Search results for "Insect Proteins"

showing 10 items of 118 documents

Artefactual band patterns by SDS-PAGE of the Vip3Af protein in the presence of proteases mask the extremely high stability of this protein.

2018

Abstract Vip3 proteins are secretable proteins from Bacillus thuringiensis with important characteristics for the microbiological control of agricultural pests. The exact details of their mode of action are yet to be disclosed and the crystallographic structure is still unknown. Vip3 proteins are expressed as protoxins that have to be activated by the insect gut proteases. A previous study on the peptidase processing of Vip3Aa revealed that the protoxin produced artefactual band patterns by SDS-PAGE due to the differential stability of this protein and the peptidases to SDS and heating (Bel et al., 2017 Toxins 9:131). To determine whether this phenomenon also applies to other Vip3A proteins…

0301 basic medicineProteases030106 microbiologyBacillus thuringiensisSpodopteraSpodopteraCleavage (embryo)Biochemistry03 medical and health sciencesBacterial ProteinsStructural BiologyBacillus thuringiensismedicineAnimalsMode of actionMolecular BiologyPolyacrylamide gel electrophoresisbiologyChemistryProtein StabilityfungiMidgutGeneral Medicinebiology.organism_classificationTrypsin030104 developmental biologyBiochemistryInsect ProteinsElectrophoresis Polyacrylamide Gelmedicine.drugPeptide HydrolasesInternational journal of biological macromolecules
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High Bacterial Agglutination Activity in a Single-CRD C-Type Lectin from Spodoptera exigua (Lepidoptera: Noctuidae)

2017

Lectins are carbohydrate-interacting proteins that play a pivotal role in multiple physiological and developmental aspects of all organisms. They can specifically interact with different bacterial and viral pathogens through carbohydrate-recognition domains (CRD). In addition, lectins are also of biotechnological interest because of their potential use as biosensors for capturing and identifying bacterial species. In this work, three C-type lectins from the Lepidoptera Spodoptera exigua were produced as recombinant proteins and their bacterial agglutination properties were characterized. The lowest protein concentration producing bacterial agglutination against a panel of different Gram+ an…

0301 basic medicineagglutinationlcsh:BiotechnologyClinical BiochemistryMicrobial Sensitivity TestsSpodopteraSpodopteraC-type lectin; agglutination; CRD; bacterial detection; <i>E. coli</i>ArticleMicrobiologylaw.inventionbacterial detectionLepidoptera genitalia03 medical and health sciences0302 clinical medicinelawC-type lectinlcsh:TP248.13-248.65Agglutination TestsExiguaEscherichia coliAnimalsLectins C-TypeAmino Acid SequenceConserved SequencePhylogenybiologyE. coliCRDGeneral Medicinebiology.organism_classificationImmunity InnateC-type lectinAgglutination (biology)030104 developmental biologyRecombinant DNANoctuidaeInsect ProteinsProtein concentration030215 immunologybiotechnology
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Occurrence of a common binding site in Mamestra brassicae, Phthorimaea operculella, and Spodoptera exigua for the insecticidal crystal proteins CryIA…

1997

Specific binding to midgut membrane proteins is required for the toxicity of insecticidal crystal proteins (ICP) from Bacillus thuringiensis. A direct relationship between toxicity and binding has been proposed. It has been hypothesized that sharing of a single receptor by more than one ICP could lead to the occurrence of multiple resistance in the event of an alteration in the common receptor. Binding of CryIA(a), CryIA(b) and CryIA(c), three structurally related ICPs, has been studied in Phthorimaea operculella, Mamestra brassicae and, Spodoptera exigua using brush border membrane vesicles (BBMV) from the midgut tissue. Using iodinated CryIA(b), the three insects showed similar results: o…

Bacterial ToxinsBacillus thuringiensisReceptors Cell SurfaceSpodopteraMothsSpodopteraBiochemistryHemolysin ProteinsBacterial ProteinsBacillus thuringiensisExiguaBotanyAnimalsBinding siteReceptorMolecular BiologyBinding SitesbiologyBacillus thuringiensis ToxinsfungiMidgutbiology.organism_classificationMolecular biologyPhthorimaea operculellaEndotoxinsMembrane proteinInsect ScienceInsect ProteinsInsect biochemistry and molecular biology
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Common receptor for Bacillus thuringiensis toxins Cry1Ac, Cry1Fa, and Cry1Ja in Helicoverpa armigera, Helicoverpa zea and Spodoptera exigua

2005

ABSTRACT Binding studies using 125 I-Cry1Ac and biotinylated Cry1Fa toxins indicate the occurrence of a common receptor for Cry1Ac, Cry1Fa, and Cry1Ja in Helicoverpa armigera , Helicoverpa zea , and Spodoptera exigua . Our results, along with previous binding data and the observed cases of cross-resistance, suggest that this pattern seems to be widespread among lepidopteran species.

