Search results for "viral protein"

showing 10 items of 182 documents

Revisiting the cysteine-rich proteins encoded in the 3’-proximal open reading frame of the positive-sense single-stranded RNA of some monopartite fil…

2020

A reexamination of proteins with conserved cysteines and basic amino acids encoded by the 3 '-proximal gene of the positive-sense single-stranded RNA of some monopartite filamentous plant viruses has been carried out. The cysteines are involved in a putative Zn-finger domain, which, together with the basic amino acids, form part of the nuclear or nucleolar localization signals. An in-depth study of one of these proteins, p15 from grapevine B virus (GVB), has shown: (i) a three-dimensional structure with four alpha-helices predicted by two independent in silico approaches, (ii) the nucleolus as the main accumulation site by applying confocal laser microscopy to a fusion between p15 and the g…

Models MolecularProtein Conformation alpha-HelicalGrapevine virus BAgroinfiltrationEvolutionProtein ConformationProtein DomainProtein domainNicotiana benthamianaGene ExpressionBiologyEvolution MolecularOpen Reading Frames03 medical and health sciencesViral ProteinsProtein DomainsPlant CellsVirologyTobaccoGene expressionAmino Acid SequenceCloning MolecularGenePhylogeny030304 developmental biologyGenetics0303 health sciencesSequence Homology Amino Acid030306 microbiologyRNASettore AGR/12 - Patologia VegetaleGeneral Medicinebiology.organism_classificationVirologyRecombinant ProteinsPlant LeavesRNA silencingRNA ViralFlexiviridaeSequence AlignmentModel
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Bacteriophage P23-77 capsid protein structures reveal the archetype of an ancient branch from a major virus lineage.

2013

Summary It has proved difficult to classify viruses unless they are closely related since their rapid evolution hinders detection of remote evolutionary relationships in their genetic sequences. However, structure varies more slowly than sequence, allowing deeper evolutionary relationships to be detected. Bacteriophage P23-77 is an example of a newly identified viral lineage, with members inhabiting extreme environments. We have solved multiple crystal structures of the major capsid proteins VP16 and VP17 of bacteriophage P23-77. They fit the 14 Å resolution cryo-electron microscopy reconstruction of the entire virus exquisitely well, allowing us to propose a model for both the capsid archi…

Models MolecularProtein ConformationViral proteinLineage (evolution)virusesCrystallography X-Raymedicine.disease_causeArticleVirusViral AssemblyBacteriophage03 medical and health sciencesProtein structureStructural BiologymedicineBacteriophagesMolecular Biology030304 developmental biologySequence (medicine)0303 health sciencesbiology030306 microbiologyCryoelectron Microscopyta1183ta1182biology.organism_classificationVirology3. Good healthCapsidEvolutionary biologyCapsid ProteinsCrystallizationStructure (London, England : 1993)
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Cis autocatalytic cleavage of glycine-linked Zika virus NS2B-NS3 protease constructs.

2019

The flaviviral heterodimeric serine protease NS2B-NS3, consisting of the NS3 protease domain and the NS2B co-factor, is essential for ZIKA virus maturation and replication in cells. For in vitro studies a 'linked' construct, where a polyglycine linker connects NS2BCF and NS3pro , is often used. This construct undergoes autocatalytic cleavage. Here, we show that linked ZIKV NS2BCF -NS3pro is cleaved in cis in the NS2BCF exclusively at position R95 and not at the previously proposed alternate cleavage site at residue R29 in the NS3pro . Cleavage neither affects protease stability nor activity, despite some observed differences in spectroscopic behavior. This minimally modified construct may t…

Models MolecularProtein Conformationmedicine.medical_treatmentBiophysicsViral Nonstructural ProteinsCleavage (embryo)ArginineVirus ReplicationBiochemistryCatalysisZika virus03 medical and health sciencesViral ProteinsStructural BiologyGeneticsmedicineHomeostasisMolecular Biology030304 developmental biologySerine protease0303 health sciencesNS3ProteasebiologyChemistryCircular Dichroism030302 biochemistry & molecular biologySerine EndopeptidasesCell BiologyZika Virusbiology.organism_classificationIn vitroRecombinant ProteinsFlavivirusSpectrometry FluorescenceBiochemistrybiology.proteinProtein MultimerizationPeptidesLinkerPeptide HydrolasesFEBS lettersReferences
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Atomic structure of the major capsid protein of rotavirus: implications for the architecture of the virion

2001

The structural protein VP6 of rotavirus, an important pathogen responsible for severe gastroenteritis in children, forms the middle layer in the triple-layered viral capsid. Here we present the crystal structure of VP6 determined to 2 A resolution and describe its interactions with other capsid proteins by fitting the atomic model into electron cryomicroscopic reconstructions of viral particles. VP6, which forms a tight trimer, has two distinct domains: a distal beta-barrel domain and a proximal alpha-helical domain, which interact with the outer and inner layer of the virion, respectively. The overall fold is similar to that of protein VP7 from bluetongue virus, with the subunits wrapping …

