Search results for "viral protein"

showing 10 items of 182 documents

A novel transmembrane domain mediating retention of a highly motile herpesvirus glycoprotein in the endoplasmic reticulum

2010

Gene m164 of murine cytomegalovirus belongs to the large group of 'private' genes that show no homology to those of other cytomegalovirus species and are thought to represent 'host adaptation' genes involved in virus-host interaction. Previous interest in the m164 gene product was based on the presence of an immunodominant CD8 T-cell epitope presented at the surface of infected cells, despite interference by viral immune-evasion proteins. Here, we provide data to reveal that the m164 gene product shows unusual features in its cell biology. A novel strategy of mass-spectrometric analysis was employed to map the N terminus of the mature protein, 107 aa downstream of the start site of the pred…

MuromegalovirusKKXXEndoplasmic reticulumMembrane ProteinsER retentionSTIM1Protein Sorting SignalsBiologyEndoplasmic ReticulumMass SpectrometryTransmembrane proteinCell biologyTransport proteinMolecular WeightGene productOpen Reading FramesProtein TransportViral ProteinsTransmembrane domainBiochemistryVirologyCOS CellsChlorocebus aethiopsAnimalsGlycoproteinsJournal of General Virology
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Major Histocompatibility Complex Class I Allele-specific Cooperative and Competitive Interactions between Immune Evasion Proteins of Cytomegalovirus

2002

Cytomegaloviruses (CMVs) deploy a set of genes for interference with antigen presentation in the major histocompatibility complex (MHC) class I pathway. In murine CMV (MCMV), three genes were identified so far: m04/gp34, m06/gp48, and m152/gp40. While their function as immunoevasins was originally defined after their selective expression, this may not necessarily reflect their biological role during infection. The three immunoevasins might act synergistically, but they might also compete for their common substrate, the MHC class I complexes. To approach this question in a systematic manner, we have generated a complete set of mutant viruses with deletions of the three genes in all seven pos…

Muromegalovirusmurine cytomegalovirusImmunologyAntigen presentationGenes MHC Class IMutagenesis (molecular biology technique)Context (language use)Virus ReplicationMajor histocompatibility complexPolymerase Chain ReactionArticleMiceViral ProteinsMuromegalovirusMHC class IEscherichia coliAnimalsImmunology and AllergyGeneAllelesBACimmune evasionGlycoproteinsGeneticsMice Inbred BALB CMembrane GlycoproteinsbiologyalleleFibroblastsbiology.organism_classificationViral replicationMHC class IIbiology.proteinCarrier ProteinsJournal of Experimental Medicine
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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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Delayed lysis confers resistance to the nucleoside analogue 5-fluorouracil and alleviates mutation accumulation in the single-stranded DNA bacterioph…

2014

ABSTRACT Rates of spontaneous mutation determine viral fitness and adaptability. In RNA viruses, treatment with mutagenic nucleoside analogues selects for polymerase variants with increased fidelity, showing that viral mutation rates can be adjusted in response to imposed selective pressures. However, this type of resistance is not possible in viruses that do not encode their own polymerases, such as single-stranded DNA viruses. We previously showed that serial passaging of bacteriophage ϕX174 in the presence of the nucleoside analogue 5-fluorouracil (5-FU) favored substitutions in the lysis protein E (P. Domingo-Calap, M. Pereira-Gomez, and R. Sanjuán, J. Virol. 86: 9640–9646, 2012, doi:10…

Mutation rateImmunologyAdaptation BiologicalMutation MissenseDNA Single-Strandedmedicine.disease_causeMicrobiologyBacteriophage03 medical and health scienceschemistry.chemical_compoundViral ProteinsBacteriolysisMutation RateVirologymedicineBacteriophagesSelection GeneticPolymerase030304 developmental biologyGenetics0303 health sciencesMutationbiology030302 biochemistry & molecular biologyMutagenesisMutation AccumulationResistance mutationbiology.organism_classificationVirologychemistryGenetic Diversity and EvolutionInsect ScienceDNA Viralbiology.proteinMutant ProteinsFluorouracilDNAJournal of virology
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Changes in protein domains outside the catalytic site of the bacteriophage Qβ replicase reduce the mutagenic effect of 5-azacytidine.