Bacterial ToxinsBiotecnologia agrícolaBacillus thuringiensisMicrobiologiaReceptors Cell SurfaceSpodopteraHelicoverpa armigeraSpodopteraBinding CompetitiveApplied Microbiology and BiotechnologyMicrobiologyLepidoptera genitaliaHemolysin ProteinsBacterial ProteinsBacillus thuringiensisExiguaBotanyInvertebrate MicrobiologyAnimalsBinding SitesBacillus thuringiensis ToxinsEcologybiologyfungibiology.organism_classificationEndotoxinsLepidopteraCry1AcInsect ProteinsNoctuidaeHelicoverpa zeaFood 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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Sequence and evolution of a hexamerin from the ant Camponotus festinatus.

2000

In the ant Camponotus festinatus, two different hexamerins accumulate stage-specifically during the late larval period and at various times in adults. These hexamerins serve as storage proteins and play important roles in brood nourishment and colony founding. We report an analysis of the cDNA sequence of C. festinatus hexamerin 2 (CfeHex2). The native protein contains 732 amino acids, which are moderately enriched in aromatic amino acids, aspartate and asparagine. Phylogenetic analyses show a close relationship of CfeHex2 to a putative toxin of the braconid wasp, Bracon hebetor. The divergence of Formicidae and Braconidae hexamerins was calculated to have begun 187 MYA, an estimate consist…

Camponotus festinatusDNA ComplementarySequence analysisBracon hebetormedia_common.quotation_subjectMolecular Sequence DataZoologyInsectEvolution MolecularPhylogeneticsGeneticsAnimalsAmino Acid SequenceMolecular BiologyPeptide sequencePhylogenymedia_commonbiologyBase SequenceSequence Homology Amino AcidEcologyAntsfungibiology.organism_classificationBroodInsect ScienceInsect ProteinsBraconidaeSequence AnalysisInsect molecular biology
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Resistance to diverse apoptotic triggers in multidrug resistant HL60 cells and its possible relationship to the expression of P-glycoprotein, Fas and…

2002

We studied the human HL60 leukemia cell line and its multidrug resistant (MDR) variant HL60R. In contrast to the HL60, HL60R showed an inability to undergo apoptosis from doxorubicin (Dox) or other different stimuli, including cisplatin, Fas ligation and serum withdrawal. HL60R cells lost surface Fas expression, but we found no evidence that Fas/FasL mediates the apoptotic effects of Dox in HL60. P-glycoprotein (P-gp) did not seem to play a major role as a specific inhibitor of apoptosis. In fact, the P-gp inhibitor verapamil reversed only partially the resistance to Dox-induced apoptosis of the MDR cells. In addition, it did not modify the rate of apoptosis induced from the other stimuli i…

Cancer ResearchProgrammed cell deathTime FactorsChromosomal Proteins Non-HistoneSurvivinDown-RegulationAntineoplastic AgentsApoptosisHL-60 CellsNerve Tissue ProteinsBiologyInhibitor of apoptosisFas ligandInhibitor of Apoptosis ProteinsInhibitory Concentration 50SurvivinTumor Cells CulturedHumansATP Binding Cassette Transporter Subfamily B Member 1RNA Messengerfas ReceptorP-glycoproteinInhibitor of apoptosis domainCaspase 3Reverse Transcriptase Polymerase Chain ReactionProteinsFlow CytometryNeuronal Apoptosis-Inhibitory ProteinNeoplasm ProteinsCell biologyProto-Oncogene Proteins c-bcl-2OncologyDoxorubicinDrug Resistance NeoplasmApoptosisCaspasesbiology.proteinInsect ProteinsNAIPCisplatinMicrotubule-Associated ProteinsCancer Letters
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A pheromone-binding protein from the cockroach Leucophaea maderae: cloning, expression and pheromone binding

