Search results for "Sf9"

showing 10 items of 11 documents

Hetero-oligomerization of Bacillus thuringiensis Cry1A proteins enhance binding to the ABCC2 transporter of Spodoptera exigua

2021

The ATP binding cassette (ABC) transporters are membrane proteins that can act as putative receptors for Cry proteins from Bacillus thuringiensis (Bt) in the midgut of different insects. For the beet armyworm, Spodoptera exigua, ABCC2 and ABCC3 have been found to interact with Cry1A proteins, the main insecticidal proteins used in Bt crops, as well as Bt-based pesticides. The ABCC2 has shown to have specific binding towards Cry1Ac and is involved in the toxic process of Cry1A proteins, but the role of this transporter and how it relates with the Cry1A proteins is still unknown. Here, we have characterized the interactions between the SeABCC2 and the main proteins that bind to the receptor. …

0301 basic medicineCell SurvivalBacillus thuringiensisATP-binding cassette transporterSpodopteraSpodopteraBiochemistryHemolysin Proteins03 medical and health sciences0302 clinical medicineBacterial ProteinsProtein DomainsBacillus thuringiensisSf9 CellsAnimalsBinding siteReceptorMolecular BiologyBinding SitesBacillus thuringiensis ToxinsbiologyChemistryfungifood and beveragesTransporterCell Biologybiology.organism_classificationMultidrug Resistance-Associated Protein 2Endotoxins030104 developmental biologyMembrane proteinCry1AcBiochemistryMutationInsect ProteinsMultidrug Resistance-Associated ProteinsProtein Multimerization030217 neurology & neurosurgeryProtein BindingBiochemical Journal
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Study of the bacillus thuringiensis Cry1Ia protein oligomerization promoted by midgut brush border membrane vesicles of lepidopteran and coleopteran …

2020

Bacillus thuringiensis (Bt) produces insecticidal proteins that are either secreted during the vegetative growth phase or accumulated in the crystal inclusions (Cry proteins) in the stationary phase. Cry1I proteins share the three domain (3D) structure typical of crystal proteins but are secreted to the media early in the stationary growth phase. In the generally accepted mode of action of 3D Cry proteins (sequential binding model), the formation of an oligomer (tetramer) has been described as a major step, necessary for pore formation and subsequent toxicity. To know if this could be extended to Cry1I proteins, the formation of Cry1Ia oligomers was studied by Western blot, after the incuba…

Leptinotarsa decemlineataBrush borderHealth Toxicology and MutagenesisBacillus thuringiensislcsh:MedicineSf21 cell lineOstrinia nubilalisToxicologyOligomer formationHemolysin Proteins<i>leptinotarsa decemlineata</i>03 medical and health sciencesWestern blotBacillus thuringiensisLobesia botranaSf9 CellsmedicineAnimalsProtein oligomerizationCry1AbIncubation<i>ostrinia nubilalis</i>030304 developmental biology0303 health sciencesBinding SitesBacillus thuringiensis ToxinsMicrovillimedicine.diagnostic_testbiology030306 microbiologyChemistryCommunicationVesiclelcsh:RfungiMembrane ProteinsMidgut<i>lobesia botrana</i>Trypsinbiology.organism_classificationColeopteraEndotoxinsLepidopteraBiochemistryBioassayProtein MultimerizationProtein Bindingmedicine.drug
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Insect Cells for Heterologous Production of Recombinant Proteins

2010

Heterologous gene expression has become an indispensable and powerful tool for the production and subsequent functional analysis of proteins that are difficult to purify from their natural sources. Furthermore, it is the method of choice for the production of variants by introducing site-specific mutations into the DNA encoding the protein of interest. However, many systems are biased by disadvantages. The inability of bacteria to confer important post-translational modifications often results in functional failure of the recombinant protein. In addition, disulfide bonds are not formed properly in bacterial systems. Mammalian cells on the other hand modify properly, but they generally provi…

PlasmidBiochemistryChemistrylawRecombinant DNAProtein biosynthesisHeterologousSf9TransfectionHeterologous expressionlaw.inventionSf21
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Midgut aminopeptidase N isoforms from Ostrinia nubilalis: Activity characterization and differential binding to Cry1Ab and Cry1Fa proteins from Bacil…

2013

Aminopeptidase N (APN) isoforms from Lepidoptera are known for their involvement in the mode of action of insecticidal Cry proteins from Bacillus thuringiensis. These enzymes belong to a protein family with at least eight different members that are expressed simultaneously in the midgut of lepidopteran larvae. Here, we focus on the characterization of the APNs from Ostrinia nubilalis (OnAPNs) to identify potential Cry receptors. We expressed OnAPNs in insect cells using a baculovirus system and analyzed their enzymatic activity by probing substrate specificity and inhibitor susceptibility. The interaction with Cry1Ab and Cry1Fa proteins (both found in transgenic insect-resistant maize) was …