2014

ABSTRACT The high genetic heterogeneity and great adaptability of RNA viruses are ultimately caused by the low replication fidelity of their polymerases. However, single amino acid substitutions that modify replication fidelity can evolve in response to mutagenic treatments with nucleoside analogues. Here, we investigated how two independent mutants of the bacteriophage Qβ replicase (Thr210Ala and Tyr410His) reduce sensitivity to the nucleoside analogue 5-azacytidine (AZC). Despite being located outside the catalytic site, both mutants reduced the mutation frequency in the presence of the drug. However, they did not modify the type of AZC-induced substitutions, which was mediated mainly by …

Mutation rateImmunologyMutantRNA-dependent RNA polymeraseBiologyVirus ReplicationMicrobiologyViral ProteinsVirologyCatalytic DomainmedicineGeneticsAllolevivirusNucleoside analogueQ beta Replicasebiology.organism_classification3. Good healthProtein Structure TertiaryViral replicationBiochemistryAmino Acid SubstitutionGenetic Diversity and EvolutionInsect ScienceAzacitidineQ beta ReplicaseBacteriophage QβNucleosidemedicine.drugMutagensJournal of virology
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Preparation of hepatitis C virus structural and non-structural protein fragments and studies of their immunogenicity

2006

Abstract Plasmids pQE-60 and pQE-30 containing 6× His-tag sequence were used for expression of fragments of HCV structural and non-structural proteins in Escherichia coli (E. coli). The following fragments were used: core (1–98 aa), NS3 (202–482 aa), and tetramer of hypervariable region 1 (HVR1) of E2 protein. The constructed plasmids directed high levels of expression of HCV proteins in E. coli JM109. After purification by the metal-affinity chromatography on nickel–nitrilotriacetic acid (Ni–NTA) agarose, the His-tagged HCV proteins were used for immunization of BALB/c mice. All three proteins were able to induce high levels of specific antibodies and, in the case of the NS3 and HVR1 tetra…

Nitrilotriacetic AcidHepatitis C virusDose-Response Relationship ImmunologicViral Nonstructural ProteinsBiologymedicine.disease_causeSensitivity and SpecificityChromatography AffinityAntigen-Antibody ReactionsMiceViral Proteinschemistry.chemical_compoundPlasmidTetramerNickelmedicineAnimalsCloning MolecularEscherichia coliCell ProliferationMice Inbred BALB CNS3Viral Core ProteinsImmunogenicityvirus diseasesHepatitis C AntibodiesVirologyMolecular biologyPeptide FragmentsRecombinant Proteinsdigestive system diseasesHypervariable regionchemistryAgaroseFemaleImmunizationHepatitis C AntigensPeptidesSpleenBiotechnologyProtein Expression and Purification
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A Sliding Window-Based Method to Detect Selective Constraints in Protein-Coding Genes and Its Application to RNA Viruses

2002

Here we present a new sliding window-based method specially designed to detect selective constraints in specific regions of a multiple protein-coding sequence alignment. In contrast to previous window-based procedures, our method is based on a nonarbitrary statistical approach to find the appropriate codon-window size to test deviations of synonymous (d(S)) and nonsynonymous (d(N)) nucleotide substitutions from the expectation. The probabilities of d(N) and d(S) are obtained from simulated data and used to detect significant deviations of d(N) and d(S) in a specific window region of the real sequence alignment. The nonsynonymous-to-synonymous rate ratio (w = d(N)/d(S)) was used to highlight…

Nonsynonymous substitutionGenes ViralSequence alignmentBiologyGenes envEvolution MolecularViral ProteinsSliding window protocolGeneticsRNA VirusesSelection GeneticMolecular BiologyGenePhylogenyEcology Evolution Behavior and SystematicsSelection (genetic algorithm)GeneticsBase SequenceReproducibility of ResultsContrast (statistics)RNAWindow (computing)Genes gagFoot-and-Mouth Disease VirusDNA ViralHIV-1Capsid ProteinsSequence AlignmentAlgorithmJournal of Molecular Evolution
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Synthesis and assembly of virus-like particles of human papillomaviruses type 6 and type 16 in fission yeast Schizosaccharomyces pombe.