2003

0264-6021 (Print) Journal Article; Odorant-binding proteins (OBPs) are thought to transport volatile compounds from air to their receptors through the sensillary lymph. In this protein family, the subgroup of pheromone-binding proteins (PBPs) is specifically tuned to the perception of the sexual pheromone. To date, the description of OBPs has been restricted to Endopterygota and Paraneoptera. Their expression in Orthopteroid has been hypothesized, but no evidence of OBP has been produced in this assemblage to date. In the present study, we describe the first OBP from a Dictyopteran insect that belongs to the cockroach Leucophaea maderae. The PBP of L. maderae (PBPLma) shares all the hallmar…

Carrier Proteins/*genetics/*metabolismProtein familymedia_common.quotation_subjectMolecular Sequence DataCockroachesEndopterygotaInsectBiochemistryPolymerase Chain ReactionPheromonesbiology.animalPheromones/*metabolismAnimalsPheromone bindingAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequenceIn Situ Hybridizationmedia_commonCockroachbiologyBase SequenceMolecularCell Biologybiology.organism_classificationRecombinant ProteinsBiochemistryCockroaches/*physiologyInsect ProteinsPheromoneCarrier ProteinsPheromone binding proteinInsect Proteins/genetics/metabolismRecombinant Proteins/chemistry/metabolismResearch ArticleCloning
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Identification and characterisation of the dopamine receptor II from the cat flea Ctenocephalides felis (CfDopRII)

2006

International audience; G protein-coupled receptors (GPCRs) represent a protein family with a wide range of functions. Approximately 30% of human drug targets are GPCRs, illustrating their pharmaceutical relevance. In contrast, the knowledge about invertebrate GPCRs is limited and is mainly restricted to model organisms like Drosophila melanogaster and Caenorhabditis elegans. Especially in ectoparasites like ticks and fleas, only few GPCRs are characterised. From the cat flea Ctenocephalides felis, a relevant parasite of cats and dogs, no GPCRs are known so far. Thus, we performed a bioinformatic analysis of available insect GPCR sequences from the honeybee Apis mellifera, the mosquito Anop…

Cat fleaAnopheles gambiaeMolecular Sequence Dataved/biology.organism_classification_rank.speciesBiochemistryCell LineReceptors DopamineAnimals Genetically ModifiedXenopus laevisAnimalsHumansAmino Acid SequenceCloning MolecularModel organismMolecular BiologyPhylogenyCaenorhabditis elegansCtenocephalides[INFO.INFO-BI] Computer Science [cs]/Bioinformatics [q-bio.QM]G protein-coupled receptorGeneticsbiologyved/biologyEcologyFelisComputational Biologybiology.organism_classificationDrosophila melanogasterMultigene FamilyInsect ScienceOocytesInsect ProteinsSiphonapteraFemaleRNA Interference[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]Drosophila melanogasterSequence Alignment[CHIM.CHEM]Chemical Sciences/Cheminformaticshormones hormone substitutes and hormone antagonistsInsect Biochemistry and Molecular Biology
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Growth of human cells on a non-woven silk fibroin net: a potential for use in tissue engineering.

2003

We have examined a novel biomaterial consisting of a non-woven fibroin net produced from silk (Bombyx mori) cocoons for its ability to support the growth of human cells. Various human cells of different tissue and cell types (endothelial, epithelial, fibroblast, glial, keratinocyte, osteoblast) were examined for adherence and growth on the nets by confocal laser microscopy after staining of the cells with calcein-AM and by electron microscopy. All the cells readily adhered and spread over the individual fibers of the nets. Most of the cells were able to grow and survive on the nets for at least 7 weeks and growth not only covered the individual fibers of the net but generally bridged the ga…

Cell typeMaterials scienceManufactured MaterialsAdolescentBiophysicsSilkFibroinBioengineeringNanotechnologyBiocompatible MaterialsBiomaterialsTissue engineeringBombyx moriBiomimetic MaterialsCell MovementCulture TechniquesMaterials TestingmedicineCell AdhesionAnimalsHumansFibroblastCells CulturedbiologyTissue EngineeringTextilesfungiBiomaterialOsteoblastMembranes Artificialbiology.organism_classificationBombyxExtracellular Matrixmedicine.anatomical_structureSILKMechanics of MaterialsCeramics and CompositesBiophysicsInsect ProteinsAdsorptionFibroinsCell DivisionBiomaterials
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