Search results for "Movement proteins"

showing 10 items of 12 documents

In vivo detection, RNA-binding properties and characterization of the RNA-binding domain of the p7 putative movement protein from carnation mottle ca…

1999

Biochemical and structural characterization studies on the p7 putative movement protein from a Spanish isolate of carnation mottle carmovirus (CarMV) have been conducted. The CarMV p7 gene was fused to a sequence coding for a six-histidine tag and expressed in bacteria, allowing the purification of CarMV p7 and the production of a specific antiserum. This antiserum led to the immunological identification of CarMV p7 in infected leaf tissue from the experimental host Chenopodium quinoa. Putative nucleic acid-binding properties of the CarMV p7 have been explored and demonstrated with both electrophoretic mobility shift and RNA-protein blot in vitro assays using digoxigenin-labeled riboprobes.…

Binding SitesCarmovirusRecombinant Fusion ProteinsMolecular Sequence DataCooperative bindingRNARNA-Binding ProteinsBiologybiology.organism_classificationMolecular biologyPlant Viral Movement ProteinsViral ProteinsBiochemistryVirologyNucleic acidEscherichia coliCarmovirusAmino Acid SequenceMovement proteinPeptide sequenceGeneBinding domainVirology
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Insertion and Topology of a Plant Viral Movement Protein in the Endoplasmic Reticulum Membrane

2002

Virus-encoded movement proteins (MPs) mediate cell-to-cell spread of viral RNA through plant membranous intercellular connections, the plasmodesmata. The molecular pathway by which MPs interact with viral genomes and target plasmodesmata channels is largely unknown. The 9-kDa MP from carnation mottle carmovirus (CarMV) contains two potential transmembrane domains. To explore the possibility that this protein is in fact an intrinsic membrane protein, we have investigated its insertion into the endoplasmic reticulum membrane. By using in vitro translation in the presence of dog pancreas microsomes, we demonstrate that CarMV p9 inserts into the endoplasmic reticulum without the aid of any addi…

BioquímicaGlycosylationMolecular Sequence DataPlasmodesmaBiologyEndoplasmic ReticulumTopologyBiochemistryProtein Structure SecondaryViral ProteinsAmino Acid SequenceMolecular BiologyEndoplasmic reticulumCarmovirusProteïnes de membranaMembrane ProteinsSTIM1Translation (biology)Cell Biologybiology.organism_classificationVirusCell biologyPlant Viral Movement ProteinsTobacco Mosaic VirusTransmembrane domainCytoplasmMembrane topologyCarmovirusJournal of Biological Chemistry
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Double-spanning Plant Viral Movement Protein Integration into the Endoplasmic Reticulum Membrane Is Signal Recognition Particle-dependent, Translocon…

2005

The current model for cell-to-cell movement of plant viruses holds that transport requires virus-encoded movement proteins that intimately associate with endoplasmic reticulum membranes. We have examined the early stages of the integration into endoplasmic reticulum membranes of a double-spanning viral movement protein using photocross-linking. We have discovered that this process is cotranslational and proceeds in a signal recognition particle-dependent manner. In addition, nascent chain photocross-linking to Sec61alpha and translocating chain-associated membrane protein reveal that viral membrane protein insertion takes place via the translocon, as with most eukaryotic membrane proteins, …

BioquímicaSec61Vesicle-associated membrane protein 8Receptors PeptideLipid BilayersReceptors Cytoplasmic and NuclearBiologyEndoplasmic ReticulumBiochemistryViral ProteinsMembranes (Biologia)Escherichia coliMolecular BiologySignal recognition particle receptorSignal recognition particleMembrane GlycoproteinsEndoplasmic reticulumCalcium-Binding ProteinsMembrane ProteinsSTIM1Cell BiologyTransloconTransmembrane proteinCell biologyPlant Viral Movement ProteinsCross-Linking ReagentsMutagenesisRNA ViralCarmovirusSignal Recognition ParticleSEC Translocation Channels
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Membrane insertion and topology of the p7B movement protein of Melon Necrotic Spot Virus (MNSV)

2007

AbstractCell-to-cell movement of the Melon Necrotic Spot Virus (MNSV) is controlled by two small proteins working in trans, an RNA-binding protein (p7A) and an integral membrane protein (p7B) separated by an amber stop codon. p7B contains a single hydrophobic region. Membrane integration of this region was observed when inserted into model proteins in the presence of microsomal membranes. Furthermore, we explored the topology and targeting mechanisms of full-length p7B. Here we present evidence that p7B integrates in vitro into the ER membrane cotranslationally and with an Nt-cytoplasmic/Ct-luminal orientation. The observed topology was monitored in vivo by fusing GFP to the Ct of p7B, enab…

