Search results for "viral protein"

showing 10 items of 182 documents

Longitudinal analysis of Mycobacterium tuberculosis 19-kDa antigen-specific T cells in patients with pulmonary tuberculosis: association with disease…

2003

CD8(+) T cells play a central role in immune protection against infection with Mycobacterium tuberculosis. One of the target epitopes for anti-M. tuberculosis directed CD8(+) T cells is the HLA-A2-restricted 19-kDa lipoprotein peptide VLTDGNPPEV. T cell clones directed against this epitope recognized not only the nominal peptide ligand, but also a closely related peptide (VPTDPNPPEV) from the HIV envelope gp120 (HIV(env) gp120) protein characterized by IFN-gamma release. This cross-reactivity was confirmed in ex vivo in M. tuberculosis 19-kDa tetramer-sorted T cells from patients with tuberculosis and in HIVgp120 tetramer-reactive T cells sorted from HIV(+) patients. M. tuberculosis 19-kDa …

TuberculosisHIV AntigensT cellImmunologyEpitopes T-LymphocyteHIV InfectionsCD146 AntigenBiologyCD8-Positive T-LymphocytesCross ReactionsHIV Envelope Protein gp120medicine.disease_causeEpitopeMycobacterium tuberculosisInterferon-gammaViral ProteinsAntigenBacterial ProteinsAntigens CDT-Lymphocyte SubsetsHLA-A2 AntigenmedicineImmunology and AllergyHumansTuberculosisLongitudinal StudiesNeural Cell Adhesion MoleculesAntigens BacterialMembrane GlycoproteinsMolecular MimicryGranulocyte-Macrophage Colony-Stimulating FactorT lymphocyteMycobacterium tuberculosisOncogene Proteins Viralmedicine.diseasebiology.organism_classificationVirologyPeptide FragmentsDNA-Binding ProteinsMolecular mimicrymedicine.anatomical_structureImmunologyInterleukin-4CD8BiomarkersEuropean journal of immunology
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Nucleotide sequence of a ssRNA phage from Acinetobacter: kinship to coliphages.

2002

The complete nucleotide sequence of ssRNA phage AP205 propagating in Acinetobacter species is reported. The RNA has three large ORFs, which code for the following homologues of the RNA coliphage proteins: the maturation, coat and replicase proteins. Their gene order is the same as that in coliphages. RNA coliphages or Leviviridae fall into two genera: the alloleviviruses, like Qβ, which have a coat read-through protein, and the leviviruses, like MS2, which do not have this coat protein extension. AP205 has no read-through protein and may therefore be classified as a levivirus. A major digression from the known leviviruses is the apparent absence of a lysis gene in AP205 at the usual positio…

Untranslated regionMolecular Sequence DataRNA-dependent RNA polymeraseGenome ViralBiologyNucleic acid secondary structureOpen Reading FramesViral ProteinsCapsidVirologyLeviviridaeAmino Acid SequenceGene3' Untranslated RegionsPhylogenyGeneticsAcinetobacterBase SequenceAllolevivirusNucleic acid sequenceRNAbiology.organism_classificationVirologyLeviviridaeNucleic Acid ConformationSequence AlignmentThe Journal of general virology
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Inhibition by cellular vacuolar ATPase impairs human papillomavirus uncoating and infection.

2014

ABSTRACT Several viruses, including human papillomaviruses, depend on endosomal acidification for successful infection. Hence, the multisubunit enzyme vacuolar ATPase (V-ATPase), which is mainly responsible for endosome acidification in the cell, represents an attractive target for antiviral strategies. In the present study, we show that V-ATPase is required for human papillomavirus (HPV) infection and that uncoating/disassembly but not endocytosis is affected by V-ATPase inhibition. The infection inhibitory potencies of saliphenylhalamide, a proven V-ATPase inhibitor, and its derivatives, as well as those of other V-ATPase inhibitors, were analyzed on different HPV types in relevant cell l…

