Search results for "Spodoptera"

showing 10 items of 125 documents

Avidin Is a Promising Tag for Fusion Proteins Produced in Baculovirus-Infected Insect Cells

1999

The baculovirus expression vector system (BEVS) has become one of the most versatile and powerful eukaryotic systems for recombinant protein expression. We have constructed a novel baculovirus transfer vector (pbacAVs+C) which allows for the efficient production, detection, and single-step purification of the desired molecule as a secretion-compatible avidin fusion protein in insect cells. It also enables fast construction of the baculoviruses by site-specific transposition in Escherichia coli. To demonstrate the power of this vector, we report here on the production of immunologically intact hevein, a major cysteine-rich latex allergen, as avidin fusion protein. Our results indicate that a…

EnteropeptidaseStreptavidinRecombinant Fusion ProteinsGenetic VectorsMolecular Sequence DataGene ExpressionSpodopteramedicine.disease_causeCell Linelaw.invention03 medical and health scienceschemistry.chemical_compoundlawLectinsmedicineAnimalsAmino Acid SequenceEscherichia coliPeptide sequenceDNA PrimersPlant Proteins030304 developmental biology0303 health sciencesBinding SitesBase Sequencebiology030302 biochemistry & molecular biologyAvidinFusion proteinMolecular biologyEnteropeptidasechemistryBiochemistryCell culturebiology.proteinRecombinant DNAPlant LectinsBaculoviridaeAntimicrobial Cationic PeptidesPlasmidsBiotechnologyAvidinProtein Expression and Purification
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Hastifolins A-G, antefeedant neo-clerodane diterpenoids from Scutellaria hastifolia

2010

From the aerial parts of Scutellaria hastifolia, family Lamiaceae (Labiatae), seven neo-clerodane diterpenoids (hastifolins A-G) were isolated. The products are similar to the known scuteparvin and are characterized by being trans-cinnamoyl derivatives. Structures and stereochemistry were determined by intensive NMR investigation. Six of the products form three pairs of epimers at C-13. Hastifolins A-C showed significant antifeedant activity.

Family LamiaceaeStereochemistryScutellariaChemical structurePlant ScienceHorticultureSpodopteraBiochemistryDiterpenes Clerodanechemistry.chemical_compoundFeeding behaviorAnimalsMolecular BiologyNuclear Magnetic Resonance BiomolecularbiologyMolecular StructureGeneral MedicineFeeding BehaviorSettore CHIM/06 - Chimica Organicabiology.organism_classificationTerpenoidchemistryLarvaScutellariaLamiaceaeEpimerDiterpeneScutellaria hastifolia Lamiaceae diterpenes neo-clerodanes epimers antifeedant
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Horizontally transmitted parasitoid killing factor shapes insect defense to parasitoids

2021

Protection from parasitism by a virus Parasitoid wasps have developed myriad systems to overcome the defense mechanisms of their hosts as they lay their eggs in the bodies and eggs of targeted species. Gasmi et al . report how the host can fight back when infected by a virus that expresses a protein conferring resistance to the parasitoid. When members of the butterfly and moth family are targeted by wasps, a protein family has evolved that is horizontally carried by viruses—and sometimes is incorporated into the host genome—and impairs the ability of parasitoid offspring to fully develop and emerge. Characterizing the ability of this protein to protect hosts against specific parasites, the…

Gene Transfer Horizontalmedia_common.quotation_subjectGenome InsectWaspsZoologyParasitismApoptosisInsect VirusesInsectSpodopteraCompetition (biology)Host-Parasite InteractionsParasitoidLepidoptera genitaliaViral Proteins03 medical and health sciences0302 clinical medicineEvolutionary arms raceAnimals030304 developmental biologymedia_common0303 health sciencesMultidisciplinarybiologyHost (biology)fungibiology.organism_classificationBiological EvolutionMicrogastrinaeNucleopolyhedrovirusesLepidopteraLarvaEntomopoxvirinaeInsect Proteins030217 neurology & neurosurgeryScience
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Disassembly of structurally modified viral nanoparticles: characterization by fluorescence correlation spectroscopy.

