Search results for "Microvilli"

showing 10 items of 37 documents

Specific binding of Bacillus thuringiensis Cry1Ea toxin, and Cry1Ac and Cry1Fa competition analyses in Anticarsia gemmatalis and Chrysodeixis include…

2019

AbstractAnticarsia gemmatalis (velvetbean caterpillar) and Chrysodeixis includens (soybean looper) are two important defoliation pests of soybeans. In the present study, we have investigated the susceptibility and brush border membrane-binding properties of both species to Bacillus thuringiensis Cry1Ea toxin. Bioassays performed in first-instar larvae demonstrated potent activity against both soybean pests in terms of mortality or practical mortality. Competition-binding studies carried out with 125Iodine-labelled Cry1Ea, demonstrated the presence of specific binding sites on the midgut brush border membrane vesicles (BBMV) of both insect species. Heterologous competition-binding experiment…

0106 biological sciences0301 basic medicineBrush borderlcsh:MedicineMoths01 natural sciencesArticleMicrobiologyApplied microbiology03 medical and health sciencesHemolysin ProteinsBacterial ProteinsChrysodeixis includensBacillus thuringiensisEnvironmental biotechnologyAnimalsCaterpillarlcsh:ScienceMultidisciplinaryBinding SitesbiologyBacillus thuringiensis ToxinsMicrovillifungilcsh:Rfood and beveragesMidgutbiology.organism_classificationEndotoxins010602 entomologyAnticarsia gemmatalis030104 developmental biologyCry1AcBiological Control AgentsLarvaBiological Assaylcsh:QPEST analysisSoybeansScientific Reports
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Enterocyte Purge and Rapid Recovery Is a Resilience Reaction of the Gut Epithelium to Pore-Forming Toxin Attack.

2016

International audience; Besides digesting nutrients, the gut protects the host against invasion by pathogens. Enterocytes may be subjected to damage by both microbial and host defensive responses, causing their death. Here, we report a rapid epithelial response that alleviates infection stress and protects the enterocytes from the action of microbial virulence factors. Intestinal epithelia exposed to hemolysin, a pore-forming toxin secreted by Serratia marcescens, undergo an evolutionarily conserved process of thinning followed by the recovery of their initial thickness within a few hours. In response to hemolysin attack, Drosophila melanogaster enterocytes extrude most of their apical cyto…

0301 basic medicineCytoplasmDisease toleranceSurvivalApoptosismedicine.disease_causeOral infectionHemolysin ProteinsLipid droplet[SDV.IDA]Life Sciences [q-bio]/Food engineeringMitochondrial extrusionIntestinal MucosaSerratia marcescensBacterial-infectionPore-forming toxinbiologyCell DeathMicrovilliPlasma-membrane[ SDV.IDA ] Life Sciences [q-bio]/Food engineeringGut EpitheliumMitochondriamedicine.anatomical_structureDrosophila melanogasterEnterocyteVirulence FactorsVarroidaeSerratia-marcescensBacterial ToxinsVirulenceMicrobiologyMicrobiologySerratia Infections03 medical and health sciencesVirologymedicineAnimalsApical cytoplasmDefense strategyDrosophila cyclin jToxinbiology.organism_classificationLipid dropletsDisease Models AnimalIntestinal Diseases030104 developmental biologyEnterocytesSerratia marcescensParasitologyDigestive SystemCell hostmicrobe
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Mesopolysaccharides: The extracellular surface layer of visceral organs

2020

The mesothelium is a dynamic and specialized tissue layer that covers the somatic cavities (pleural, peritoneal, and pericardial) as well as the surface of the visceral organs such as the lung, heart, liver, bowel and tunica vaginalis testis. The potential therapeutic manipulation of visceral organs has been complicated by the carbohydrate surface layer—here, called the mesopolysaccharide (MPS)—that coats the outer layer of the mesothelium. The traditional understanding of MPS structure has relied upon fixation techniques known to degrade carbohydrates. The recent development of carbohydrate-preserving fixation for high resolution imaging techniques has provided an opportunity to re-examine…

0301 basic medicinePathologyRespiratory Systemlcsh:MedicineBiochemistryEpitheliumMice0302 clinical medicineLectinsMedicine and Health SciencesElectron Microscopylcsh:ScienceLungFixation (histology)MicroscopyMultidisciplinaryMembrane GlycoproteinsMicrovilliOrganic CompoundsChemistryQRThoraxExtracellular MatrixChemistrymedicine.anatomical_structureLiverTransmission electron microscopy030220 oncology & carcinogenesisPhysical SciencesPleuraeMedicineCellular Structures and OrganellesAnatomyResearch ArticleChemical Elementsmedicine.medical_specialtyScienceCarbohydratesResearch and Analysis MethodsRuthenium03 medical and health sciencesMicroscopy Electron TransmissionPolysaccharidesmedicineExtracellularAnimalsSurface layerProcess (anatomy)LungMyocardiumOrganic Chemistrylcsh:RChemical CompoundsBiology and Life SciencesProteinsCell BiologyMesothelium030104 developmental biologyMurine lungTransmission Electron Microscopylcsh:QLungsPLoS ONE
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Shared midgut binding sites for Cry1A.105, Cry1Aa, Cry1Ab, Cry1Ac and Cry1Fa proteins from Bacillus thuringiensis in two important corn pests, Ostrin…