Models MolecularRotavirusCations DivalentViral proteinvirusesMolecular Sequence DataHemagglutinins ViralTrimerCrystal structureBiologyCrystallography X-Raymedicine.disease_causeProtein Structure SecondaryArticleGeneral Biochemistry Genetics and Molecular BiologyVirus03 medical and health sciencesCapsidRotavirusAtomic modelmedicineAnimalsAmino Acid SequenceAntigens ViralMolecular BiologyPeptide sequence030304 developmental biology0303 health sciencesSequence Homology Amino AcidGeneral Immunology and Microbiology030306 microbiologyViral Core ProteinsGeneral NeuroscienceVirionvirus diseasesMolecular biologyZincCapsidSolventsBiophysicsCapsid ProteinsCattleThe EMBO Journal
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Insights into virus evolution and membrane biogenesis from the structure of the marine lipid-containing bacteriophage PM2.

2008

Recent, primarily structural observations indicate that related viruses, harboring no sequence similarity, infect hosts of different domains of life. One such clade of viruses, defined by common capsid architecture and coat protein fold, is the so-called PRD1-adenovirus lineage. Here we report the structure of the marine lipid-containing bacteriophage PM2 determined by crystallographic analyses of the entire approximately 45 MDa virion and of the outer coat proteins P1 and P2, revealing PM2 to be a primeval member of the PRD1-adenovirus lineage with an icosahedral shell and canonical double beta barrel major coat protein. The view of the lipid bilayer, richly decorated with membrane protein…

Models MolecularViral proteinProtein ConformationvirusesMolecular Sequence DataBiologymedicine.disease_causeCrystallography X-Ray03 medical and health sciencesProtein structuremedicineLipid bilayerMolecular Biology030304 developmental biology0303 health sciences030306 microbiologyCorticoviridaeVirionCell BiologyVirologyBiological EvolutionLipidsCell biologyBeta barrelMembrane proteinCapsidViral evolutionMembrane biogenesisVirusesCalciumCapsid ProteinsMolecular cell
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Two Antigenic Peptides from Genes m123 and m164 of Murine Cytomegalovirus Quantitatively Dominate CD8 T-Cell Memory in the H-2 d Haplotype

2001

ABSTRACT The importance of CD8 T cells for the control of cytomegalovirus (CMV) infection has raised interest in the identification of immunogenic viral proteins as candidates for vaccination and cytoimmunotherapy. The final aim is to determine the viral “immunome” for any major histocompatibility complex class I molecule by antigenicity screening of proteome-derived peptides. For human CMV, there is a limitation to this approach: the T cells used as responder cells for peptide screening are usually memory cells that have undergone in vivo selection. On this basis, pUL83 (pp65) and pUL123 (IE1 or pp68 to -72) were classified as immunodominant proteins. It is an open question whether this li…

MuromegalovirusAdoptive cell transferAntigenicityImmunologyCD8-Positive T-LymphocytesBiologymedicine.disease_causeMajor histocompatibility complexMicrobiologyImmediate-Early ProteinsViral Matrix ProteinsMiceOpen Reading FramesViral ProteinsImmune systemVirologymedicineAnimalsCytotoxic T cellAntigens ViralMice Inbred BALB CH-2 AntigensCytomegalovirusHerpesviridae InfectionsPhosphoproteinsVirologyPeptide FragmentsHaplotypesInsect ScienceProteomeImmunologybiology.proteinPathogenesis and ImmunityFemaleImmunologic MemorySpleenCD8Journal of Virology
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The Putative Natural Killer Decoy Early Genem04(gp34) of Murine Cytomegalovirus Encodes an Antigenic Peptide Recognized by Protective Antiviral CD8 T…

2000

ABSTRACTSeveral early genes of murine cytomegalovirus (MCMV) encode proteins that mediate immune evasion by interference with the major histocompatibility complex class I (MHC-I) pathway of antigen presentation to cytolytic T lymphocytes (CTL). Specifically, them152gene product gp37/40 causes retention of MHC-I molecules in the endoplasmic reticulum (ER)-Golgi intermediate compartment. Lack of MHC-I on the cell surface should activate natural killer (NK) cells recognizing the “missing self.” The retention, however, is counteracted by them04early gene product gp34, which binds to folded MHC-I molecules in the ER and directs the complex to the cell surface. It was thus speculated that gp34 mi…