Green Fluorescent ProteinsPlant virusBiologyTopologyEndoplasmic ReticulumGreen fluorescent proteinViral ProteinsVirologyMovement proteinIntegral membrane proteinMelon necrotic spot virusEndoplasmic reticulumCarmovirusProteïnes de membranaMembrane Proteinsbiology.organism_classificationMembrane integrationMembrane protein topologyVirusPlant Viral Movement ProteinsMovement proteinsCucurbitaceaeMembraneMembrane proteinCarmovirusMNSVVirology
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Plant virus cell-to-cell movement is not dependent on the transmembrane disposition of its movement protein

2009

ABSTRACT The cell-to-cell transport of plant viruses depends on one or more virus-encoded movement proteins (MPs). Some MPs are integral membrane proteins that interact with the membrane of the endoplasmic reticulum, but a detailed understanding of the interaction between MPs and biological membranes has been lacking. The cell-to-cell movement of the Prunus necrotic ringspot virus (PNRSV) is facilitated by a single MP of the 30K superfamily. Here, using a myriad of biochemical and biophysical approaches, we show that the PNRSV MP contains only one hydrophobic region (HR) that interacts with the membrane interface, as opposed to being a transmembrane protein. We also show that a proline resi…

ImmunologyMolecular Sequence DataMicrobiologiaBiologyIlarvirusMicrobiologyCell membraneSequence Analysis ProteinVirologymedicineAmino Acid SequenceMovement proteinPeptide sequenceIntegral membrane proteinPhospholipidsEndoplasmic reticulumCircular DichroismCell MembraneProteïnes de membranaBiological membraneVirus InternalizationTransmembrane proteinCell biologyVirus-Cell InteractionsVirusPlant Viral Movement ProteinsMembranemedicine.anatomical_structureBiochemistryInsect ScienceMutationPrunusHydrophobic and Hydrophilic InteractionsSequence Alignment
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RNA-binding properties and membrane insertion of Melon necrotic spot virus (MNSV) double gene block movement proteins

2006

AbstractAdvances in structural and biochemical properties of carmovirus movement proteins (MPs) have only been obtained in p7 and p9 from Carnation mottle virus (CarMV). Alignment of carmovirus MPs revealed a low conservation of amino acid identity but interestingly, similarity was elevated in regions associated with the functional secondary structure elements reported for CarMV which were conserved in all studied proteins. Nevertheless, some differential features in relation with CarMV MPs were identified in those from Melon necrotic virus (MNSV) (p7A and p7B). p7A was a soluble non-sequence specific RNA-binding protein, but unlike CarMV p7, its central region alone could not account for t…

Molecular Sequence DataSequence alignmentBiologyMembranes (Biologia)VirologyAmino Acid SequencePeptide sequenceProtein secondary structureIntegral membrane proteinPlant DiseasesMelon necrotic spot virusCarmovirusProteïnes de membranaRNA-Binding ProteinsRNAbiology.organism_classificationRNA-binding domainVirusPlant Viral Movement ProteinsCucurbitaceaeMovement proteinsBiochemistryCarnation mottle virusMelon plantsCarmovirusMNSVMembrane insertionSequence AlignmentGene DeletionVirology
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Mutational analysis of the RNA-binding domain of the Prunus necrotic ringspot virus (PNRSV) movement protein reveals its requirement for cell-to-cell…

2005

AbstractThe movement protein (MP) of Prunus necrotic ringspot virus (PNRSV) is required for cell-to-cell movement. MP subcellular localization studies using a GFP fusion protein revealed highly punctate structures between neighboring cells, believed to represent plasmodesmata. Deletion of the RNA-binding domain (RBD) of PNRSV MP abolishes the cell-to-cell movement. A mutational analysis on this RBD was performed in order to identify in vivo the features that govern viral transport. Loss of positive charges prevented the cell-to-cell movement even though all mutants showed a similar accumulation level in protoplasts to those observed with the wild-type (wt) MP. Synthetic peptides representin…

MutantMolecular Sequence DataPlasmodesmaBiologyCircular dichroismIlarvirusGFPViral ProteinsVirologyMovement proteinTobaccoAmino Acid SequenceMovement proteinRNA binding domainProtein secondary structureProtoplastsRNABiological Transportbiology.organism_classificationSubcellular localizationSubcellular locationMolecular biologyVirusProtein Structure TertiaryPlant LeavesPlant Viral Movement ProteinsPrunus necrotic ringspot virusRNA ViralCell-to-cell movementPeptidesProteïnesPrunus necrotic ringspot virusBinding domainVirology
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Population genetics of cucumber mosaic virus infecting medicinal, aromatic and ornamental plants from northern Italy

