Search results for "Protein Domains"

showing 10 items of 78 documents

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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Blattella germanica displays a large arsenal of antimicrobial peptide genes

2020

Defence systems against microbial pathogens are present in most living beings. The German cockroach Blattella germanica requires these systems to adapt to unhealthy environments with abundance of pathogenic microbes, in addition to potentially control its symbiotic systems. To handle this situation, four antimicrobial gene families (defensins, termicins, drosomycins and attacins) were expanded in its genome. Remarkably, a new gene family (blattellicins) emerged recently after duplication and fast evolution of an attacin gene, which is now encoding larger proteins with the presence of a long stretch of glutamines and glutamic acids. Phylogenetic reconstruction, within Blattellinae, suggests …

0106 biological sciences0301 basic medicinePore Forming Cytotoxic ProteinsGenome InsectEvolutionary biology010603 evolutionary biology01 natural sciencesGenomeArticle03 medical and health sciencesProtein DomainsPhylogeneticsGene duplicationGene expressionGene familyAnimalsAmino Acid SequenceSymbiosisGenePhylogenyRegulation of gene expressionGeneticsGerman cockroachMultidisciplinarybiologyAntimicrobial responsesBlattellidaebiology.organism_classificationGenome evolution030104 developmental biologyGene Expression RegulationEntomology
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The IM30/Vipp1 C-terminus associates with the lipid bilayer and modulates membrane fusion.

2017

IM30/Vipp1 proteins are crucial for thylakoid membrane biogenesis in chloroplasts and cyanobacteria. A characteristic C-terminal extension distinguishes these proteins from the homologous bacterial PspA proteins, and this extension has been discussed to be key for the IM30/Vipp1 activity. Here we report that the extension of the Synechocystis IM30 protein is indispensable, and argue that both, the N-terminal PspA-domain as well as the C-terminal extension are needed in order for the IM30 protein to conduct its in vivo function. In vitro, we show that the PspA-domain of IM30 is vital for stability/folding and oligomer formation of IM30 as well as for IM30-triggered membrane fusion. In contra…

0106 biological sciences0301 basic medicineVesicle-associated membrane protein 8ChloroplastsLipid BilayersBiophysicsBiology01 natural sciencesBiochemistryMembrane FusionThylakoidsArticle03 medical and health sciencesBacterial ProteinsProtein DomainsIntegral membrane proteinMembranesMembrane transport proteinPeripheral membrane proteinSynechocystisLipid bilayer fusionMembrane ProteinsCell BiologyCell biology030104 developmental biologyMembrane proteinMembrane biogenesisbiology.protein010606 plant biology & botanyMembrane Fusion ActivityProtein BindingBiochimica et biophysica acta. Bioenergetics
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NMR Investigation of Structures of G-Protein Coupled Receptor Folding Intermediates

2016

Folding of G-protein coupled receptors (GPCRs) according to the two-stage model (Popot, J. L., and Engelman, D. M. (1990) Biochemistry 29, 4031-4037) is postulated to proceed in 2 steps: partitioning of the polypeptide into the membrane followed by diffusion until native contacts are formed. Herein we investigate conformational preferences of fragments of the yeast Ste2p receptor using NMR. Constructs comprising the first, the first two, and the first three transmembrane (TM) segments, as well as a construct comprising TM1-TM2 covalently linked to TM7 were examined. We observed that the isolated TM1 does not form a stable helix nor does it integrate well into the micelle. TM1 is significant…

0301 basic medicine10120 Department of ChemistryBioquímicaSaccharomyces cerevisiae Proteins1303 BiochemistryProtein ConformationStereochemistrySaccharomyces cerevisiaeBiochemistryMicelleRessonància magnètica nuclear1307 Cell BiologyG03 medical and health sciencesprotein coupled receptorGPCRProtein Domains540 Chemistry1312 Molecular BiologyAmino Acid SequenceNuclear Magnetic Resonance BiomolecularMolecular BiologyMicellesG protein-coupled receptorSequence Homology Amino Acid030102 biochemistry & molecular biologyChemistryProteïnes de membranaFoldingCell BiologyTransloconPeptide FragmentsTransmembrane proteinNMRFolding (chemistry)Crystallography030104 developmental biologyStructural biology10036 Medical ClinicProtein Structure and FoldingReceptors Mating FactorHelixProtein folding
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Identification and Characterization of a Single High-Affinity Fatty Acid Binding Site in Human Serum Albumin.

