Search results for "Vip proteins"

showing 4 items of 4 documents

A Genomic and Proteomic Approach to Identify and Quantify the Expressed Bacillus thuringiensis Proteins in the Supernatant and Parasporal Crystal

2018

The combined analysis of genomic and proteomic data allowed us to determine which cry and vip genes are present in a Bacillus thuringiensis (Bt) isolate and which ones are being expressed. Nine Bt isolates were selected from Spanish collections of Bt based on their vip1 and vip2 gene content. As a first step, nine isolates were analyzed by PCR to select those Bt isolates that contained genes with the lowest similarity to already described vip1 and vip2 genes (isolates E-SE10.2 and O-V84.2). Two selected isolates were subjected to a combined genomic and proteomic analysis. The results showed that the Bt isolate E-SE10.2 codifies for two new vegetative proteins, Vip2Ac-like_1 and Sip1Aa-like_…

0301 basic medicineInsecticidesbiologyInsect pest controlHealth Toxicology and MutagenesisSingle typelcsh:Rcry proteinslcsh:Medicinevip proteinsToxicologybiology.organism_classificationMolecular biologyinsect pest control; crop protection; vip proteins; cry proteins03 medical and health sciences030104 developmental biologyinsect pest controlBacillus thuringiensisGeneProteïnescrop protection
researchProduct

Insights into the Structure of the Vip3Aa Insecticidal Protein by Protease Digestion Analysis

2017

Vip3 proteins are secretable proteins from Bacillus thuringiensis whose mode of action is still poorly understood. In this study, the activation process for Vip3 proteins was closely examined in order to better understand the Vip3Aa protein stability and to shed light on its structure. The Vip3Aa protoxin (of 89 kDa) was treated with trypsin at concentrations from 1:100 to 120:100 (trypsin:Vip3A, w:w). If the action of trypsin was not properly neutralized, the results of SDS-PAGE analysis (as well as those with Agrotis ipsilon midgut juice) equivocally indicated that the protoxin could be completely processed. However, when the proteolytic reaction was efficiently stopped, it was revealed t…

0301 basic medicineProteasesHealth Toxicology and MutagenesisSize-exclusion chromatographyBeta sheetBacillus thuringiensislcsh:MedicineBiologyToxicologyCleavage (embryo)ArticleProtein Structure Secondary03 medical and health sciencestrypsin inhibitorsBacterial ProteinsSDS-PAGE artefactprotease stabilitymedicinebacterial secreted proteinsAnimalsTrypsinMode of actionProtein secondary structureVip proteinsIntestinal Secretionslcsh:Rtoxin activationVip proteins; bacterial secreted proteins; toxin activation; proteolytic activation; trypsin inhibitors; <i>Bacillus thuringiensis</i>; SDS-PAGE artefact; protease stabilityTrypsinMolecular biologyLepidoptera030104 developmental biologyBiochemistryproteolytic activationLarvaProteolysisPeptidesAlpha helixmedicine.drugToxins
researchProduct

A Genomic and Proteomic Approach to Identify and Quantify the Expressed

2018

The combined analysis of genomic and proteomic data allowed us to determine which cry and vip genes are present in a Bacillus thuringiensis (Bt) isolate and which ones are being expressed. Nine Bt isolates were selected from Spanish collections of Bt based on their vip1 and vip2 gene content. As a first step, nine isolates were analyzed by PCR to select those Bt isolates that contained genes with the lowest similarity to already described vip1 and vip2 genes (isolates E-SE10.2 and O-V84.2). Two selected isolates were subjected to a combined genomic and proteomic analysis. The results showed that the Bt isolate E-SE10.2 codifies for two new vegetative proteins, Vip2Ac-like_1 and Sip1Aa-like_…

InsecticidesBacterial Proteinsinsect pest controlBacterial ToxinsBacillus thuringiensiscry proteinsGenomicsvip proteinsArticlecrop protectionToxins
researchProduct

Encapsulation of the Bacillus thuringiensis secretable toxins Vip3Aa and Cry1Ia in Pseudomonas fluorescens

2013

Vip3A and Cry1I toxins are secreted during the vegetative growth of Bacillus thuringiensis. Vip3A toxins do not share homology to the crystal (Cry) proteins and are active against a different spectrum of lepidopteran species. Cry1I toxins share similarity with the Cry1 protein group but do not accumulate in the parasporal crystal. Since Vip3A and Cry1I toxins are released from the cell, they are excluded from biological formulates based on spores and crystals of B. thuringiensis. As an approach to obtain novel sprayable insecticides containing Vip3 or Cry1I toxins, Vip3Aa and Cry1Ia proteins were expressed in Pseudomonas fluorescens. This bacterium, non-pathogenic to animals or plants, can …

InsecticidesExpression vectorbiologyBacterial pathogenPseudomonas fluorescensHeterologous expression systemSpodopterabiology.organism_classificationmedicine.disease_causeMicrobial controlMicrobiologyInsect ScienceBacillus thuringiensismedicineBioassayHeterologous expressionAgronomy and Crop ScienceEscherichia coliCry proteinsBacteriaVip proteinsBiological Control
researchProduct