Search results for "Allolevivirus"

showing 6 items of 6 documents

Mosaic Qβ coats as a new presentation model

1998

The new protein carrier was developed on the basis of recombinant RNA phage Qbeta capsid. C-terminal UGA extension of the short form of Qbeta coat, so-called A1 extension, served as a target for presentation of foreign peptides on the outer surface of mosaic Qbeta particles. In conditions of enhanced UGA suppression, the proportion of A1-extended to short coats in mosaic particles dropped from 48% to 14%, with an increase of the length of A1 extension. A model insertion, short preS1 epitope 31-DPAFR-35 of hepatitis B surface antigen, demonstrated superficial location on the mosaic Qbeta particles and ensured specific antigenicity and immunogenicity.

AntigenicityRecombinant Fusion ProteinsGenetic VectorsBiophysicsBiologyHepatitis b surface antigenBiochemistryEpitopelaw.inventionCapsid assemblyMiceCapsidPhage QβPeptide LibraryStructural BiologylawGeneticsAnimalsHepatitis B virus preS1Cloning MolecularMolecular BiologyAllolevivirusMice Inbred BALB CCoat protein UGA suppressionVirus AssemblyImmunogenicityA1 extensionRNACell BiologyImmunogenicityVirologyMolecular biologyCapsidCarrier proteinCodon TerminatorRecombinant DNACapsid ProteinsFEBS Letters
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Mutilation of RNA phage Qβ virus-like particles: from icosahedrons to rods

2000

Icosahedral virus-like particles (VLPs) of RNA phage Qbeta are stabilized by four disulfide bonds of cysteine residues 74 and 80 within the loop between beta-strands F and G (FG loop) of the monomeric subunits, which determine the five-fold and quasi-six-fold symmetry contacts of the VLPs. In order to reduce the stability of Qbeta VLPs, we mutationally converted the amino acid stretch 76-ANGSCD-81 within the FG loop into the 76-VGGVEL-81 sequence. It led to production in Escherichia coli cells of aberrant rod-like Qbeta VLPs, along with normal icosahedral capsids. The length of the rod-like particles exceeded 4-30 times the diameter of icosahedral Qbeta VLPs.

Icosahedral symmetryvirusesGenetic VectorsMolecular Sequence DataBiophysicsBiologymedicine.disease_causecomplex mixturesBiochemistryVirus-like particleStructural BiologyGeneticsmedicineAmino Acid SequenceCysteineMolecular BiologyEscherichia coliPeptide sequenceIcosahedronAlloleviviruschemistry.chemical_classificationSequence Homology Amino AcidRod-like structureVirionvirus diseasesRNASelf-assemblyCell Biologybiochemical phenomena metabolism and nutritionAmino acidCrystallographyCapsidchemistryMutagenesis Site-DirectedRNA ViralRNA phage QβVirus-like particleCysteineFEBS Letters
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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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Correlation between mutation rate and genome size in riboviruses: mutation rate of bacteriophage Qβ.

2013

Abstract Genome sizes and mutation rates covary across all domains of life. In unicellular organisms and DNA viruses, they show an inverse relationship known as Drake’s rule. However, it is still unclear whether a similar relationship exists between genome sizes and mutation rates in RNA genomes. Coronaviruses, the RNA viruses with the largest genomes (∼30 kb), encode a proofreading 3′ exonuclease that allows them to increase replication fidelity. However, it is unknown whether, conversely, the RNA viruses with the smallest genomes tend to show particularly high mutation rates. To test this, we measured the mutation rate of bacteriophage Qβ, a 4.2-kb levivirus. Amber reversion-based Luria–D…

Mutation rate[SDE.MCG]Environmental Sciences/Global ChangesMutantGenome ViralInvestigationsGenomeEvolution Molecular03 medical and health scienceschemistry.chemical_compound[SDV.EE.ECO]Life Sciences [q-bio]/Ecology environment/EcosystemsGenome SizeMutation Rate[SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseasesGeneticsEscherichia coliGenome sizeComputingMilieux_MISCELLANEOUS030304 developmental biologyGenetics[SDV.EE.SANT]Life Sciences [q-bio]/Ecology environment/HealthAllolevivirus0303 health sciences[SDV.MHEP.ME]Life Sciences [q-bio]/Human health and pathology/Emerging diseasesbiology030302 biochemistry & molecular biologyRNAbiology.organism_classification[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology3. Good healthchemistry[SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/VirologyProofreading[SDE.BE]Environmental Sciences/Biodiversity and EcologyBacteriophage QβDNAGenetics
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The crystal structure of bacteriophage Qβ at 3.5 å resolution

1996

Abstract Background: The capsid protein subunits of small RNA bacteriophages form a T=3 particle upon assembly and RNA encapsidation. Dimers of the capsid protein repress translation of the replicase gene product by binding to the ribosome binding site and this interaction is believed to initiate RNA encapsidation. We have determined the crystal structure of phage Qβ with the aim of clarifying which factors are the most important for particle assembly and RNA interaction in the small phages. Results The crystal structure of bacteriophage Qβ determined at 3.5 a resolution shows that the capsid is stabilized by disulfide bonds on each side of the flexible loops that are situated around the fi…

Small RNAcrystal structureProtein ConformationvirusesMolecular Sequence DataBeta sheetMS2RNA-dependent RNA polymeraseCapsidProtein structureStructural BiologyAmino Acid SequenceBinding siteMolecular BiologyAllolevivirusBinding SitesCrystallographySequence Homology Amino AcidbiologyRNA-Binding ProteinsRNAbiology.organism_classificationProtein Structure TertiaryCrystallographyCapsidBiophysicsSequence AlignmentBacteriophage QβStructure
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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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