Search results for "Midgut"

showing 10 items of 81 documents

Unusual basement layer in the midgut of gammaridean Niphargus virei Chevreux (Crustacea, Amphipoda).

1988

The basement membrane of the midgut and posterior caeca epithelium in the gammaridean amphipod Niphargus virei Chevreux, 1896 is made of an unusual structure. This basal lamina, properly called “basal layer”, shows a dense sheet formed by a system of dense hexagonal plates connected by thin filaments. Histochemical studies and enzymatic reactions lead to the conclusion that these structures are proteinaceous, without collagenous protein, and embedded in a neutral polysaccharide matrix. The possible mechanical significance of these mesenteric structures is discussed.

HistologyAmphipodaMatrix (biology)Basement MembraneCrustaceamedicineAnimalsMolecular BiologyBasement membranebiologyStaining and LabelingHistocytochemistryProteinsMidgutCell BiologyGeneral MedicineAnatomybiology.organism_classificationCrustaceanEpitheliumMedical Laboratory TechnologyMicroscopy Electronmedicine.anatomical_structureBasal laminaCollagenAnatomyGeneral Agricultural and Biological SciencesLayer (electronics)Digestive SystemHistochemistry
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Lack of Detrimental Effects of Bacillus thuringiensis Cry Toxins on the Insect Predator Chrysoperla carnea : a Toxicological, Histopathological, and …

2006

ABSTRACT The effect of Cry proteins of Bacillus thuringiensis on the green lacewing ( Chrysoperla carnea ) was studied by using a holistic approach which consisted of independent, complementary experimental strategies. Tritrophic experiments were performed, in which lacewing larvae were fed Helicoverpa armigera larvae reared on Cry1Ac, Cry1Ab, or Cry2Ab toxins. In complementary experiments, a predetermined amount of purified Cry1Ac was directly fed to lacewing larvae. In both experiments no effects on prey utilization or fitness parameters were found. Since binding to the midgut is an indispensable step for toxicity of Cry proteins to known target insects, we hypothesized that specific bind…

InsectanoctuidaeBacterial ToxinsBacillus thuringiensisHelicoverpa armigeraApplied Microbiology and BiotechnologyHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanyExiguaInvertebrate MicrobiologyAnimalsBioassaycrystal proteinsPest Control BiologicalChrysoperla carnealarval midgutBacillus thuringiensis ToxinsMicrovilliEcologybiologybinding-sitesfungitoxicityMidgutbiology.organism_classificationspodoptera-exiguaEndotoxinsPRI BioscienceBiochemistryCry1Acmaize expressing cry1abNoctuidaeDigestive Systemborder membrane-vesicleshelicoverpa-armigera lepidopteraFood ScienceBiotechnologyresistant transgenic plants
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Screening for Bacillus thuringiensis Crystal Proteins Active against the Cabbage Looper, Trichoplusia ni

2000

Abstract Toxicity tests were performed to find among Cry1 and Cry2 Bacillus thuringiensis crystal proteins those with high activity against the cabbage looper. Tests were performed with neonate larvae on surface-contaminated artificial diet. The crystal proteins found to be toxic were, from higher to lower toxicity: Cry1Ac, Cry1Ab, Cry1C, Cry2Aa, Cry1J, and Cry1F (LC50 of 1.1–4.1, 3.4–4.4, 12, 34, 87, and 250 ng/cm2, respectively). Cry1B, Cry1D, and Cry1E can be considered nontoxic (LC50 higher than 2500 ng/cm2). Cry1Aa was moderately toxic to nontoxic, depending on the source (LC50 of 420 ng/cm2 from PGS and 8100 ng/cm2 from Ecogen). In vitro binding assays with trypsin-activated 125I-labe…

InsecticidesBacillus thuringiensis ToxinsBrush borderBacterial ToxinsfungiBacillus thuringiensisMidgutMothsBiologybiology.organism_classificationBacillalesEndotoxinsIodine RadioisotopesHemolysin ProteinsBacterial ProteinsCry1AcBiochemistryCabbage looperBacillus thuringiensisBotanyToxicityTrichoplusiaAnimalsPest Control BiologicalEcology Evolution Behavior and SystematicsJournal of Invertebrate Pathology
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Mechanism of Resistance to Bacillus thuringiensis Toxin Cry1Ac in a Greenhouse Population of the Cabbage Looper, Trichoplusia ni

2007

ABSTRACT The cabbage looper, Trichoplusia ni , is one of only two insect species that have evolved resistance to Bacillus thuringiensis in agricultural situations. The trait of resistance to B. thuringiensis toxin Cry1Ac from a greenhouse-evolved resistant population of T. ni was introgressed into a highly inbred susceptible laboratory strain. The resulting introgression strain, GLEN-Cry1Ac-BCS, and its nearly isogenic susceptible strain were subjected to comparative genetic and biochemical studies to determine the mechanism of resistance. Results showed that midgut proteases, hemolymph melanization activity, and midgut esterase were not altered in the GLEN-Cry1Ac-BCS strain. The pattern of…