MuromegalovirusGenes ViralImmunologyAntigen presentationchemical and pharmacologic phenomenaGenome ViralCD8-Positive T-LymphocytesMajor histocompatibility complexMicrobiologyImmediate-Early ProteinsGene productMiceViral ProteinsImmune systemAntigenPeptide LibraryVirologyAnimalsCytotoxic T cellHistocompatibility Antigen H-2DAntigens ViralCells CulturedGlycoproteinsMice Inbred BALB CMembrane GlycoproteinsbiologyHistocompatibility Antigens Class IH-2 AntigensVirologyKiller Cells NaturalCTL*Insect Sciencebiology.proteinPathogenesis and ImmunityFemaleCarrier ProteinsPeptidesCD8T-Lymphocytes CytotoxicJournal of Virology
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Processing and Presentation of Murine Cytomegalovirus pORFm164-Derived Peptide in Fibroblasts in the Face of All Viral Immunosubversive Early Gene Fu…

2002

ABSTRACTCD8 T cells are the principal effector cells in the resolution of acute murine cytomegalovirus (mCMV) infection in host organs. This undoubted antiviral and protective in vivo function of CD8 T cells appeared to be inconsistent with immunosubversive strategies of the virus effected by early (E)-phase genesm04,m06, andm152. The so-called immune evasion proteins gp34, gp48, and gp37/40, respectively, were found to interfere with peptide presentation at different steps in the major histocompatibility complex (MHC) class I pathway of antigen processing and presentation in fibroblasts. Accordingly, they were proposed to prevent recognition and lysis of infected fibroblasts by cytolytic T…

MuromegalovirusImmunologyAntigen presentationMajor histocompatibility complexMicrobiologyImmediate-Early ProteinsMiceOpen Reading FramesViral ProteinsImmune systemAntigenVirologyMHC class IAnimalsCytotoxic T cellAntigens ViralGenes Immediate-EarlyCells CulturedAntigen PresentationMice Inbred BALB CMembrane GlycoproteinsbiologyAntigen processingFibroblastsVirologyPeptide FragmentsCTL*Insect Sciencebiology.proteinPathogenesis and ImmunityFemaleT-Lymphocytes CytotoxicJournal of Virology
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The Immune Evasion Paradox: Immunoevasins of Murine Cytomegalovirus Enhance Priming of CD8 T Cells by Preventing Negative Feedback Regulation▿

2008

ABSTRACTCytomegaloviruses express glycoproteins that interfere with antigen presentation to CD8 T cells. Although the molecular modes of action of these “immunoevasins” differ between cytomegalovirus species, the convergent biological outcome is an inhibition of the recognition of infected cells. In murine cytomegalovirus, m152/gp40 retains peptide-loaded major histocompatibility complex class I molecules in acis-Golgi compartment, m06/gp48 mediates their vesicular sorting for lysosomal degradation, and m04/gp34, although not an immunoevasin in its own right, appears to assist in the concerted action of all three molecules. Using the Ld-restricted IE1 epitope YPHFMPTNL in the BALB/c mouse m…

MuromegalovirusImmunologyAntigen presentationPriming (immunology)Genome ViralBiologyCD8-Positive T-LymphocytesMajor histocompatibility complexVirus ReplicationMicrobiologyEpitopeImmediate early proteinImmediate-Early ProteinsEpitopesMiceViral ProteinsImmune systemAntigenVirologyCytotoxic T cellAnimalsAntigen PresentationMice Inbred BALB CHerpesviridae InfectionsKiller Cells NaturalInsect ScienceImmunologybiology.proteinPathogenesis and ImmunityFemaleLymph NodesImmunologic MemorySpleen
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Cytomegalovirus Encodes a Positive Regulator of Antigen Presentation

2006

ABSTRACT Murine cytomegalovirus encodes three regulators of antigen presentation to antiviral CD8 T cells. According to current paradigms, all three regulators are committed to the inhibition of the presentation of antigenic peptides. Whereas m152/gp40 catalyzes the retention of peptide-loaded major histocompatibility complex (MHC) class I molecules in a cis -Golgi compartment, m06/gp48 binds stably to class I molecules and directs them into the cellular cargo-sorting pathway of lysosomal degradation. Regulator m04/gp34 also binds stably to class I molecules, but unlike m152 and m06, it does not downmodulate MHC class I cell surface expression. It has entered the literature as a direct inhi…

MuromegalovirusImmunologyAntigen presentationRegulatorCD8-Positive T-LymphocytesVirus ReplicationMajor histocompatibility complexMicrobiologyMiceViral ProteinsMuromegalovirusAntigenVirologyMHC class IAnimalsHumansCytotoxic T cellAntigens ViralCells CulturedGlycoproteinsAntigen PresentationMice Inbred BALB CMembrane GlycoproteinsbiologyAntigen processingHistocompatibility Antigens Class IH-2 AntigensFibroblastsEmbryo Mammalianbiology.organism_classificationAdoptive TransferMolecular biologyMice Inbred C57BLInsect ScienceCytomegalovirus Infectionsbiology.proteinPathogenesis and ImmunityFemaleCarrier ProteinsPeptidesT-Lymphocytes CytotoxicJournal of Virology
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