Search results for "InSe"

showing 10 items of 3069 documents

Genomics and Proteomics Analyses Revealed Novel Candidate Pesticidal Proteins in a Lepidopteran-Toxic Bacillus thuringiensis Strain

2020

Discovery and identification of novel insecticidal proteins in Bacillus thuringiensis (Bt) strains are of crucial importance for efficient biological control of pests and better management of insect resistance. In this study, the Bt strain KhF, toxic for Plodia interpunctella and Grapholita molesta larvae, underwent genomics and proteomics analyses to achieve a better understanding of the bases of its pathogenicity. The whole-genome sequencing results revealed that the KhF strain contained nine coding sequences with homologies to Bt insecticidal genes. The lepidopteran toxic mixture of spores and crystals of this Bt strain was subjected to liquid chromatography and tandem mass spectrometry …

Health Toxicology and MutagenesisXpp proteinslcsh:MedicineMpp proteinsGenomicsinsect bioassayToxicologymedicine.disease_causeProteomicsTandem mass spectrometryDNA sequencing03 medical and health sciencesBacillus thuringiensismedicinecharacterizationLC-MS/MSGene<i>Plodia interpunctella</i>030304 developmental biology0303 health sciencesStrain (chemistry)biology030306 microbiologyToxinPharmacology. Therapylcsh:Rfungibiology.organism_classificationgenome sequencingBiochemistry<i>Grapholita molesta</i>Toxins
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Perlecan Maintains the Integrity of Cartilage and Some Basement Membranes

1999

Perlecan is a heparan sulfate proteoglycan that is expressed in all basement membranes (BMs), in cartilage, and several other mesenchymal tissues during development. Perlecan binds growth factors and interacts with various extracellular matrix proteins and cell adhesion molecules. Homozygous mice with a null mutation in the perlecan gene exhibit normal formation of BMs. However, BMs deteriorate in regions with increased mechanical stress such as the contracting myocardium and the expanding brain vesicles showing that perlecan is crucial for maintaining BM integrity. As a consequence, small clefts are formed in the cardiac muscle leading to blood leakage into the pericardial cavity and an ar…

Heart Defects Congenitalcardiac muscleMesenchymeSchwartz–Jampel syndromeRestriction MappingPerlecanBasement MembraneExtracellular matrixMiceMice CongenicchondrodysplasiaCalcification PhysiologicexencephalyLamininmedicineAnimalsNeural Tube DefectsCells CulturedBasement membranebiologyCartilageOssification HeterotopicHomozygoteCell Biologymedicine.diseaseMice Mutant StrainsBasement membrane assemblyCell biologyperlecanMutagenesis Insertionalmedicine.anatomical_structureCartilageBiochemistryGene Targetingbiology.proteinOriginal ArticleGenes LethalProteoglycansCollagenHeparitin SulfateExostoses Multiple HereditaryHeparan Sulfate ProteoglycansThe Journal of Cell Biology
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Differences in the midgut proteolytic activity of twoHeliothis virescens strains, one susceptible and one resistant toBacillus thuringiensis toxins

1996

The development of resistance to Bacillus thuringiensis toxic proteins is a growing concern because it could threaten both conventional and gene transfer use of this environmentally safe biological insecticide. The most common mechanism of resistance involves changes in binding affinity of toxin receptors in the insect midgut membrane. This has not been the case in Heliothis virescens. We have investigated changes in midgut proteolytic activity as a possibility to explain the resistance observed in this insect species. We have developed an improvement of known methods to demonstrate proteolytic activity in crude extracts. Using this method we have found differences in the proteolytic activi…

Heliothis virescensbiologyStrain (chemistry)PhysiologyToxinmedia_common.quotation_subjectfungiMidgutGeneral MedicineInsectbiology.organism_classificationmedicine.disease_causeBiochemistryIn vitroMicrobiologyInsect ScienceBacillus thuringiensismedicineReceptormedia_commonArchives of Insect Biochemistry and Physiology
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The Cylapinae of French Guiana: an illustrated catalogue with the description of a new species (Insecta, Heteroptera, Miridae)

2023

An illustrated catalogue of Cylapinae (Insecta, Heteroptera, Miridae) from French Guiana is provided. Valdasus cerdai, n. sp. is described as new. Cylapus antennatus (Carvalho &amp; Fontes, 1968), C. citus Bergroth, 1922, C. ruficeps Bergroth, 1922, C. tucuriensis (Carvalho, 1989) and Peltidocylapus caudatus Wolski, 2021 are recorded from French Guiana for the first time. The validity of Valdasoides Carvalho, 1989 is discussed. &#x0D;  