InsecticidesBacterial ToxinsPopulationBacillus thuringiensisDrug ResistanceBrassicaInsect ControlApplied Microbiology and BiotechnologyMicrobiologyHemolysin ProteinsBacterial ProteinsCabbage looperBacillus thuringiensisHemolymphBotanyInvertebrate MicrobiologyTrichoplusiaAnimalseducationeducation.field_of_studyBacillus thuringiensis ToxinsEcologybiologyStrain (chemistry)fungifood and beveragesMidgutbiology.organism_classificationEndotoxinsLepidopteraCry1AcFood ScienceBiotechnologyApplied and Environmental Microbiology
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Overproduction of the Bacillus thuringiensis Vip3Aa16 toxin and study of its insecticidal activity against the carob moth Ectomyelois ceratoniae

2015

Abstract The vip3Aa16 gene of Bacillus thuringiensis strain BUPM95 was cloned and expressed in Escherichia coli . Optimization of Vip3A16 protein expression was conducted using Plackett–Burman design and response surface methodology. Accordingly, the optimum Vip3A16 toxin production was 170 μg/ml at 18 h post-induction time and 39 °C post-induction temperature. This corresponds to an improvement of 21 times compared to the starting conditions. The insecticidal activity, evaluated against Ectomyelois ceratoniae , displayed an LC 50 value of 40 ng/cm 2 and the midgut histopathology of Vip3Aa16 fed larvae showed vacuolization of the cytoplasm, brush border membrane destruction, vesicle formati…

InsecticidesEctomyelois ceratoniaebiologyBrush borderToxinBacillus thuringiensisMidgutMothsbiology.organism_classificationmedicine.disease_causeMicrobiologyBacterial ProteinsVacuolizationBacillus thuringiensismedicineAnimalsOverproductionEscherichia coliEcology Evolution Behavior and SystematicsJournal of Invertebrate Pathology
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The Rapid Evolution of Resistance to Vip3Aa Insecticidal Protein in Mythimna separata (Walker) Is Not Related to Altered Binding to Midgut Receptors

2021

Laboratory selection for resistance of field populations is a well-known and useful tool to understand the potential of insect populations to evolve resistance to insecticides. It provides us with estimates of the frequency of resistance alleles and allows us to study the mechanisms by which insects developed resistance to shed light on the mode of action and optimize resistance management strategies. Here, a field population of Mythimna separata was subjected to laboratory selection with either Vip3Aa, Cry1Ab, or Cry1F insecticidal proteins from Bacillus thuringiensis. The population rapidly evolved resistance to Vip3Aa reaching, after eight generations, a level of >3061-fold resistance…

InsecticidesHealth Toxicology and Mutagenesismedia_common.quotation_subjectPopulationBacillus thuringiensisInsectMothsToxicologyInsecticide Resistance03 medical and health sciencesMythimna separataHemolysin ProteinsBacterial ProteinsBacillus thuringiensis<i>Bacillus thuringiensis</i>cross resistanceBt toxinsAnimalseducationCross-resistance030304 developmental biologymedia_commonGenetics0303 health sciencesLarvaeducation.field_of_studybiologyResistance (ecology)Bacillus thuringiensis Toxins030306 microbiologyCommunicationfungiRMidgutbiology.organism_classificationEndotoxinsLarvaoriental armywormMedicineProtein BindingToxins
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Susceptibility of Spodoptera frugiperda and S. exigua to Bacillus thuringiensis Vip3Aa insecticidal protein

2011

The Vip3Aa protein is an insecticidal protein secreted by Bacillus thuringiensis during the vegetative stage of growth. The activity of this protein has been tested after different steps/protocols of purification using Spodoptera frugiperda as a control insect. The results showed that the Vip3Aa protoxin was stable and retained full toxicity after being subjected to common biochemical steps used in protein purification. Bioassays with the protoxin in S. frugiperda and S. exigua showed pronounced differences in LC(50) values when mortality was measured at 7 vs. 10d. At 7d most live larvae were arrested in their development. LC(50) values of "functional mortality" (dead larvae plus larvae rem…

InsecticidesLongevityBacillus thuringiensisInsect pest controlInsect proteaseBacterial ProteinSpodopteraSpodopteraMedian lethal doseMicrobiologyLethal Dose 50Vegetative insecticidal proteinBacterial ProteinsSpecies SpecificityBacillus thuringiensisparasitic diseasesExiguaProtein purificationBotanyAnimalsBacillus thuringiensiBioassayPest Control BiologicalInsecticideEcology Evolution Behavior and SystematicsbiologyAnimalfungiMidgutbiology.organism_classificationBioinsecticideHost-Pathogen InteractionMode of actionLarvaHost-Pathogen InteractionsInstarBiological AssayElectrophoresis Polyacrylamide GelDisease SusceptibilityJournal of Invertebrate Pathology
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Proteolytic processing of Bacillus thuringiensis Vip3A proteins by two Spodoptera species