2012

An epidemiological survey carried at the Herb Garden of Casola Valsenio (Emilia Romagna region; Northern Italy) from 2006 to 2009 resulted in finding Cucumber mosaic virus (CMV) as the infectious agent of several ornamental, medicinal and aromatic plants. All CMV-infected plant species showed leaf symptoms followed, in some cases, by flower colour-breaking and stunting. Genetic analysis consisted in the characterization of movement protein gene of each CMV-isolate by single strand polymorphism analysis and sequencing. Phylogenetic trees identified only two isolates as member of subgroup II, while all other isolates were part of subgroup IA. This survey confirms an unexpected increment of CM…

Nonsynonymous substitutionORNAMENTAL PLANTSMolecular Sequence DataPopulationPopulation geneticsBiologyGENETIC CHARACTERIZATIONCucumovirusNucleotide diversityCucumber mosaic virusVirologyGenetic variationBotanyCluster AnalysisSelection GeneticeducationPhylogenyGeneticseducation.field_of_studySequence Homology Amino AcidPhylogenetic treeCMVGenetic Variationfood and beveragesSettore AGR/12 - Patologia VegetaleSequence Analysis DNAGeneral MedicinePlantsPlant Viral Movement ProteinsGenetics PopulationAmino Acid SubstitutionItalyGenetic structureRNA ViralOFFICINAL PLANTSCMV Population genetics
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The ER-Membrane Transport System Is Critical for Intercellular Trafficking of the NSm Movement Protein and Tomato Spotted Wilt Tospovirus.

2015

Plant viruses move through plasmodesmata to infect new cells. The plant endoplasmic reticulum (ER) is interconnected among cells via the ER desmotubule in the plasmodesma across the cell wall, forming a continuous ER network throughout the entire plant. This ER continuity is unique to plants and has been postulated to serve as a platform for the intercellular trafficking of macromolecules. In the present study, the contribution of the plant ER membrane transport system to the intercellular trafficking of the NSm movement protein and Tomato spotted wilt tospovirus (TSWV) is investigated. We showed that TSWV NSm is physically associated with the ER membrane in Nicotiana benthamiana plants. An…

RNA viruses0301 basic medicineLeavesCell MembranesNicotiana benthamianaPlant ScienceEndoplasmic ReticulumPathology and Laboratory MedicineBiochemistrySolanum lycopersicumTospovirusBunyavirusesMedicine and Health SciencesArabidopsis thalianaMovement proteinBiology (General)Integral membrane proteinSecretory PathwaybiologyPlant BiochemistryPlant AnatomyPlasmodesmataProteïnes de membranafood and beveragesPlantsPlants Genetically ModifiedCell biologyTransport proteinPlant Viral Movement ProteinsProtein TransportMedical MicrobiologyCell ProcessesViral PathogensVirusesPathogensCellular Structures and OrganellesTomato Spotted Wilt VirusResearch ArticleBioquímicaCell PhysiologyQH301-705.5Arabidopsis ThalianaImmunologyPlant PathogensBrassicaPlasmodesmaResearch and Analysis MethodsMicrobiologyPlant Viral Pathogens03 medical and health sciencesModel OrganismsPlant and Algal ModelsVirologyTobaccoGeneticsIntegral Membrane ProteinsSecretionMicrobial PathogensMolecular BiologyPlant DiseasesBiology and life sciencesEndoplasmic reticulumfungiOrganismsMembrane ProteinsCell BiologyPlant PathologyRC581-607biology.organism_classificationVirosis (Plantes)VirologyPlant Leaves030104 developmental biologyMembrane TraffickingParasitologyImmunologic diseases. AllergyPLoS Pathogens
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The Tobacco mosaic virus movement protein associates with but does not integrate into biological membranes

2014

Plant positive-strand RNA viruses require association with plant cell endomembranes for viral translation and replication, as well as for intra- and intercellular movement of the viral progeny. The membrane association and RNA binding of the Tobacco mosaic virus (TMV) movement protein (MP) are vital for orchestrating the macromolecular network required for virus movement. A previously proposed topological model suggests that TMV MP is an integral membrane protein with two putative -helical transmembrane (TM) segments. Here we tested this model using an experimental system that measured the efficiency with which natural polypeptide segments were inserted into the ER membrane under conditions…

Recombinant Fusion ProteinsvirusesMolecular Sequence DataImmunologyGene ExpressionMicrobiologiaBiologyEndoplasmic ReticulumMicrobiologyCell membraneGenes ReporterPlant CellsVirologymedicineTobacco mosaic virusAmino Acid SequenceMovement proteinIntegral membrane proteinStructure and AssemblyCell MembraneViral translationfungifood and beveragesBiological membraneVirologyTransmembrane proteinTransport proteinCell biologyVirusPlant Viral Movement ProteinsTobacco Mosaic VirusProtein Transportmedicine.anatomical_structureInsect ScienceHydrophobic and Hydrophilic InteractionsProtein Binding
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