Vacuolar Proton-Translocating ATPasesEndosomeCell SurvivalCellBiologyAlphapapillomavirusEndocytosisInhibitory postsynaptic potentialAntiviral AgentsCell LineViral ProteinsmedicineHumansPharmacology (medical)Vacuolar ATPasePharmacologychemistry.chemical_classificationVacuolar Proton-Translocating ATPasesVirologyEndocytosisCell biologyInfectious Diseasesmedicine.anatomical_structureEnzymechemistryCell cultureHeLa CellsAntimicrobial agents and chemotherapy
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Signal sequences modulate the immunogenic performance of human hepatitis C virus E2 gene

2005

Abstract Envelope protein E2 of human hepatitis C virus (HCV) is an attractive component of a prototype HCV vaccine. Delivered by DNA immunogens, E2 evokes specific immune response of Th1-type, failing to induce either considerable antibody production, or T-helper cell proliferation. We aimed at modulating the immunogenic performance of E2 gene by changing the mode of protein expression in eukaryotic cells. Plasmids were constructed encoding full-length E2 and nonstructural protein 1 (p7) fused to either 13 or 38 C-terminal amino acids (aa) of HCV E1 that contain second hydrophobic segment of E1 stop-transfer signal, or a complete E1 stop-transfer signal with duplicated second hydrophobic s…

Viral Hepatitis VaccinesSignal peptideGenes ViralMolecular Sequence DataImmunologyHeterologousHepacivirusProtein Sorting SignalsBiologyInjections IntramuscularEpitopeMiceViral ProteinsPlasmidViral Envelope ProteinsChlorocebus aethiopsEscherichia coliAnimalsHumansAmino Acid SequenceMolecular BiologyGeneCellular localizationCell Line TransformedMice Inbred BALB CImmunogenicityGenetic VariationCell Transformation ViralMolecular biologyCOS Cellsbiology.proteinAntibodyHeLa CellsPlasmidsMolecular Immunology
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Purified Membrane-Containing Procapsids of Bacteriophage PRD1 Package the Viral Genome

2009

Icosahedral-tailed double-stranded DNA (dsDNA) bacteriophages and herpesviruses translocate viral DNA into a preformed procapsid in an ATP-driven reaction by a packaging complex that operates at a portal vertex. A similar packaging system operates in the tailless dsDNA phage PRD1 (Tectiviridae family), except that there is an internal membrane vesicle in the procapsid. The unit-length linear dsDNA genome with covalently linked 5'-terminal proteins enters the procapsid through a unique vertex. Two small integral membrane proteins, P20 and P22, provide a conduit for DNA translocation. The packaging machinery also contains the packaging ATPase P9 and the packaging efficiency factor P6. Here we…

Viral Plaque AssayvirusesATPaseViral Plaque AssayGenomeViral Proteins03 medical and health scienceschemistry.chemical_compoundCapsidBacteriophage PRD1Structural BiologyBacteriophage PRD1Molecular BiologyIntegral membrane protein030304 developmental biology0303 health sciencesMicrobial Viabilitybiology030306 microbiologyVirus AssemblyCell MembraneMembrane ProteinsMolecular biologyMembranechemistryDNA Viralbiology.proteinBiophysicsTectiviridaeDNAJournal of Molecular Biology
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Replication of hepatitis C virus

2000

Viral pathogenesisHepatitis C virusVirus AssemblyViral transformationHepatitis CHepacivirusBiologymedicine.diseasemedicine.disease_causeTransfectionVirus ReplicationMicrobiologyVirologyPathogenesisViral ProteinsViral replicationReplication (statistics)medicineAnimalsRNA ViralOncovirusCells Cultured
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The Efficacy of Antigen Processing Is Critical for Protection against Cytomegalovirus Disease in the Presence of Viral Immune Evasion Proteins▿

2009

ABSTRACT Cytomegaloviruses (CMVs) code for immunoevasins, glycoproteins that are specifically dedicated to interfere with the presentation of antigenic peptides to CD8 T cells. Nonetheless, the biological outcome is not an immune evasion of the virus, since CD8 T cells can control CMV infection even when immunoevasins are expressed. Here, we compare the processing of a protective and a nonprotective epitope derived from the same viral protein, the antiapoptotic protein M45 in the murine model. The data provide evidence to conclude that protection against CMVs critically depends on antigenic peptides generated in an amount sufficient to exhaust the inhibitory capacity of immunoevasins.