Gene isoformendocrine systemCD13 AntigensMothsBiochemistrySubstrate SpecificityOstriniaHemolysin ProteinsBacterial ProteinsBacillus thuringiensisToxicity TestsSf9 CellsAnimalsReceptorMolecular Biologychemistry.chemical_classificationBacillus thuringiensis ToxinsbiologyfungiMidgutbiology.organism_classificationLigand (biochemistry)Molecular biologyEndotoxinsGastrointestinal TractIsoenzymesBlotEnzymechemistryBiochemistryInsect ScienceProtein BindingInsect Biochemistry and Molecular Biology
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Functional characterization of two human olfactory receptors expressed in the baculovirus Sf9 insect cell system

2005

Olfactory receptors (ORs) are the largest member of the G-protein-coupled receptors which mediate early olfactory perception in discriminating among thousands of odorant molecules. Assigning odorous ligands to ORs is a prerequisite to gaining an understanding of the mechanisms of odorant recognition. The functional expression of ORs represents a critical step in addressing this issue. Due to limitations in heterologous expression, very few mammal ORs have been characterized, and so far only one is from human origin. Consequently, OR function still remains poorly understood, especially in humans, whose genome encodes a restricted chemosensory repertoire compared with most mammal species. In …

InsectaPhysiologyG protein[SPI.GPROC] Engineering Sciences [physics]/Chemical and Process EngineeringSf9BiologyOlfactory Receptor NeuronsCell LineReceptors G-Protein-Coupled03 medical and health sciencesBehavioral Neuroscience0302 clinical medicineCalcium imagingPhysiology (medical)[SDV.IDA]Life Sciences [q-bio]/Food engineeringmedicineAnimalsHumans[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringReceptorComputingMilieux_MISCELLANEOUS030304 developmental biologyG protein-coupled receptorOrphan receptor0303 health sciencesMicroscopy ConfocalOlfactory receptorGenomics[SDV.IDA] Life Sciences [q-bio]/Food engineeringGTP-Binding Protein alpha SubunitsSensory SystemsCell biologyINSECTEmedicine.anatomical_structureOdorantsImmunologyCalcium[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]Heterologous expressionBaculoviridae030217 neurology & neurosurgery
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Role of Bacillus thuringiensis Cry1A toxins domains in the binding to the ABCC2 receptor from Spodoptera exigua

2018

Abstract Cry proteins from Bacillus thuringiensis (Bt) have been used to control insect pests either as formulated sprays or as in Bt-crops. However, field-evolved resistance to Bt proteins is threatening the long-term use of Bt products. The SeABCC2 locus has been genetically linked to resistance to a Bt bioinsecticide (Xentari™) in Spodoptera exigua (a mutation producing a truncated form of the transporter lacking an ATP binding domain was found in the resistant insects). Here, we investigated the role of SeABCC2 in the mode of action of Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ca, and two Cry1A-1Ca hybrids by expressing the receptor in Sf21 and HEK293T cell lines. Cell toxicity assays showed that Sf2…

0106 biological sciences0301 basic medicineCell SurvivalBacillus thuringiensisGene ExpressionSpodopteraSpodopteraTransfection01 natural sciencesBiochemistryHemolysin ProteinsStructure-Activity Relationship03 medical and health sciencesBacterial ProteinsProtein DomainsBacillus thuringiensisExiguaSf9 CellsAnimalsHumansProtein IsoformsBinding siteReceptorMolecular BiologySf21Binding SitesBacillus thuringiensis Toxinsbiologyfungibiology.organism_classificationMultidrug Resistance-Associated Protein 2Recombinant ProteinsClone CellsEndotoxins010602 entomologyHEK293 Cells030104 developmental biologyBiochemistryCry1AcLarvaInsect ScienceMutationInsect ProteinsMultidrug Resistance-Associated ProteinsPlasmidsProtein BindingBinding domainInsect Biochemistry and Molecular Biology
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Improvement of baculovirus as protein expression vector and as biopesticide by CRISPR/Cas9 editing

2019

The clustered regularly interspaced short palindromic repeats (CRISPR) system?associated Cas9 endonuclease is a molecular tool that enables specific sequence editing with high efficiency. In this study, we have explored the use of CRISPR/Cas9 system for the engineering of baculovirus. We have shown that the delivering of Cas9-single guide RNA ribonucleoprotein (RNP) complex with or without DNA repair template into Sf21 insect cells through lipofection might be efficient to produce knockouts as well as knock-ins into the baculovirus. To evaluate potential application of our CRISPR/Cas9 method to improve baculovirus as protein expression vector and as biopesticide, we attempted to knockout se…

DNA repairvirusesBACULOVIRUSGenetic VectorsBioengineeringComputational biologyGenome ViralINGENIERÍAS Y TECNOLOGÍASBiologySpodopteraApplied Microbiology and BiotechnologyGenomelaw.inventionBiotecnología Industrial03 medical and health sciencesGenome editingGENOME EDITINGlawKNOCK-INSf9 CellsCRISPRAnimalsVector (molecular biology)Guide RNANUCLEOPOLYHEDROVIRUSPest Control BiologicalGeneCRISPR/CAS9030304 developmental biologyRibonucleoproteinGene Editing0303 health sciencesExpression vector030306 microbiologyCas93. Good healthKNOCKOUTRecombinant DNACRISPR-Cas SystemsBaculoviridaeBiotechnology
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Overexpression and functional characterization of kinin receptors reveal subtype-specific phosphorylation.