2013

First generation of insect-protected transgenic corn (Bt-corn) was based on the expression of Cry1Ab or Cry1Fa proteins. Currently, the trend is the combination of two or more genes expressing proteins that bind to different targets. In addition to broadening the spectrum of action, this strategy helps to delay the evolution of resistance in exposed insect populations. One of such examples is the combination of Cry1A.105 with Cry1Fa and Cry2Ab to control O. nubilalis and S. frugiperda. Cry1A.105 is a chimeric protein with domains I and II and the C-terminal half of the protein from Cry1Ac, and domain III almost identical to Cry1Fa. The aim of the present study was to determine whether the c…

Agricultural BiotechnologyApplied MicrobiologyCoated vesiclePlant SciencePlasma protein bindingMothsBiochemistryOstriniaPlagues ControlBacillus thuringiensisBiomacromolecule-Ligand InteractionsPlant PestsMultidisciplinaryMicrovillibiologyGenetically Modified OrganismsQRAgricultureRecombinant ProteinsBiochemistryLarvaMedicineDisease SusceptibilityAgrochemicalsResearch ArticleBiotechnologyProtein BindingScienceProtein domainBiotecnologia agrícolaBacillus thuringiensisCoated VesiclesCerealsCropsSpodopteraSpodopteraMicrobiologyBinding CompetitiveZea maysBacterial ProteinsBotanyAnimalsPesticidesBinding siteProtein InteractionsBiologyTransgenic PlantsfungiProteinsPlant Pathologybiology.organism_classificationFusion proteinMaizeGastrointestinal TractKineticsPlant BiotechnologyPest ControlProteïnes
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Genetic variability of Spodoptera frugiperda Smith (Lepidoptera: Noctuidae) populations from Latin America is associated with variations in susceptib…

2006

ABSTRACT Bacillus thuringiensis strains isolated from Latin American soil samples that showed toxicity against three Spodoptera frugiperda populations from different geographical areas (Mexico, Colombia, and Brazil) were characterized on the basis of their insecticidal activity, crystal morphology, sodium dodecyl sulfate-polyacrylamide gel electrophoresis of parasporal crystals, plasmid profiles, and cry gene content. We found that the different S. frugiperda populations display different susceptibilities to the selected B. thuringiensis strains and also to pure preparations of Cry1B, Cry1C, and Cry1D toxins. Binding assays performed with pure toxin demonstrated that the differences in the …

Bacterial ToxinsBacillus thuringiensisSpodopteraSpodopteraApplied Microbiology and BiotechnologyPolymerase Chain ReactionLepidoptera genitaliaHemolysin ProteinsBacterial ProteinsBacillus thuringiensisGenetic variationparasitic diseasesInvertebrate MicrobiologyAnimalsGenetic variabilityPest Control BiologicalSoil MicrobiologyGeneticsGenetic diversityGenetically modified maizeEcologybiologyBacillus thuringiensis ToxinsMicrovillibusiness.industryfungiGenetic Variationbiology.organism_classificationBiotechnologyRandom Amplified Polymorphic DNA TechniqueEndotoxinsLatin AmericaNoctuidaebusinessFood ScienceBiotechnologyApplied and environmental microbiology
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Resistance to the Bacillus thuringiensis bioinsecticide in a field population of Plutella xylostella is due to a change in a midgut membrane receptor.

1991

The biochemical mechanism for resistance to Bacillus thuringiensis crystal proteins was studied in a field population of diamondback moths (Plutella xylostella) with a reduced susceptibility to the bioinsecticidal spray. The toxicity and binding characteristics of three crystal proteins [CryIA(b), CryIB, and CryIC] were compared between the field population and a laboratory strain. The field population proved resistant (greater than 200-fold compared with the laboratory strain) to CryIA(b), one of the crystal proteins in the insecticidal formulation. Binding studies showed that the two strains differ in a membrane receptor that recognizes CryIA(b). This crystal protein did not bind to the b…

Bacterial ToxinsBacillus thuringiensismedicine.disease_causeBinding CompetitiveMicrobiologyInsecticide ResistanceHemolysin ProteinsBacterial ProteinsBacillus thuringiensismedicineEscherichia coliAnimalsPest Control BiologicalEscherichia coliMultidisciplinaryBacillaceaebiologyStrain (chemistry)Bacillus thuringiensis ToxinsMicrovilliParasporal bodyPlutellaMidgutGene Expression Regulation Bacterialbiology.organism_classificationBacillalesMolecular biologyEndotoxinsLepidopteraGenes BacterialResearch Article
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Lack of Cry1Fa binding to the midgut brush border membrane in a resistant colony of Plutella xylostella moths with a mutaton in the ABCC2 locus

2012

ABSTRACT Previous studies reported “mode 1” Bacillus thuringiensis resistance in a colony of diamondback moths (NO-QA), and recently, this resistance has been mapped to an ABC transporter ( ABCC2 ) locus. We report the lack of binding of Cry1Fa to insects derived from this colony and compare our data with those from other insects with ABCC2 -associated resistance.