2005

Abstract Analysis of the breakdown products of engineered viral particles can give useful information on the particle structure. We used various methods to breakdown both a recombinant enveloped virus and virus-like particles (VLPs) from two non-enveloped viruses and analysed the resulting subunits by fluorescence correlation spectroscopy (FCS). Analysis of the enveloped baculovirus, Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV), displaying the green fluorescent protein (GFP) fused to its envelope protein gp64 was performed in the presence and absence of 5 mM SDS and 25 mM DTT. Without treatment, the viral particle showed a diffusion time of 3.3 ms. In the presence of SDS…

General Immunology and MicrobiologyChemistryvirusesRecombinant Fusion ProteinsGreen Fluorescent ProteinsTrimerFluorescence correlation spectroscopyGeneral MedicineMothsSpodopteraFluorescenceMolecular biologyGeneral Biochemistry Genetics and Molecular BiologyGreen fluorescent proteinCell LineKineticsViral ProteinsVirus-like particleViral envelopeCapsidParticleAnimalsGeneral Agricultural and Biological SciencesBaculoviridaeComptes rendus biologies
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Baculoviral display of functional scFv and synthetic IgG-binding domains.

2000

Viral vectors displaying specific ligand binding moities such as scFv fragments or intact antibodies hold promise for the development of targeted gene therapy vectors. In this report we describe baculoviral vectors displaying either functional scFv fragments or the synthetic Z/ZZ IgG binding domain derived from protein A. Display on the baculovirus surface was achieved via fusion of the scFv fragment or Z/ZZ domain to the N-terminus of gp64, the major envelope protein of the Autographa californica nuclear polyhedrosis virus, AcNPV. As examples of scFv fragments we have used a murine scFv specific for the hapten 2-phenyloxazolone and a human scFv specific for carcinoembryonic antigen. In pri…

Genetic enhancementvirusesRecombinant Fusion ProteinsBlotting WesternBiophysicschemical and pharmacologic phenomenaEnzyme-Linked Immunosorbent AssayVectors in gene therapySpodopteraBiochemistryViral vector03 medical and health sciencesMice0302 clinical medicineAntibody SpecificityPeptide LibraryAnimalsHumansMolecular BiologyImmunoglobulin FragmentsCells Cultured030304 developmental biology0303 health sciencesbiologyOxazoloneNuclear Polyhedrosis VirusCell Biologyrespiratory systembiology.organism_classificationMolecular biology3. Good healthCarcinoembryonic AntigenAutographa californicaIgG binding030220 oncology & carcinogenesisImmunoglobulin Gbiology.proteinBinding Sites AntibodyAntibodyHaptenBaculoviridaeHaptensViral Fusion ProteinsBiochemical and biophysical research communications
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The sf32 unique gene of Spodoptera frugiperda multiple nucleopolyhedrovirus (SfMNPV) is a non-essential gene that could be involved in nucleocapsid o…

2013

A recombinant virus lacking the sf32 gene (Sf32null), unique to the Spodoptera frugiperda multiple nucleopolyhedrovirus (SfMNPV), was generated by homologous recombination from a bacmid comprising the complete viral genome (Sfbac). Transcriptional analysis revealed that sf32 is an early gene. Occlusion bodies (OBs) of Sf32null contained 62% more genomic DNA than viruses containing the sf32 gene, Sfbac and Sf32null-repair, although Sf32null DNA was three-fold less infective when injected in vivo. Sf32null OBs were 18% larger in diameter and contained 17% more nucleocapsids within ODVs than those of Sfbac. No significant differences were detected in OB pathogenicity (50% lethal concentration)…

GenotypevirusesScienceGenome ViralSpodopteraSpodopteraVirus ReplicationOcclusion-derived virionsRecombinant virusHomology (biology)VirusViral Proteins03 medical and health sciencesAnimalsNucleocapsidSpodoptera frugiperda multiple nucleopolyhedrovirus (SfMNPV)Gene030304 developmental biology0303 health sciencesGenes Essential[SDV.BA.MVSA]Life Sciences [q-bio]/Animal biology/Veterinary medicine and animal HealthMultidisciplinaryNucleocapsid organizationbiology030306 microbiologyfungiQVirionRbiology.organism_classificationVirologyNucleopolyhedroviruses3. Good healthViral replicationEssential geneLarvaDNA Viral[SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/VirologyMedicinesf32Homologous recombinationResearch ArticlePLoS ONE
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Reduced membrane-bound alkaline phosphatase does not affect binding of Vip3Aa in a Heliothis virescens resistant colony

2020

The Vip3Aa insecticidal protein from Bacillus thuringiensis (Bt) is produced by specific transgenic corn and cotton varieties for efficient control of target lepidopteran pests. The main threat to this technology is the evolution of resistance in targeted insect pests and understanding the mechanistic basis of resistance is crucial to deploy the most appropriate strategies for resistance management. In this work, we tested whether alteration of membrane receptors in the insect midgut might explain the &gt

