0000000000516132

AUTHOR

Souad Rouis

showing 2 related works from this author

Ephestia kuehniella tolerance to Bacillus thuringiensis Cry1Aa is associated with reduced oligomer formation

2016

The basis of the different susceptibility of Ephestia kuehniella to the Cry1Aa and Cry1Ac δ-endotoxins from Bacillus thuringiensis kurstaki BNS3 was studied. Both toxins bound specifically to the BBMV of E. kuehniella. The result of the ligand blot showed that Cry1Ac bound to three putative receptors of about 100, 65 and 80 kDa and Cry1Aa interacted only with a 100 kDa protein. Pronase digestion of the BBMV-bound toxins was used to analyze the toxin insertion. Both toxins inserted into the BBMV as monomers however, a 14 kDa peptide of α4-α5 which correspond to the oligomeric form of this peptide was detected in case of Cry1Ac only. Analysis of the in vitro oligomerisation of these toxins in…

0301 basic medicineProtein ConformationBacillus thuringiensisBiophysicsPeptidemedicine.disease_causeBiochemistryOligomerHemolysin Proteins03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsBacillus thuringiensismedicineAnimalsReceptorMolecular Biologychemistry.chemical_classificationBacillus thuringiensis Toxins030102 biochemistry & molecular biologybiologyToxinfungiCell BiologyLigand (biochemistry)biology.organism_classificationEndotoxinsLepidopteraBlot030104 developmental biologyBiochemistryCry1AcchemistryProtein MultimerizationBiochemical and Biophysical Research Communications
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Investigation of the steps involved in the difference of susceptibility of Ephestia kuehniella and Spodoptera littoralis to the Bacillus thuringiensi…

2011

BUPM95 is a Bacillus thuringiensis subsp. kurstaki strain producing the Vip3Aa16 toxin with an interesting insecticidal activity against the Lepidopteran larvae Ephestia kuehniella. Study of different steps in the mode of action of this Vegetative Insecticidal Protein on the Mediterranean flour moth (E. kuehniella) was carried out in the aim to investigate the origin of the higher susceptibility of this insect to Vip3Aa16 toxin compared to that of the Egyptian cotton leaf worm Spodoptera littoralis. Using E. kuehniella gut juice, protoxin proteolysis generated a major band corresponding to the active toxin and another band of about 22kDa, whereas the activation of Vip3Aa16 by S. littoralis …

ProteasesProteolysismedia_common.quotation_subjectBacillus thuringiensisDrug ResistanceActivationBacillusInsectMothsSpodopteraBiologymedicine.disease_causeMicrobiologyBacterial ProteinsVip3Aa16Bacillus thuringiensismedicineAnimalsPest Control BiologicalSpodoptera littoralisEcology Evolution Behavior and SystematicsEphestia kuehniellamedia_commonmedicine.diagnostic_testToxinfungiSpodoptera littoralisbiology.organism_classificationMediterranean flour mothLarvaBacillusthuringiensisMidgut putative receptorJournal of Invertebrate Pathology
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