1995

AbstractWe have synthesized capsid proteins of human papillomavirus types 6 (HPV 6) and 16 (HPV 16) in fission yeast Schizosaccharomyces pombe and produced virus-like particles (VLP). The capsid proteins were localized in the nucleus by indirect immunofluorescence and cell fractionation analyses. The VLP were produced in both yeast clones synthesizing L1 alone and L1/L2 and purified by sulfato-cellulofine chromatography. Electron microscopic examination showed that these VLP were similar in structure to native HPV particles. Two HPV 16 L1 variants (16 B27L1 and 16 T3L1), isolated from benign cervical samples, produced many more (68- and 14-fold) VLP than the prototype L1 (16 PL1) derived fr…

Oncogene ProteinsImmunoprecipitationvirusesMolecular Sequence DataBiologyVirusSepharoseViral ProteinsCapsidVirologySchizosaccharomycesCloning MolecularPapillomaviridaeDNA PrimersBase SequenceVirionvirus diseasesOncogene Proteins Viralbiology.organism_classificationMolecular biologyYeastRecombinant ProteinsMicroscopy ElectronCapsidSchizosaccharomyces pombeCapsid ProteinsCell fractionationVirology
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Taking Advantage of Viral Immune Evasion: Virus-Derived Proteins Represent Novel Biopharmaceuticals

2006

In healthy individuals, natural and adaptive immune responses are able to control virus entry into the host. In particular, CD8(+)-mediated cytotoxicity, sustained by the intervention of CD4+ cells, represents the major key event leading to virus eradication. On the other hand, viruses are able to evade from host immune response via several mechanisms, and special emphasis will be placed on hepatitis C virus and chronic Epstein-Barr infections also in view of personal data. Virokines, viroreceptors, and serpins greatly contribute to viral immune escape, and, among virokines, interleukin (IL)-10 has been object of intensive studies. Finally, all these products have been used as biopharmaceut…

PharmacologyHepatitis C virusOrganic ChemistryInterleukinVirus Physiological PhenomenaBiologymedicine.disease_causeAntiviral AgentsBiochemistryVirologyVirusViral ProteinsImmune systemViral entryVirusesDrug DiscoveryImmunologyAntigenic variationmedicineHumansMolecular MedicineCD8Virus Physiological PhenomenaCurrent Medicinal Chemistry
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Globally defining the effects of mutations in a picornavirus capsid

2021

The capsids of non-enveloped viruses are highly multimeric and multifunctional protein assemblies that play key roles in viral biology and pathogenesis. Despite their importance, a comprehensive understanding of how mutations affect viral fitness across different structural and functional attributes of the capsid is lacking. To address this limitation, we globally define the effects of mutations across the capsid of a human picornavirus. Using this resource, we identify structural and sequence determinants that accurately predict mutational fitness effects, refine evolutionary analyses, and define the sequence specificity of key capsid-encoded motifs. Furthermore, capitalizing on the derive…

PicornavirusViral proteinQH301-705.5Sciencevirusesmedicine.medical_treatmentPicornaviridaeComputational biologymedicine.disease_causeGenomeGeneral Biochemistry Genetics and Molecular BiologyVirusImmune systemcapsidmedicineSingle amino acidBiology (General)GeneTropismHost proteinGeneticsEvolutionary BiologyMicrobiology and Infectious DiseaseMutationmutational fitness effectsProteaseGeneral Immunology and MicrobiologybiologyGeneral NeuroscienceQRviral proteaseGeneral Medicinebiochemical phenomena metabolism and nutritionbiology.organism_classificationViruspicornavirusViral proteaseCapsidMutationMedicineCapsid ProteinsHuman genomeDeep mutational scanningResearch ArticleHuman
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