Search results for "INSECT"

showing 10 items of 2033 documents

Mutations in the Bacillus thuringiensis Cry1Ca toxin demonstrate the role of domains II and III in specificity towards Spodoptera exigua larvae

2004

Several mutants of the Bacillus thuringiensis Cry1Ca toxin affected with regard to specific activity towards Spodoptera exigua were studied. Alanine was used to replace single residues in loops 2 and 3 of domain II (mutant pPB19) and to replace residues 541– 544 in domain III (mutant pPB20). Additionally, a Cry1Ca mutant combining all mutations was constructed (mutant pPB21). Toxicity assays showed a marked decrease in toxicity against S. exigua for all mutants, while they retained their activity against Manduca sexta, confirming the importance of these residues in determining insect specificity. Parameters for binding to the specific receptors in BBMV (brush border membrane vesicles) of S.…

Models MolecularMutantLaboratory of Virologyaminopeptidase nmedicine.disease_causeBiochemistrybrush-border membraneToxin oligomerizationSubstrate SpecificityBacterial toxin; Manduca sexta; Mode of action; Protoxin activation; Toxin oligomerization; Toxin receptor bindingHemolysin Proteinsmanduca-sextaBacillus thuringiensisheliothis-virescensAlanine:CIENCIAS DE LA VIDA::Bioquímica [UNESCO]MicrovillibiologyPRI BioscienceBiochemistryMode of actionLarvaThermodynamicsResearch ArticleProtein BindingBacterial Toxinspink-bollwormBacillus thuringiensisSpodopteraSpodopteraBinding CompetitiveManduca sextaLaboratorium voor VirologieBacterial ProteinsExiguamedicineirreversible bindingAnimalscrystal proteinsProtoxin activationProtein Structure QuaternaryMode of actionMolecular BiologyBacillus thuringiensis ToxinsToxin receptor bindingToxininsecticidal toxinpore formationCytoplasmic VesiclesfungiUNESCO::CIENCIAS DE LA VIDA::BioquímicaBacterial toxinCell Biologybiology.organism_classificationProtein Structure TertiaryEndotoxinsManduca sextaMutationcryia delta-endotoxins
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Effect of ATP Binding and Hydrolysis on Dynamics of Canine Parvovirus NS1▿ †

2010

ABSTRACT The replication protein NS1 is essential for genome replication and protein production in parvoviral infection. Many of its functions, including recognition and site-specific nicking of the viral genome, helicase activity, and transactivation of the viral capsid promoter, are dependent on ATP. An ATP-binding pocket resides in the middle of the modular NS1 protein in a superfamily 3 helicase domain. Here we have identified key ATP-binding amino acid residues in canine parvovirus (CPV) NS1 protein and mutated amino acids from the conserved A motif (K406), B motif (E444 and E445), and positively charged region (R508 and R510). All mutations prevented the formation of infectious viruse…

Models MolecularParvovirus CaninevirusesImmunologyMolecular Sequence DataPlasma protein bindingViral Nonstructural ProteinsMicrobiologyCell Linechemistry.chemical_compoundAdenosine TriphosphateDogsVirologyAnimalsAmino Acid SequenceBinding siteBinding SitesbiologyHydrolysisDNA replicationHelicaseFluorescence recovery after photobleachingFusion proteinMolecular biologyGenome Replication and Regulation of Viral Gene ExpressionProtein Structure TertiaryViral replicationchemistryBiochemistryAmino Acid SubstitutionInsect Sciencebiology.proteinCatsMutagenesis Site-DirectedSequence AlignmentDNAProtein Binding
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News from an Ancient World: Two Novel Astacin Metalloproteases from the Horseshoe Crab

2008

In this work, we report the cloning, heterologous expression, and characterization of two novel astacin proteases from the chelicerate Limulus polyphemus (horseshoe crab), designated as LAST (Limulus astacin) and LAST_MAM (Limulus astacin containing a MAM domain), respectively. The expression pattern showed ubiquitous occurrence of LAST_MAM, while LAST was predominantly restricted to the eyes and brain, indicating a function in the nervous system. Both enzymes contain the characteristic metzincin-type zinc-binding region and Met turn. While LAST is made up only of the typical prodomain and astacin-like protease domain, LAST_MAM contains an additional MAM (meprin A5 protein tyrosine phosphat…

Models MolecularProteasesDNA ComplementaryInsectaProtein familymedicine.medical_treatmentMolecular Sequence DataContext (language use)Protein tyrosine phosphataseBiologyHydroxamic AcidsNervous SystemCollagen Type IGene Expression Regulation EnzymologicCell LineEvolution MolecularStructural BiologyHorseshoe CrabsmedicineAnimalsProtein oligomerizationAmino Acid SequenceRNA MessengerCloning MolecularMolecular BiologyPhylogenyExtracellular Matrix ProteinsProteaseBase SequenceCaseinsMetalloendopeptidasesbiology.organism_classificationProtein Structure TertiaryBiochemistryStructural Homology ProteinLimulusAstacinOligopeptidesProtein Processing Post-TranslationalJournal of Molecular Biology
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The crystal structure of a cockroach pheromone-binding protein suggests a new ligand binding and release mechanism.