2017

A single high-affinity fatty acid binding site in the important human transport protein serum albumin (HSA) is identified and characterized using an NBD (7-nitrobenz-2-oxa-1,3-diazol-4-yl)-C12 fatty acid. This ligand exhibits a 1:1 binding stoichiometry in its HSA complex with high site-specificity. The complex dissociation constant is determined by titration experiments as well as radioactive equilibrium dialysis. Competition experiments with the known HSA-binding drugs warfarin and ibuprofen confirm the new binding site to be different from Sudlow-sites I and II. These binding studies are extended to other albumin binders and fatty acid derivatives. Furthermore an X-ray crystal structure …

0301 basic medicineAzolesSerum albuminIbuprofenSerum Albumin HumanMolecular Dynamics Simulation010402 general chemistryCrystallography X-Ray01 natural sciencesCatalysis03 medical and health sciencesProtein DomainsFatty acid bindingmedicineFluorescence Resonance Energy TransferHumansBinding siteBovine serum albuminNitrobenzeneschemistry.chemical_classificationBinding SitesbiologyChemistry010405 organic chemistryFatty AcidsFatty acidGeneral ChemistryGeneral MedicineLigand (biochemistry)Human serum albumin0104 chemical sciencesbody regionsDissociation constant030104 developmental biologyBiochemistryembryonic structuresbiology.proteinWarfarinmedicine.drugProtein BindingAngewandte Chemie (International ed. in English)
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Role of pulmonary surfactant protein Sp-C dimerization on membrane fragmentation: An emergent mechanism involved in lung defense and homeostasis.

2020

Surfactant protein C (SP-C) is a protein present in the pulmonary surfactant system that is involved in the biophysical properties of this lipoprotein complex, but it also has a role in lung defense and homeostasis. In this article, we propose that the link between both functions could rely on the ability of SP-C to induce fragmentation of phospholipid membranes and generate small vesicles that serve as support to present different ligands to cells in the lungs. Our results using bimolecular fluorescence complementation and tunable resistive pulse sensing setups suggest that SP-C oligomerization could be the triggering event that causes membrane budding and nanovesiculation. As shown by flu…

0301 basic medicineBiophysicsBiochemistryCell Line03 medical and health sciencesBimolecular fluorescence complementation0302 clinical medicinePulmonary surfactantProtein DomainsHumansAmino Acid SequenceFragmentation (cell biology)Unilamellar LiposomesChemistryVesicleSurfactant protein CCell BiologyMembrane buddingFlow CytometryPulmonary Surfactant-Associated Protein CEndocytosisRecombinant ProteinsCell biology030104 developmental biology030228 respiratory systemMembrane proteinStructural biologyMicroscopy FluorescencePeptidomimeticsProtein MultimerizationDimerizationBiochimica et biophysica acta. Biomembranes
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Dual Constant Domain-Fab: A novel strategy to improve half-life and potency of a Met therapeutic antibody

2016

The kinase receptor encoded by the Met oncogene is a sensible target for cancer therapy. The chimeric monovalent Fab fragment of the DN30 monoclonal antibody (MvDN30) has an odd mechanism of action, based on cell surface removal of Met via activation of specific plasma membrane proteases. However, the short half-life of the Fab, due to its low molecular weight, is a severe limitation for the deployment in therapy. This issue was addressed by increasing the Fab molecular weight above the glomerular filtration threshold through the duplication of the constant domains, in tandem (DCD-1) or reciprocally swapped (DCD-2). The two newly engineered molecules showed biochemical properties comparable…