Viral proteinImmunologyAntigen presentationCytomegalovirusBiologyCD8-Positive T-Lymphocytesmedicine.disease_causeMicrobiologyVirusEpitopeEpitopesMiceViral ProteinsImmune systemAntigenVirologyRibonucleotide ReductasesmedicineCytotoxic T cellAnimalsHumansAntigen PresentationAntigen processingVirologyPeptide FragmentsInsect ScienceImmunologyCytomegalovirus InfectionsPathogenesis and ImmunityApoptosis Regulatory Proteins
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Expression and cellular localization of the Nef protein from human immunodeficiency virus-1 in stably transfected B-cells.

1992

Nef protein, encoded by the regulatory nef gene of human immunodeficiency virus type 1 (HIV-1), was expressed in the B-cell line Raji. The cells were stably transfected with plasmids containing the nef transcriptional cassette. They expressed Nef with an Mr of 27,000; the yield could be augmented by incubation with the tumor promoter 12-O-tetradecanoylphorbol-13-acetate. The intracellular localization of Nef was analyzed applying immunofluorescence microscopy using a confocal laser scanning microscope. The antigen was stained with a monoclonal antibody directed against the N-terminal part of Nef. The experiments revealed that in non-dividing cells Nef is present both in the cytoplasm and th…

Viral proteinvirusesGenetic VectorsFluorescent Antibody TechniqueBiologymedicine.disease_causeTransfectionVirusGene Products nefGene productAntigenVirologyGene expressionmedicineTumor Cells CulturedHumansnef Gene Products Human Immunodeficiency VirusCellular localizationB-LymphocytesMicroscopyvirus diseasesGeneral MedicineTransfectionVirologyMolecular biologyCytoplasmHIV-1Tetradecanoylphorbol AcetateArchives of virology
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Coxsackievirus B3-Induced Cellular Protrusions: Structural Characteristics and Functional Competence▿†

2011

ABSTRACT Virus-induced alterations in cell morphology play important roles in the viral life cycle. To examine the intracellular events of coxsackievirus B3 (CVB3) infection, green monkey kidney (GMK) cells were either inoculated with the virus or transfected with the viral RNA. Various microscopic and flow cytometric approaches demonstrated the emergence of CVB3 capsid proteins at 8 h posttransfection, followed by morphological transformation of the cells. The morphological changes included formation of membranous protrusions containing viral capsids, together with microtubules and actin. Translocation of viral capsids into these protrusions was sensitive to cytochalasin D, suggesting the …

Viral proteinvirusesImmunologyCellBiologymedicine.disease_causeKidneyMicrobiologyVirusCell Linechemistry.chemical_compoundViral ProteinsImaging Three-DimensionalViral entryVirologymedicineEnterovirus InfectionsAnimalsHumansActinCytochalasin DTransfectionMolecular biologyCell biologyVirus-Cell InteractionsEnterovirus B HumanMicroscopy Electronmedicine.anatomical_structurechemistryInsect ScienceCapsid ProteinsIntracellular
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Structural Properties of Carnation Mottle Virus p7 Movement Protein and Its RNA-binding Domain

2001

Plant viral movement proteins (MPs) participate actively in the intra- and intercellular movement of RNA plant viruses to such an extent that MP dysfunction impairs viral infection. However, the molecular mechanism(s) of their interaction with cognate nucleic acids are not well understood, partly due to the lack of structural information. In this work, a protein dissection approach was used to gain information on the structural and RNA-binding properties of this class of proteins, as exemplified by the 61-amino acid residue p7 MP from carnation mottle virus (CarMV). Circular dichroism spectroscopy showed that CarMV p7 is an alpha/beta RNA-binding soluble protein. Using synthetic peptides de…

chemistry.chemical_classificationBinding SitesCarlavirusC-terminusMolecular Sequence DataRNA-Binding ProteinsRNACell BiologyBiologyAlanine scanningBiochemistryProtein Structure SecondaryAmino acidViral ProteinsProtein structureBiochemistrychemistryRNAAmino Acid SequenceBinding siteMolecular BiologyPeptide sequenceBinding domainJournal of Biological Chemistry
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