HemipteraCylapiniInsectaArthropodaFulviininew species for science and for French Guianatrue bugsAnimaliaAnimal Science and ZoologyBiodiversityMiridaeEcology Evolution Behavior and SystematicsTaxonomyZootaxa
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Hemocytes of Rhynchophorus ferrugineus (Olivier)(Coleoptera: Curculionidae) and their response to Saccharomyces cerevisiae and Bacillus thuringiensis

2011

Originally from tropical Asia, the Red Palm Weevil (RPW Rhynchophorus ferrugineus (Olivier) is the most dangerous and deadly pest of many palm trees, and there have been reports of its recent detection in France, Greece and Italy. At present, emphasis is on the development of integrated pest management based on biological control rather than on chemical insecticides, however the success of both systems is often insufficient. In this regard, RPW appears to be one pest that is very difficult to control. Thus inves- tigations into the natural defences of this curculionid are advisable. RPW hemocytes, the main immuno- competent cells in the insect, are described for the first time. We identifie…

HemocytesRed Palm Weevil Infection Insect immunity Hemolymph Biological controlBacillus thuringiensisBiological pest controlSettore BIO/05 - ZoologiaSaccharomyces cerevisiaeBiologyMicrobiologyPhagocytosisHemolymphBacillus thuringiensisBotanyHemolymphAnimalsPest Control BiologicalEcology Evolution Behavior and SystematicsLarvaWeevilfungibiology.organism_classificationBlood Cell CountBiopesticideRhynchophorusSettore AGR/11 - Entomologia Generale E ApplicataLarvaHost-Pathogen InteractionsWeevilsPEST analysis
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Mutational analysis of the cysteine residues in the hepatitis B virus small envelope protein.

1993

The small envelope protein of hepatitis B virus is the major component of the viral coat and is also secreted from cells as a 20-nm subviral particle, even in the absence of other viral proteins. Such empty envelope particles are composed of approximately 100 copies of this polypeptide and host-derived lipids and are stabilized by extensive intermolecular disulfide cross-linking. To study the contribution of disulfide bonds to assembly and secretion of the viral envelope, single and multiple mutants involving all 14 cysteines in HepG2 and COS-7 cells were analyzed. Of the six cysteines located outside the region carrying the surface antigen, Cys-48, Cys-65, and Cys-69 were each found to be …

Hepatitis B virusCarcinoma HepatocellularImmunologyMolecular Sequence DataBiologyEndoplasmic ReticulumTransfectionMicrobiologyProtein Structure SecondaryCell LineSerineProtein structureVirus-like particleViral envelopeViral Envelope ProteinsVirologyTumor Cells CulturedAnimalsHumansAmino Acid SequenceCysteinePeptide sequenceGel electrophoresisBase SequenceEndoplasmic reticulumLiver NeoplasmsOligonucleotides AntisenseMolecular biologyRecombinant ProteinsBiochemistryInsect ScienceMutagenesis Site-DirectedCysteineResearch Article
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Deletions in the hepatitis B virus small envelope protein: effect on assembly and secretion of surface antigen particles

1992

The small envelope S protein of hepatitis B virus carrying the surface antigen has the unique property of mobilizing cellular lipids into empty envelope particles which are secreted from mammalian cells. We studied the biogenesis of such particles using site-directed mutagenesis. In this study, we describe the effect of deletions in the N-terminal hydrophobic and hydrophilic domains of the S protein. Whereas short overlapping deletions of hydrophilic sequences flanking the first hydrophobic domain were tolerated, larger deletions of the same sequences were not. Conversely, the hydrophilic region preceding the second hydrophobic domain was not permissive for even short deletions. Deletion of…

Hepatitis B virusMolecular Sequence DataImmunologyMutantMutagenesis (molecular biology technique)Biologymedicine.disease_causeMicrobiologyViral Envelope ProteinsViral envelopeVirologymedicineInterleukin 9SecretionCloning MolecularCells CulturedSecretory pathwayMutationHepatitis B Surface AntigensBase SequenceTunicamycinEndoplasmic reticulumPrecipitin TestsMolecular biologyInsect ScienceMutagenesis Site-DirectedChromosome DeletionPlasmidsResearch ArticleJournal of Virology
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Hepatitis B virus maturation is sensitive to functional inhibition of ESCRT-III, Vps4, and gamma 2-adaptin.