2014

Abstract Vip3 proteins have been described to be secreted by Bacillus thuringiensis during the vegetative growth phase and to display a broad insecticidal spectrum against lepidopteran larvae. Vip3Aa protoxin has been reported to be significantly more toxic to Spodoptera frugiperda than to Spodoptera exigua and differences in the midgut processing have been proposed to be responsible. In contrast, we have found that Vip3Ae is essentially equally toxic against these two species. Proteolysis experiments were performed to study the stability of Vip3A proteins to peptidase digestion and to see whether the differences found could explain differences in toxicity against these two Spodoptera speci…

InsecticidesPhysiologyProteolysisBacterial ProteinSpodopteraSpodopteraMicrobiologyVegetative insecticidal proteinBacterial ProteinsSpecies SpecificitySpodoptera exiguaBacillus thuringiensisExiguamedicineAnimalsPest Control BiologicalMidgut peptidaseInsecticideChymotrypsinbiologymedicine.diagnostic_testAnimalMedicine (all)Serine EndopeptidasesfungiSpodoptera frugiperdaMidgutbiology.organism_classificationTrypsinSerine EndopeptidaseSerine peptidaseBiochemistryMode of actionLarvaInsect Sciencebiology.proteinDigestionDigestive Systemmedicine.drugJournal of Insect Physiology
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Combining Hexanoic Acid Plant Priming with Bacillus thuringiensis Insecticidal Activity against Colorado Potato Beetle

2013

Interaction between insect herbivores and host plants can be modulated by endogenous and exogenous compounds present in the source of food and might be successfully exploited in Colorado potato beetle (CPB) pest management. Feeding tests with CPB larvae reared on three solanaceous plants (potato, eggplant and tomato) resulted in variable larval growth rates and differential susceptibility to Bacillus thuringiensis Cry3Aa toxin as a function of the host plant. An inverse correlation with toxicity was observed in Cry3Aa proteolytic patterns generated by CPB midgut brush-border membrane vesicles (BBMV) from Solanaceae-fed larvae, being the toxin most extensively proteolyzed on potato, followed…

Insecticidesmedicine.disease_causeMass Spectrometrylcsh:Chemistrychemistry.chemical_compoundHemolysin ProteinsPlant Growth RegulatorsCysteine ProteasesBacillus thuringiensisPlant defense against herbivoryColorado potato beetleElectrophoresis Gel Two-Dimensionallcsh:QH301-705.5SpectroscopySolanaceaeHexanoic acidbiologyfood and beveragesGeneral MedicineComputer Science ApplicationsColeopterasurgical procedures operativeBiochemistryLarvaHost-Pathogen Interactionsplant hormonesInsect ProteinsSolanaceaeproteolysisColoradoMolecular Sequence DataBacillus thuringiensisCatalysisArticleMicrobiologyCry3Aa toxinInorganic Chemistryintestain proteasesBacterial Proteinsplant defensemedicineAnimalsAmino Acid SequencePhysical and Theoretical ChemistryprimingMolecular BiologyCaproatesSolanum tuberosumBacillus thuringiensis ToxinsToxinOrganic ChemistryColorado potato beetlefungiBody WeightMidgutColorado potato beetle;<i> Bacillus thuringiensis</i>; Cry3Aa toxin; intestain proteases; proteolysis; Solanaceae; hexanoic acid; priming; plant defense; plant hormonesFeeding Behaviorbiology.organism_classificationDietEndotoxinsPapainchemistrylcsh:Biology (General)lcsh:QD1-999hexanoic acidPeptidesDigestive SystemSequence AlignmentInternational Journal of Molecular Sciences
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Acute appendicitis in a patient with situs viscerum inversus totalis: Role of laparoscopic approach. A case report and brief literature review

2020

Highlights • Abdominal pain due to acute appendicitis in one of the most causes of access to Emergency Room requiring surgical consult and treatment. • The occurrence of anatomical anomalies should be considered especially when clinical and imaging features are misleading. In these cases laparoscopic surgery can be a safe tool in order to confirm uncertain diagnosis. • We report a case of acute appendicitis in a 23-year-old Caucasian men with situs viscerum inversus detected on radiological investigation. • Laparoscopic approach was used to confirm the diagnosis and to perform appendectomy. Trocars placement was tailored for this peculiar case. • Situs viscerum inversus and midgut malrotati…

Laparoscopic surgerycongenital hereditary and neonatal diseases and abnormalitiesmedicine.medical_specialtyAbdominal painMidgut malrotationmedicine.medical_treatmentCase ReportLaparoscopic surgery03 medical and health sciencesStandard anatomical position0302 clinical medicineotorhinolaryngologic diseasesmedicineUrgent laparoscopyAcute appendicitisSitus viscerum inversusbusiness.industryGeneral surgeryAppendixmedicine.anatomical_structure030220 oncology & carcinogenesisAcute appendicitis030211 gastroenterology & hepatologySurgeryDifferential diagnosismedicine.symptomMidgut malrotationSitus viscerum inversusbusiness
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