1999

G protein-coupled receptors such as the receptors for bradykinin are present in low copy numbers in most natural cells. To overcome the problems associated with the analysis of these receptors at the protein level, we used highly efficient expression systems such as the baculovirus/insect cell system. However, the structural and functional statuses of recombinant receptors have often remained elusive. We have expressed the two types of human kinin receptors, B1 and B2, in Sf9 cells. Both receptors are found on the surface of infected cells where they display the same pharmacological profiles as their cognate receptors of native cells. The functional analysis of kinin receptors coupled to th…

DNA ComplementaryReceptor Bradykinin B2ImmunoprecipitationSf9SpodopteraBradykininReceptor Bradykinin B1TransfectionBiochemistryAnimalsHumansBinding siteCloning MolecularPhosphorylationReceptorMicroscopy ConfocalKinaseChemistryReceptors BradykininCell MembraneKininMolecular biologyRecombinant ProteinsCell biologyKineticsPhosphorylationCalciumIntracellularBiochemistry
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Protein tyrosine nitration and thiol oxidation by peroxynitrite-strategies to prevent these oxidative modifications.

2013

The reaction product of nitric oxide and superoxide, peroxynitrite, is a potent biological oxidant. The most important oxidative protein modifications described for peroxynitrite are cysteine-thiol oxidation and tyrosine nitration. We have previously demonstrated that intrinsic heme-thiolate (P450)-dependent enzymatic catalysis increases the nitration of tyrosine 430 in prostacyclin synthase and results in loss of activity which contributes to endothelial dysfunction. We here report the sensitive peroxynitrite-dependent nitration of an over-expressed and partially purified human prostacyclin synthase (3.3 μM) with an EC50 value of 5 μM. Microsomal thiols in these preparations effectively co…

thiol oxidationprotein tyrosine nitrationlcsh:Chemistrychemistry.chemical_compoundCytochrome P-450 Enzyme SystemSf9 CellsTyrosinelcsh:QH301-705.5Spectroscopychemistry.chemical_classification0303 health sciencesbiologySuperoxide030302 biochemistry & molecular biologyGeneral MedicineComputer Science ApplicationsIntramolecular OxidoreductasesBiochemistryThiolprostacyclin synthasesuperoxideOxidation-ReductionPeroxynitriteOxidative phosphorylationSpodopteraCatalysisArticleperoxynitriteNitric oxideProstacyclin synthaseInorganic Chemistry03 medical and health sciencesnitric oxideddc:570NitrationPeroxynitrous AcidAnimalsHumansSulfhydryl CompoundsPhysical and Theoretical ChemistryMolecular Biology030304 developmental biologyOrganic Chemistrynitric oxide; superoxide; peroxynitrite; protein tyrosine nitration; thiol oxidation; peroxynitrite scavengers; prostacyclin synthasechemistrylcsh:Biology (General)lcsh:QD1-999biology.proteinTyrosineCattleperoxynitrite scavengersProtein Processing Post-TranslationalInternational journal of molecular sciences
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Human parvovirus B19 induced apoptotic bodies contain altered self-antigens that are phagocytosed by antigen presenting cells.

2013

Human parvovirus B19 (B19V) from the erythrovirus genus is known to be a pathogenic virus in humans. Prevalence of B19V infection has been reported worldwide in all seasons, with a high incidence in the spring. B19V is responsible for erythema infectiosum (fifth disease) commonly seen in children. Its other clinical presentations include arthralgia, arthritis, transient aplastic crisis, chronic anemia, congenital anemia, and hydrops fetalis. In addition, B19V infection has been reported to trigger autoimmune diseases such as systemic lupus erythematosus and rheumatoid arthritis. However, the mechanisms of B19V participation in autoimmunity are not fully understood. B19V induced chronic dise…

Programmed cell deathScienceAntigen-Presenting CellsArthritisApoptosisAutoimmunitySpodopteraViral Nonstructural ProteinsBiologymedicine.disease_causeAutoantigensVirusautoimmuniteettiImmune toleranceAutoimmunityParvoviridae InfectionsPathogenesis03 medical and health sciences0302 clinical medicineImmune systemPhagocytosisImmune ToleranceParvovirus B19 HumanSf9 CellsHuman Parvovirus B19medicineta319AnimalsHumansAntigen-presenting cellself-antigens030304 developmental biology0303 health sciencesMultidisciplinaryQta1182RHep G2 CellsFlow Cytometrymedicine.diseaseVirology3. Good healthImmunologyMicroscopy Electron ScanningMedicineResearch Article030215 immunologyPLoS ONE
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