Search results for "Lipid bilayer fusion"

showing 10 items of 30 documents

Mg2+ binding triggers rearrangement of the IM30 ring structure, resulting in augmented exposure of hydrophobic surfaces competent for membrane binding

2018

The "inner membrane-associated protein of 30 kDa" (IM30), also known as "vesicle-inducing protein in plastids 1" (Vipp1), is found in the majority of photosynthetic organisms that use oxygen as an energy source, and its occurrence appears to be coupled to the existence of thylakoid membranes in cyanobacteria and chloroplasts. IM30 is most likely involved in thylakoid membrane biogenesis and/or maintenance, and has recently been shown to function as a membrane fusion protein in presence of Mg2+ However, the precise role of Mg2+ in this process and its impact on the structure and function of IM30 remains unknown. Here, we show that Mg2+ binds directly to IM30 with a binding affinity of ∼1 mm …

0301 basic medicineMembrane fusion proteinChemistryPspALipid bilayer fusionIsothermal titration calorimetryMg2+Cell BiologyBiochemistry[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry03 medical and health sciences030104 developmental biologyThylakoidMembrane biogenesisBiophysicsFourier transform IREnergy sourceMolecular BiologyMembrane biophysicsIM30BiogenesisJournal of Biological Chemistry
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Vesicle transport and photoreceptor death: fishing for molecular links.

2013

Intracellular vesicle transport defects can induce retinal degeneration and photoreceptor cell death, but the molecular connections between these processes remains poorly understood. Reporting in Developmental Cell, Nishiwaki et al. (2013) suggest that a vesicle fusion cis-SNARE complex component translates vesicular transport defects into photoreceptor cell apoptosis.

Retinal degenerationVesicle fusionLipid bilayer fusionIntracellular vesicleApoptosisCell BiologyBiologymedicine.diseaseMembrane FusionGeneral Biochemistry Genetics and Molecular BiologyPhotoreceptor cellCell biologyVesicular transport proteinSoluble N-Ethylmaleimide-Sensitive Factor Attachment Proteinsmedicine.anatomical_structureProto-Oncogene Proteins c-bcl-2ApoptosismedicineRetinal Cone Photoreceptor CellsAnimalsMolecular BiologyDevelopmental BiologyDevelopmental cell
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A Bimolecular Multicellular Complementation System for the Detection of Syncytium Formation: A New Methodology for the Identification of Nipah Virus …

2019

Fusion of viral and cellular membranes is a key step during the viral life cycle. Enveloped viruses trigger this process by means of specialized viral proteins expressed on their surface, the so-called viral fusion proteins. There are multiple assays to analyze the viral entry including those that focus on the cell-cell fusion induced by some viral proteins. These methods often rely on the identification of multinucleated cells (syncytium) as a result of cell membrane fusions. In this manuscript, we describe a novel methodology for the study of cell-cell fusion. Our approach, named Bimolecular Multicellular Complementation (BiMuC), provides an adjustable platform to qualitatively and quanti…

0301 basic medicinevirusesmembrane fusionlcsh:QR1-502virusNipah virusBiologyGiant Cells01 natural scienceslcsh:MicrobiologySmall Molecule Libraries03 medical and health sciencesVirus entryViral envelopeViral life cycleViral entryVirologyDrug DiscoveryHumansSyncytiumDrug discoveryBrief ReportbiomolèculesHigh-throughput screeningLipid bilayer fusionVirus InternalizationFusion proteinHigh-Throughput Screening Assays0104 chemical sciencesCell biologyBimolecular complementation010404 medicinal & biomolecular chemistryMulticellular organismHEK293 Cells030104 developmental biologyInfectious DiseasesViruses
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IM30 triggers membrane fusion in cyanobacteria and chloroplasts

2015

The thylakoid membrane of chloroplasts and cyanobacteria is a unique internal membrane system harbouring the complexes of the photosynthetic electron transfer chain. Despite their apparent importance, little is known about the biogenesis and maintenance of thylakoid membranes. Although membrane fusion events are essential for the formation of thylakoid membranes, proteins involved in membrane fusion have yet to be identified in photosynthetic cells or organelles. Here we show that IM30, a conserved chloroplast and cyanobacterial protein of approximately 30 kDa binds as an oligomeric ring in a well-defined geometry specifically to membranes containing anionic lipids. Triggered by Mg2+, membr…

ChloroplastsGeneral Physics and AstronomyBiologyMembrane FusionThylakoidsGeneral Biochemistry Genetics and Molecular BiologyBacterial ProteinsCentrifugation Density GradientIntegral membrane proteinMultidisciplinaryGalactolipidsPeripheral membrane proteinSynechocystisLipid bilayer fusionfood and beveragesPhosphatidylglycerolsGeneral ChemistryTransmembrane proteinCell biologyChloroplastMembraneThylakoidLiposomesQuantasomeGlycolipidsProtein BindingNature Communications
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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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Intracellular route of canine parvovirus entry.

1998

ABSTRACT The present study was designed to investigate the endocytic pathway involved in canine parvovirus (CPV) infection. Reduced temperature (18°C) or the microtubule-depolymerizing drug nocodazole was found to inhibit productive infection of canine A72 cells by CPV and caused CPV to be retained in cytoplasmic vesicles as indicated by immunofluorescence microscopy. Consistent with previously published results, these data indicate that CPV enters a host cell via an endocytic route and further suggest that microtubule-dependent delivery of CPV to late endosomes is required for productive infection. Cytoplasmic microinjection of CPV particles was used to circumvent the endocytosis and membr…

CytoplasmMicroinjectionsParvovirus CanineEndosomeanimal diseasesvirusesImmunologyEndocytic cycleBiologyVirus ReplicationEndocytosisMicrotubulesMicrobiologyCell LineDogsVirologyAnimalsMicroinjectionParvovirusNocodazoleTemperatureCanine parvovirusLipid bilayer fusionbiology.organism_classificationVirologyEndocytosisVirus-Cell InteractionsMicroscopy FluorescenceViral replicationInsect Science
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Occlusion-derived baculovirus: interaction with human cells and evaluation of the envelope protein P74 as a surface display platform.