HELIOTHIS-VIRESCENSInsecticidesHealth Toxicology and Mutagenesislcsh:MedicinePROTEIN0601 Biochemistry and Cell BiologyToxicologyBiotecnologiaInsecticide ResistanceBacillus thuringiensisSITES0303 health sciencesbiologyChemistryfood and beveragesPlants Genetically ModifiedLepidopteraBiochemistryFood Science & TechnologyInsect ProteinsAlkaline phosphatase1115 Pharmacology and Pharmaceutical Sciencestobacco budwormLife Sciences & BiomedicineSPODOPTERA-FRUGIPERDA MIDGUTProtein BindingEXPRESSIONBrush borderBacillus thuringiensisCRY1ACArticleVESICLES03 medical and health sciencesBACILLUS-THURINGIENSISBacterial ProteinsDownregulation and upregulationinsecticidal proteinsCell surface receptor<i>Bacillus thuringiensis</i>AnimalsCROPS030304 developmental biologyScience & TechnologyGenetically modified maizeHeliothis virescens030306 microbiologylcsh:RfungiMembrane ProteinsMidgutAlkaline Phosphatasebiology.organism_classificationTOXIN RESISTANCEinsect resistanceProteïnes
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Human histidine-rich glycoprotein expressed in SF9 insect cells inhibits apatite formation

1997

Histidine-rich glycoprotein (HRG) is structurally related to the alpha2-HS glycoprotein/fetuin family of mammalian plasma proteins; both belong to the cystatin superfamily of proteins. We expressed recombinant human HRG and alpha2-HS in Sf9 insect cells for functional analysis. Recombinant HRG bound heparin and fibrinogen while alpha2-HS did not. Both proteins inhibited the formation of apatite, recombinant HRG (IC50 approximately 1 microM) with 2-fold lower molar activity than alpha2-HS (IC50 approximately 0.5 microM). The inhibition in vitro of apatite formation suggests a new function for plasma HRG protein, inhibition of phase separation in blood vessels.

Histidine-rich glycoproteinHistidine-rich glycoproteinalpha-2-HS-GlycoproteinBiophysicsSerum proteinSf9SpodopteraFibrinogenBiochemistryα2-HS-glycoproteinBone and BonesCell Linelaw.inventionStructural BiologylawApatitesCalcium homeostasisGeneticsmedicineAnimalsHumansMolecular Biologychemistry.chemical_classificationHeparinChemistryProteinsBlood ProteinsCell BiologyFetuinBlood proteinsRecombinant ProteinsIn vitroBiochemistryProtein BiosynthesisRecombinant DNAGlycoproteinProtein Bindingmedicine.drugFEBS Letters
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Protein Kinase C μ Is Regulated by the Multifunctional Chaperon Protein p32

2000

We identified the multifunctional chaperon protein p32 as a protein kinase C (PKC)-binding protein interacting with PKCalpha, PKCzeta, PKCdelta, and PKC mu. We have analyzed the interaction of PKC mu with p32 in detail, and we show here in vivo association of PKC mu, as revealed from yeast two-hybrid analysis, precipitation assays using glutathione S-transferase fusion proteins, and reciprocal coimmunoprecipitation. In SKW 6.4 cells, PKC mu is constitutively associated with p32 at mitochondrial membranes, evident from colocalization with cytochrome c. p32 interacts with PKC mu in a compartment-specific manner, as it can be coimmunoprecipitated mainly from the particulate and not from the so…

ImmunoprecipitationRecombinant Fusion ProteinsGolgi ApparatusSaccharomyces cerevisiaeSpodopteraMitogen-activated protein kinase kinaseBiologyTransfectionBiochemistryCell LineMitochondrial ProteinsAnimalsHumansCloning MolecularKinase activityMolecular BiologyProtein Kinase CProtein kinase CGlutathione TransferaseB-LymphocytesBinding SitesMembrane GlycoproteinsKinaseAutophosphorylationJNK Mitogen-Activated Protein KinasesCell BiologyFusion proteinMitochondriaReceptors ComplementCell biologybody regionsHyaluronan ReceptorsProtein kinase domainBiochemistryMitogen-Activated Protein KinasesCarrier ProteinsMolecular ChaperonesProtein BindingJournal of Biological Chemistry
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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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