2007

ABSTRACT Hepatitis B virus (HBV) is an enveloped DNA virus that presumably buds at intracellular membranes of infected cells. HBV budding involves two endocytic host proteins, the ubiquitin-interacting adaptor γ2-adaptin and the Nedd4 ubiquitin ligase. Here, we demonstrate that HBV release also requires the cellular machinery that generates internal vesicles of multivesicular bodies (MVBs). In order to perturb the MVB machinery in HBV-replicating liver cells, we used ectopic expression of dominant-negative mutants of different MVB components, like the ESCRT-III complex-forming CHMP proteins and the Vps4 ATPases. Upon coexpression of mutated CHMP3, CHMP4B, or CHMP4C forms, as well as of ATPa…

Hepatitis B virusVacuolar Proton-Translocating ATPasesEndosomeImmunologyEndocytic cycleVesicular Transport Proteinsmacromolecular substancesEndosomesmedicine.disease_causeMicrobiologyESCRTVirusCell LineViral ProteinsVirologymedicineHumansAdaptor Protein Complex gamma SubunitsHepatitis B virusAdenosine TriphosphatasesMicroscopy ConfocalbiologyEndosomal Sorting Complexes Required for TransportVirus AssemblyDNA virusMolecular biologyUbiquitin ligaseCell biologyGenome Replication and Regulation of Viral Gene ExpressionMicroscopy FluorescenceInsect Sciencebiology.proteinHepatocytesATPases Associated with Diverse Cellular ActivitiesEctopic expressionJournal of virology
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Hepatitis B Virus Large Envelope Protein Interacts with γ2-Adaptin, a Clathrin Adaptor-Related Protein

2001

ABSTRACT For the outcome of a hepatitis B virus (HBV) infection, the viral L envelope protein with its pre-S domain performs pivotal functions by mediating attachment of HBV to liver cells, envelopment of viral capsids, release of (sub)viral particles, regulation of supercoiled DNA amplification, and transcriptional transactivation. To assess its multiple functions and host-protein assistance involved, we initiated a two-hybrid screen using the L-specific pre-S1 domain as bait. With this approach, we have identified γ2-adaptin, a putative member of the clathrin adaptor proteins responsible for protein sorting and trafficking, as a specific binding partner of L protein. Evidence for a physic…

Hepatitis B virusVesicle-associated membrane protein 8ImmunoprecipitationImmunologyGolgi ApparatusTransfectionmedicine.disease_causeMicrobiologyClathrinChromatography AffinityCytosolViral Envelope ProteinsMutant proteinYeastsVirologyProtein targetingmedicineAnimalsBinding siteAdaptor Protein Complex gamma SubunitsBinding SitesbiologyMembrane ProteinsPrecipitin TestsClathrinTransmembrane proteinVirus-Cell InteractionsCell biologyInsect ScienceCOS CellsMutationbiology.proteinClathrin adaptor proteinsProtein BindingJournal of Virology
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Myristylation is involved in intracellular retention of hepatitis B virus envelope proteins

1991

The envelope of hepatitis B virus contains three related proteins, one of which is myristylated. The nonmyristylated small and middle protein are assembled into empty envelope particles which are secreted from cells, whereas the myristylated large envelope protein is mainly found in complete virions and is not secreted in the absence of the nucleocapsid. The block to secretion can be partially overcome by mutation or deletion of the myristylation site. Creation of a myristyl attachment site in the small protein impairs the secretion of empty envelope particles but not their intracellular assembly. Myristylation may therefore play a crucial role in hepatitis B virus replication by channeling…

Hepatitis B virusvirusesDNA Mutational AnalysisImmunologyIn Vitro TechniquesBiologyVirus Replicationmedicine.disease_causeMyristic AcidMicrobiologyVirusStructure-Activity RelationshipCapsidViral Envelope ProteinsViral envelopeVirologymedicineHumansSecretionProtein PrecursorsHepatitis B virusMutationHepatitis B Surface Antigensbiology.organism_classificationVirologyCell CompartmentationMolecular WeightCapsidHepadnaviridaeViral replicationInsect ScienceMyristic AcidsProtein Processing Post-TranslationalResearch ArticleJournal of Virology
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