2008

To develop complementary baculovirus-based tools for gene delivery and display technologies, the interaction of occlusion-derived baculovirus (ODV) with human cells, and the functionality of the P74 ODV envelope protein for display of the IgG-binding Z domains (ZZP74) were evaluated. The cellular binding of ODV was concentration-dependent and saturable. Only minority of the bound virions were internalized at both 37 and 4 degrees C, suggesting usage of direct membrane fusion as the entry mode. The intracellular transport of ODV was confined in vesicular structures peripheral to the plasma membrane, impeding subsequent nuclear entry and transgene expression. Transduction of ODV was not rescu…

virusesBlotting WesternVirus AttachmentBioengineeringBiologyGene deliverySpodopteraApplied Microbiology and BiotechnologyCell Linechemistry.chemical_compoundTransduction (genetics)Viral envelopeMicroscopy Electron TransmissionViral Envelope ProteinsCell Line TumorAnimalsHumansMicroscopy ConfocalfungiLipid bilayer fusionSodium butyrateGeneral MedicineMolecular biologyFusion proteinCell biologyNocodazolechemistryCell cultureElectrophoresis Polyacrylamide GelBaculoviridaeBiotechnologyJournal of biotechnology
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Direct Visualization of the Conformational Dynamics of Single Influenza Hemagglutinin Trimers

2018

Influenza hemagglutinin (HA) is the canonical type I viral envelope glycoprotein and provides a template for the membrane-fusion mechanisms of numerous viruses. The current model of HA-mediated membrane fusion describes a static "spring-loaded" fusion domain (HA2) at neutral pH. Acidic pH triggers a singular irreversible conformational rearrangement in HA2 that fuses viral and cellular membranes. Here, using single-molecule Förster resonance energy transfer (smFRET)-imaging, we directly visualized pH-triggered conformational changes of HA trimers on the viral surface. Our analyses reveal reversible exchange between the pre-fusion and two intermediate conformations of HA2. Acidification of p…

0301 basic medicineProtein ConformationHemagglutinin (influenza)Hemagglutinin Glycoproteins Influenza VirusBiologyArticleGeneral Biochemistry Genetics and Molecular BiologyReaction coordinate03 medical and health sciencesViral envelopeInfluenza HumanFluorescence Resonance Energy TransferHumansDynamic equilibriumFusionCell MembraneLipid bilayer fusionHydrogen-Ion ConcentrationVirus InternalizationSingle Molecule ImagingHEK293 CellsHemagglutinins030104 developmental biologyMembraneFörster resonance energy transferA549 CellsInfluenza A virusBiophysicsbiology.proteinProtein BindingCell
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Stability of Asymmetric Lipid Bilayers Assessed by Molecular Dynamics Simulations

2009

The asymmetric insertion of amphiphiles into biological membranes compromises the balance between the inner and outer monolayers. As a result, area expansion of the receiving leaflet and curvature strain may lead to membrane permeation, shape changes, or membrane fusion events. We have conducted both atomistic and coarse-grained molecular dynamics simulations of dipalmitoyl-phosphatidylcholine (DPPC) bilayers to study the effect of an asymmetric distribution of lipids between the two monolayers on membrane stability. Highly asymmetric lipid bilayers were found to be surprisingly stable within the submicrosecond time span of the simulations. Even the limiting case of a monolayer immersed in …

12-DipalmitoylphosphatidylcholineLipid BilayersBiochemistryCatalysisColloid and Surface ChemistryCOARSE-GRAINED MODELSHAPE TRANSFORMATIONSMonolayerComputer SimulationLipid bilayer phase behaviorLipid bilayerChemistryBilayerLipid bilayer fusionBiological membraneGeneral ChemistryLipid bilayer mechanicsANTIMICROBIAL PEPTIDESCrystallographyMembraneTRANSMEMBRANE DISTRIBUTIONEGG PHOSPHATIDYLCHOLINEPhosphatidylcholinesPORE FORMATIONBiophysicsPRESSURE PROFILESMECHANOSENSITIVE CHANNELlipids (amino acids peptides and proteins)OCTYL GLUCOSIDEPHOSPHOLIPID-BILAYERSJournal of the American Chemical Society
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Hexapeptides that interfere with HIV-1 fusion peptide activity in liposomes block GP41-mediated membrane fusion

2006

AbstractUpon receptor-mediated activation, the gp41 hydrophobic, conserved fusion peptide inserts into the target membrane and promotes the kind of perturbations required for the progression of the HIV-cell fusion reaction. Using a synthetic combinatorial library we have identified all d-amino acid hexapeptide sequences that inhibited the fusion peptide capacity of perturbing model membranes. Two hexapeptides that effectively inhibited the fusion peptide in these systems were subsequently shown to inhibit cell–cell fusion promoted by gp41 expressed at cell surfaces. These observations might be of importance for understanding the mechanisms underlying fusion peptide activity and suggest new …

CellBiophysicsMembrane fusionCHO CellsGp41BiochemistryFusion peptideMembranes (Biologia)Structural BiologyCricetinaeGeneticsmedicineNuclear fusionAnimalsMolecular BiologyFusion inhibitorFusionLiposomeChemistryLipid bilayer fusionViral fusionCell Biologygp41HIV Envelope Protein gp41Cell biologyMembranemedicine.anatomical_structureBiochemistryLiposomesHIV-1PèptidsPeptidesFusion peptide
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