2003

Pheromone-binding proteins (PBPs) are small helical proteins found in sensorial organs, particularly in the antennae, of moth and other insect species. They were proposed to solubilize and carry the hydrophobic pheromonal compounds through the antennal lymph to receptors, participating thus in the peri-receptor events of signal transduction. The x-ray structure of Bombyx mori PBP (BmorPBP), from male antennae, revealed a six-helix fold forming a cavity that contains the pheromone bombykol. We have identified a PBP (LmaPBP) from the cockroach Leucophaea maderae in the antennae of the females, the gender attracted by pheromones in this species. Here we report the crystal structure of LmaPBP a…

Models MolecularProtein FoldingProtein ConformationMolecular Sequence DataCockroachesCrystallography X-RayLigandsBiochemistryBombykolchemistry.chemical_compoundBombyx moribiology.animalAnimalsAmino Acid SequenceCloning MolecularMolecular BiologyFluorescent DyesCockroachbiologySequence Homology Amino AcidCell BiologyHydrogen-Ion Concentrationbiology.organism_classificationLigand (biochemistry)BombyxButanonesTransport proteinKineticschemistryBiochemistryHelixBiophysicsPheromoneInsect ProteinsFemalePheromone binding proteinCarrier ProteinsProtein BindingThe Journal of biological chemistry
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Proteome response of Tribolium castaneum larvae to Bacillus thuringiensis toxin producing strains.

2012

Susceptibility of Tribolium castaneum (Tc) larvae was determined against spore-crystal mixtures of five coleopteran specific and one lepidopteran specific Bacillus thuringiensis Cry toxin producing strains and those containing the structurally unrelated Cry3Ba and Cry23Aa/Cry37Aa proteins were found toxic (LC(50) values 13.53 and 6.30 µg spore-crystal mixture/µL flour disc, respectively). Using iTRAQ combined with LC-MS/MS allowed the discovery of seven novel differentially expressed proteins in early response of Tc larvae to the two active spore-crystal mixtures. Proteins showing a statistically significant change in treated larvae compared to non-intoxicated larvae fell into two major cat…

Models MolecularProteomicsProteomeTranscription GeneticOdorant bindingProtein ConformationApplied Microbiologylcsh:MedicinePathogenesismedicine.disease_causeReceptors OdorantBiochemistryProtein structureBacillus thuringiensislcsh:SciencePhylogenyTriboliumMultidisciplinaryImmune System ProteinsSpectrometric Identification of ProteinsbiologyChemosensory proteinAgricultureHost-Pathogen InteractionLarvaHost-Pathogen InteractionsInsect ProteinsResearch Articleanimal structuresProtein subunitLipoproteinsBacterial ToxinsMolecular Sequence DataBacillus thuringiensisMicrobiologyBacterial ProteinsRibosomal proteinMicrobial ControlDefense ProteinsmedicineAnimalsAmino Acid SequencePesticidesBiologyToxinfungilcsh:RProteinsbiology.organism_classificationMolecular biologyApolipoproteinsOdorant-binding proteinbiology.proteinlcsh:QPest ControlSequence AlignmentZoologyEntomologyProtein AbundancePLoS ONE
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Cockroach allergens Per a 3 are oligomers

2009

Allergens from cockroaches cause major asthma-related health problems worldwide. Among them Per a 3 belongs to the most potent allergens. Although the sequences of some members of the Per a 3-family are known, their biochemical and biophysical properties have not been investigated. Here we present for the first time a thorough structural characterization of these allergens, which have recently been tested to induce an increase of allergy specific indicators in blood of Europeans. We isolated two Per a 3 isoforms, which occur freely dissolved in the hemolymph as hexamers with molecular masses of 465+/-25kDa (P II) and 512+/-25kDa (P I). Their sedimentation coefficients (S(20,W)) were determi…

Models MolecularSequence analysismedicine.medical_treatmentProtein subunitMolecular Sequence DataImmunologySequence alignmentRandom hexamermedicine.disease_causeMass SpectrometryAllergenmedicineAnimalsPeriplanetaProtein IsoformsAmino Acid SequencePeptide sequenceBase SequencebiologyCircular DichroismHemocyaninSequence Analysis DNAAllergensbiology.organism_classificationMicroscopy ElectronMicroscopy FluorescenceBiochemistryImmunologyInsect ProteinsElectrophoresis Polyacrylamide GelAmerican cockroachSequence AlignmentUltracentrifugationDevelopmental BiologyDevelopmental & Comparative Immunology
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The Minor Capsid Protein VP11 of Thermophilic Bacteriophage P23-77 Facilitates Virus Assembly by Using Lipid-Protein Interactions