BioquímicaBrush borderBiotecnologia agrícolaDrug ResistanceResistència als plaguicidesLocus (genetics)ATP-binding cassette transporterDrug resistanceApplied Microbiology and BiotechnologyLepidoptera genitaliaHemolysin ProteinsPlagues ControlBacterial ProteinsBacillus thuringiensisInvertebrate MicrobiologyAnimalsGeneticsBacillus thuringiensis ToxinsMicrovilliEcologybiologyfungiPlutellaMidgutbiology.organism_classificationMultidrug Resistance-Associated Protein 2EndotoxinsLepidopteraMutationMultidrug Resistance-Associated ProteinsProtein BindingFood ScienceBiotechnology
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Specific binding of radiolabeled Cry1Fa insecticidal protein from Bacillus thuringiensis to midgut sites in lepidopteran species

2012

ABSTRACT Cry1Fa insecticidal protein was successfully radiolabeled with 125 I-Na. Specific binding to brush border membrane vesicles was shown for the lepidopteran species Ostrinia nubilalis , Spodoptera frugiperda , Spodoptera exigua , Helicoverpa armigera , Heliothis virescens , and Plutella xylostella . Homologous competition assays were performed to obtain equilibrium binding parameters ( K d [dissociation constant] and R t [concentration of binding sites]) for these six insect species.

BioquímicavirusesBiotecnologia agrícolaBacillus thuringiensisHelicoverpa armigeraSpodopteraSpodopteraApplied Microbiology and BiotechnologyOstriniaIodine RadioisotopesHemolysin ProteinsPlagues ControlBacterial ProteinsSpecies SpecificityBacillus thuringiensisExiguaBotanyparasitic diseasesPlaguicidesInvertebrate MicrobiologyAnimalsBinding siteTransport VesiclesBinding SitesEcologybiologyHeliothis virescensBacillus thuringiensis ToxinsMicrovillifungiPlutellabiology.organism_classificationEndotoxinsLepidopteraBiochemistryDigestive SystemProteïnesFood ScienceBiotechnology
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Lyophilization of lepidopteran midguts: a preserving method for Bacillus thuringiensis toxin binding studies

2004

Binding assays with brush border membrane vesicles (BBMV) from insect midguts are commonly used in the study of the interactions between Bacillus thuringiensis Cry toxins and their receptors. Collaboration between laboratories often require that frozen insect samples are sent in dry ice. Because of customs restrictions and delays, sample thawing is always a risk and often the biological material becomes ruined during shipping. We have tested lyophilization as an alternative method for preserving insect midguts for binding studies with B. thuringiensis Cry toxins. For this purpose, BBMV were prepared from both frozen and lyophilized midguts from three lepidopteran species: Spodoptera exigua,…

Brush borderBacillus thuringiensisReceptors Cell SurfaceHelicoverpa armigeraSpodopteramedicine.disease_causeHost-Parasite InteractionsMicrobiologyBacterial ProteinsBacillus thuringiensisExiguamedicineAnimalsBinding sitePest Control BiologicalEcology Evolution Behavior and SystematicsCryopreservationMicrovillibiologyToxinfungibiology.organism_classificationLepidopteraFreeze DryingBiochemistryManduca sextaInsect ProteinsDigestive SystemJournal of Invertebrate Pathology
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Immunohistochemical Detection of Binding of Cryia Crystal Proteins of Bacillus thuringiensis in Highly Resistant Strains of Plutella xylostella (L.) …

1995

We detected binding of insecticidal crystal proteins from Bacillus thuringiensis in one susceptible strain and six resistant strains of diamondback moth, Plutella xylostella, from Hawaii. Immunohistochemical tests with tissue sections from larval midguts showed specific binding of CryIA(a), CryIA(b), and CryIA(c) to brush border membranes. CryIE, which is not toxic to P. xylostella, did not bind to midgut tissues. Larvae from one of the resistant strains ingested extremely high concentrations of a commercial formulation containing the three CryIA proteins without suffering midgut cell damage or mortality. This same resistant strain had previously been found to have greatly reduced binding o…

Brush borderBacterial ToxinsBacillus thuringiensisBiophysicsMothsHemolysin ProteinsBiochemistryEpitheliumHawaiiInsecticide ResistanceHemolysin ProteinsBacterial ProteinsIn vivoBacillus thuringiensisBotanyAnimalsPest Control BiologicalMolecular BiologyDiamondback mothBacillus thuringiensis ToxinsMicrovillibiologyStrain (chemistry)fungiPlutellaMidgutCell Biologybiology.organism_classificationImmunohistochemistryMolecular biologyEndotoxinsLarvaBiochemical and Biophysical Research Communications
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