringiensisToxicologyBinding CompetitiveInsect resistance managementEndotoxinsHemolysin ProteinsInsecticidal proteinsBacterial ProteinsAnimalsWeevilsToxicon
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Characterisation of the structure-function relationship of the Bacillus thuringiensis Vip3A insecticidal proteins

2017

L'agricultura contemporània exigeix cada cop més un ús sostenible d’agroquímics per tal de reduir l'impacte ambiental i el risc per la salut del consumidor. Alguns bacteris entomopatògens produeixen proteïnes insecticides que s'acumulen en cossos d'inclusió o cristalls paraesporales (com ara les proteïnes Cry i Cyt), així com proteïnes insecticides que són secretades al medi de cultiu. Entre les últimes, hi ha les proteïnes Vip, que es divideixen en quatre famílies d'acord amb la seva identitat d'aminoàcids. Les proteïnes Vip1 i Vip2 actuen com toxines binàries i són tòxiques per a alguns coleòpters i hemípters. Per la família de les Vip4, que és l’última família de proteïnes Vip descoberta…

Insecticidal proteinsBiological controlBacillus thuringiensisProtein structureProtein functionIPMVip3A proteins
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The Independent Biological Activity of Bacillus thuringiensis Cry23Aa Protein Against Cylas puncticollis

2020

The Cry23Aa/Cry37Aa proteins from Bacillus thuringiensis (Bt) have been described toxic to Cylas puncticollis larvae. In general, it is believed that Cry23Aa and Cry37Aa act jointly to exert the insecticidal activity, while there is no evidence of their toxicity individually. Therefore, in the present study, the contribution of each protein in the insecticidal activity toward C. puncticollis larvae has been assessed. The results showed that both proteins were toxic for C. puncticollis larvae when tested individually. Contrary to what was claimed previously, our results suggest that the presence of both proteins is not necessary to exert toxicity against C. puncticollis larvae. Also, the bin…

Microbiology (medical)Agriculture and Food SciencesSWEET-POTATO WEEVILlcsh:QR1-502sweet potato weevilsbinary toxinMicrobiologylcsh:Microbiology03 medical and health sciencesmode of actioninsecticidal proteinsBacillus thuringiensisBioassayCry37AaBinding siteSPHAERICUS TOXINMode of action030304 developmental biologybinding assay0303 health sciencesPore-forming toxinLarvabiology030306 microbiologyCRYSTAL PROTEINCOMPONENTSfungiMidgutBiological activityBORDER MEMBRANE-VESICLESENTOMOPATHOGENIC FUNGIbiology.organism_classificationEFFICACYBiochemistrybioassayCOLEOPTERABRUNNEUSRESISTANCEFrontiers in Microbiology
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