2015

ABSTRACT Thermus thermophilus bacteriophage P23-77 is the type member of a new virus family of icosahedral, tailless, inner-membrane-containing double-stranded DNA (dsDNA) viruses infecting thermophilic bacteria and halophilic archaea. The viruses have a unique capsid architecture consisting of two major capsid proteins assembled in various building blocks. We analyzed the function of the minor capsid protein VP11, which is the third known capsid component in bacteriophage P23-77. Our findings show that VP11 is a dynamically elongated dimer with a predominantly α-helical secondary structure and high thermal stability. The high proportion of basic amino acids in the protein enables electrost…

Models MolecularvirusesMolecular Sequence DataStatic ElectricityImmunologyMicrobiologyProtein–protein interactionBacteriophagechemistry.chemical_compoundCapsidVirologyBacteriophagesAmino Acid SequenceThermusPeptide sequenceProtein secondary structureprotein-lipid systemsbiologyVirus AssemblyStructure and AssemblyCapsomereVirionThermus thermophilusLipid Metabolismbiology.organism_classificationLipidsMolecular biologychemistryCapsidInsect Sciencethermophilic virusesBiophysicsCapsid ProteinsDNAkapsidiJournal of Virology
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Crystallization and preliminary crystallographic study of a pheromone-binding protein from the cockroachLeucophaea maderae

2002

Pheromone-binding proteins (PBPs) are small helical proteins (13-18 kDa) present in various sensory organs of moths and other insect species. An antennal protein from the cockroach Leucophaea maderae (LmaPBP) has been found to share all the hallmarks of the PBP family and is expressed specifically in the female adult antennae, the gender that perceives the sex pheromone. Here, the crystallization of LmaPBP expressed as a recombinant protein in Escherichia coli periplasm is reported. Crystals of LmaPBP were obtained by the sitting-drop vapour-diffusion method using a nanodrop-dispensing robot. The protein crystallizes in two different crystal forms. Form 1 belongs to space group P1, with uni…

Molecular Sequence DataCockroachesCrystallography X-Raymedicine.disease_causelaw.inventionStructural Biologylawbiology.animalmedicineAnimalsAmino Acid SequenceCrystallizationEscherichia coliCockroachSequence Homology Amino AcidbiologyChemistryResolution (electron density)General MedicinePeriplasmic spaceRecombinant ProteinsCrystallographySex pheromoneRecombinant DNAInsect ProteinsFemaleCarrier ProteinsCrystallizationPheromone binding proteinSequence AlignmentActa Crystallographica Section D Biological Crystallography
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Characterization of the hemoglobin of the backswimmer Anisops deanei (Hemiptera).

2012

Abstract While O 2 -binding hemoglobin-like proteins are present in many insects, prominent amounts of hemoglobin have only been found in a few species. Backswimmers of the genera Anisops and Buenoa (Notonectidae) have high concentrations of hemoglobin in the large tracheal cells of the abdomen. Oxygen from the hemoglobin is delivered to a gas bubble and controls the buoyant density, which enables the bugs to maintain their position without swimming and to remain stationary in the mid-water zone where they hunt for prey. We have obtained the cDNA sequences of three Anisops deanei hemoglobin chains by RT-PCR and RACE techniques. The deduced amino acid sequences show an unusual insertion of a…

Molecular Sequence DataNotonectidaeLigandsBiochemistrylaw.inventionHemipteraHemoglobinslawComplementary DNAAnimalsHumansGlobinAmino Acid SequenceMolecular BiologyPhylogenychemistry.chemical_classificationbiologyHeteropteraSequence Analysis DNAbiology.organism_classificationHemipteraBiological EvolutionAmino acidOxygenKineticschemistryBiochemistryInsect ScienceRecombinant DNAInsect ProteinsHemoglobinInsect biochemistry and molecular biology
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Molecular characterization of the zerknüllt region of the Antennapedia complex of D. subobscura.

1995

We have characterized at the molecular level the zerknullt (zen) region of the Drosophila subobscura Antennapedia complex. The sequence comparison between D. subobscura and D. melanogaster shows an irregular distribution of the conserved and diverged regions, with the homeobox and a putative activating domain completely conserved. Comparisons of the promoter sequence and pattern of expression of the gene during development suggest that the regulation of zen has been conserved during evolution. The conservation of zen expression in a subpopulation of the polar cells indicates the existence of an important role in such cells. We describe a transitory segmented pattern of expression of zen in …

Molecular Sequence DataPair-rule geneGenes InsectAntennapediaGenomeChromosomesGeneticsMelanogasterAnimalsDrosophila ProteinsAmino Acid SequenceRNA MessengerCloning MolecularPromoter Regions GeneticGeneGenetics (clinical)In Situ HybridizationGeneticsHomeodomain ProteinsbiologyBase SequencefungiGenes HomeoboxChromosomeChromosome MappingGene Expression Regulation DevelopmentalNuclear Proteinsbiology.organism_classificationDrosophila subobscuraDNA-Binding ProteinsRepressor ProteinsInsect HormonesAntennapedia Homeodomain ProteinHomeoboxDrosophilaSequence AlignmentTranscription FactorsChromosoma
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