0301 basic medicineCancer ResearchMice SCIDCancer targeted therapy0302 clinical medicineMice Inbred NODEpidermal growth factor receptorPhosphorylationbiologyChemistryImmunoglobulin Fab FragmentsAntibodies MonoclonalGeneral MedicineArticlesProto-Oncogene Proteins c-metHalf-lifeCell biologyOncology030220 oncology & carcinogenesisColonic NeoplasmsMetMolecular MedicineFemalemedicine.symptomSignal transductionAntibodySignal Transductionmedicine.drug_classColonAntibody; Cancer targeted therapy; Fab; Half-life; Met; Protein engineering; Cancer Research; Genetics; Molecular MedicineAntineoplastic AgentsMonoclonal antibody03 medical and health sciencesImmunoglobulin Fab FragmentsProtein DomainsCell Line TumormedicineGeneticsAnimalsHumansFabAntibodyCell growthMolecular biology030104 developmental biologyHEK293 CellsMechanism of actionHepatocyte Growth Factor ReceptorA549 Cellsbiology.proteinProtein engineering
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The secreted protein acidic and rich in cysteine is a critical mediator of cell death program induced by WIN/TRAIL combined treatment in osteosarcoma…

2015

Abstract Secreted protein acidic and rich in cysteine (SPARC) is a multi-functional protein which modulates cell-cell and cell-matrix interactions. In cancer cells, SPARC behaves as a tumor promoter in a number of tumors, but it can also act as a tumor suppressor factor. Our previous results showed that the synthetic cannabinoid WIN55,212-2 (WIN), a potent cannabinoid receptor agonist, is able to sensitize osteosarcoma MG63 cells to TNF-related apoptosis-inducing ligand (TRAIL)-induced apoptosis which is accompanied with endoplasmic reticulum (ER)-stress induction and the increase in autophagic markers. In the present investigation, we studied the role of SPARC in WIN/TRAIL-induced apoptosi…

0301 basic medicineCancer ResearchProgrammed cell deathCell SurvivalMorpholinesCellSPARC cannabinoids osteosarcoma apoptosis caspase-8 activationApoptosisBone NeoplasmsBiologyNaphthalenesTNF-Related Apoptosis-Inducing Ligand03 medical and health sciences0302 clinical medicineProtein DomainsSettore BIO/10 - BiochimicaCell Line TumormedicineCytotoxic T cellHumansOsteonectinGene SilencingCaspase 8OsteosarcomaOncogeneCell DeathEndoplasmic reticulumCell MembraneCell cycleEndoplasmic Reticulum StressCell biologyBenzoxazines030104 developmental biologymedicine.anatomical_structureOncologyApoptosis030220 oncology & carcinogenesisCancer cellRNA InterferenceInternational journal of oncology
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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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The Stalk Domain of NKp30 Contributes to Ligand Binding and Signaling of a Preassembled NKp30-CD3ζ Complex

2016

The natural cytotoxicity receptor (NCR) NKp30 (CD337) is a key player for NK cell immunosurveillance of infections and cancer. The molecular details of ligand recognition and its connection to CD3ζ signaling remain unsolved. Here, we show that the stalk domain (129KEHPQLGAGTVLLLR143) of NKp30 is very sensitive to sequence alterations, as mutations lead to impaired ligand binding and/or signaling capacity. Surprisingly, the stalk domains of NKp30 and NKp46, another NCR employing CD3ζ for signaling, were not exchangeable without drastic deficiencies in folding, plasma membrane targeting, and/or ligand-induced receptor signaling. Further mutational studies, N-glycosylation mapping, and plasma …

0301 basic medicineCell signalingCD3 ComplexImmunologyProtein domainBiologyCD3 ComplexBiochemistryCell membraneMice03 medical and health sciencesProtein DomainsCell surface receptormedicineAnimalsHumansMolecular BiologyNatural Cytotoxicity Triggering Receptor 3Natural Cytotoxicity Triggering Receptor 1Cell MembraneCell BiologyLigand (biochemistry)Cell biology030104 developmental biologymedicine.anatomical_structureMembrane proteinBiochemistrySignal transductionHeLa CellsSignal TransductionJournal of Biological Chemistry
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