Search results for "Caps"

showing 10 items of 745 documents

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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Nasal immunization of mice with a rotavirus DNA vaccine that induces protective intestinal IgA antibodies

2004

International audience; DNA vaccination using a plasmid encoding the rotavirus inner capsid VP6 has been explored in the mouse model of rotavirus infection. BALB/c mice were immunized with a VP6 DNA vaccine by the intramuscular, nasal and oral routes. VP6 DNA vaccination by the nasal and oral routes induced the production of anti-VP6 IgA antibodies by intestinal lymphoid cells. Intramuscular DNA injection stimulated the production of serum anti-VP6 IgG but not serum anti-VP6 IgA antibodies. Protection against shedding of rotaviruses in stools after oral challenge with the murine EDIM rotavirus strain was investigated in the immunized mice. A significant reduction in the level of rotavirus a…

Immunoglobulin A[SDV]Life Sciences [q-bio]virusesAdministration OralAntibodies Viralmedicine.disease_causeImmunoglobulin GFecesMice0302 clinical medicineRotavirusVaccines DNAAntigens ViralMice Inbred BALB CVaccines Synthetic0303 health sciencesvirus diseasesVirus Shedding3. Good healthInfectious DiseasesMolecular MedicineFemaleDNA vaccineEnzyme-Linked Immunosorbent AssayBiologyInjections IntramuscularRotavirus InfectionsDNA vaccination03 medical and health sciencesAntigenmedicineAnimalsViral sheddingAdministration Intranasal030304 developmental biologyGeneral VeterinaryGeneral Immunology and Microbiologyintestinal IgA antibodyRotavirus VaccinesPublic Health Environmental and Occupational HealthVirologyImmunoglobulin ADisease Models AnimalrotavirusImmunizationImmunoglobulin GImmunologybiology.proteinCapsid ProteinsNasal administration030215 immunologyVaccine
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Relationship between within-host fitness and virulence in the vesicular stomatitis virus: correlation with partial decoupling.

2012

ABSTRACT Given the parasitic nature of viruses, it is sometimes assumed that rates of viral replication and dissemination within hosts (within-host fitness) correlate with virulence. However, there is currently little empirical evidence supporting this principle. To test this, we quantified the fitness and virulence of 21 single- or double-nucleotide mutants of the vesicular stomatitis virus in baby hamster kidney cells (BHK-21). We found that, overall, these two traits correlated positively, but significant outliers were identified. Particularly, a single mutation in the conserved C terminus of the N nucleocapsid (U1323A) had a strongly deleterious fitness effect but did not alter or even …

ImmunologyMutantVirulenceApoptosisBiologymedicine.disease_causeVirus ReplicationMicrobiologyVesicular stomatitis Indiana virusCell Line03 medical and health sciencesVesicular StomatitisMiceVirologyCricetinaemedicineBaby hamster kidney cellAnimals030304 developmental biologyGlycoproteinsGenetics0303 health sciencesMutationMice Inbred BALB CVirulence030302 biochemistry & molecular biologyCell MembraneBrainNucleocapsid Proteinsbiology.organism_classification3. Good healthProtein Structure TertiaryViral replicationGenetic Diversity and EvolutionVesicular stomatitis virusInsect ScienceMutationFemaleNeuron deathVesicular StomatitisJournal of virology
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Identification of a Dynein Interacting Domain in the Papillomavirus Minor Capsid Protein L2

2006

ABSTRACT Papillomaviruses enter cells via endocytosis (H. C. Selinka et al., Virology 299:279-287, 2002). After egress from endosomes, the minor capsid protein L2 accompanies the viral DNA to the nucleus and subsequently to the subnuclear promyelocytic leukemia protein bodies (P. M. Day et al., Proc. Natl. Acad. Sci. USA 101:14252-14257, 2004), suggesting that this protein may be involved in the intracytoplasmic transport of the viral genome. We now demonstrate that the L2 protein is able to interact with the microtubule network via the motor protein dynein. L2 protein was found attached to microtubules after uncoating of incoming human papillomavirus pseudovirions. Based on immunofluoresce…

ImmunoprecipitationImmunologyDyneinActive Transport Cell NucleusGenome ViralMicrotubulesMicrobiologyMotor proteinPromyelocytic leukemia proteinMicrotubuleDynein ATPaseVirologyHumansPapillomaviridaebiologyPapillomavirus InfectionsDyneinsOncogene Proteins ViralMolecular biologyEndocytosisVirus-Cell InteractionsMicroscopy FluorescenceCapsidInsect ScienceDNA Viralbiology.proteinDynactinCapsid ProteinsIntranuclear SpaceHeLa CellsProtein BindingJournal of Virology
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Dissection of human papillomavirus type 33 L2 domains involved in nuclear domains (ND) 10 homing and reorganization

2003

Abstract We have recently shown that the minor capsid protein L2 of human papillomavirus type 33 (HPV33) recruits the transcriptional repressor Daxx into nuclear domains (ND) 10 and causes the loss of the transcriptional activator Sp100 from these subnuclear structures (Florin et al., 2002b) . In order to dissect L2 domains involved in nuclear translocation, ND10 homing, loss of Sp100, and recruitment of Daxx, a detailed deletion mutagenesis of L2 was performed. Using immunofluorescence and green fluorescent protein fusions, we have identified two nuclear localization signals (NLS) in the central and C-terminal part of L2, respectively, homologous to previously identified NLS in HPV6B L2 (S…

ImmunoprecipitationRecombinant Fusion ProteinsGreen Fluorescent ProteinsNuclear Localization SignalsActive Transport Cell NucleusFluorescent Antibody TechniqueBiologyImmunofluorescenceAutoantigensGreen fluorescent proteinDeath-associated protein 6DaxxVirologyTumor Cells CulturedmedicineSp100HumansNLSPapillomaviridaeAdaptor Proteins Signal TransducingCell Nucleusmedicine.diagnostic_testIntracellular Signaling Peptides and ProteinsND10Nuclear ProteinsAntigens NuclearL2Oncogene Proteins ViralPapillomavirusbiochemical phenomena metabolism and nutritionMolecular biologyDeletion MutagenesisLuminescent ProteinsCapsidMutagenesisCapsid ProteinsCarrier ProteinsCo-Repressor ProteinsGene DeletionNuclear localization sequenceMolecular ChaperonesVirology
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An L2 SUMO interacting motif is important for PML localization and infection of human papillomavirus type 16

2014

Summary Human papillomaviruses (HPV) induce warts and cancers on skin and mucosa. The HPV16 capsid is composed of the proteins L1 and L2. After cell entry and virus disassembly, the L2 protein accompanies the viral DNA to promyelocytic leukaemia nuclear bodies (PML-NBs) within the host nuclei enabling viral transcription and replication. Multiple components of PML-NBs are regulated by small ubiquitin-like modifiers (SUMOs) either based on covalent SUMO modification (SUMOylation), or based on non-covalent SUMO interaction via SUMO interacting motifs (SIMs). We show here that the HPV16 L2 comprises at least one SIM, which is crucial for the L2 interaction with SUMO2 in immunoprecipitation and…

ImmunoprecipitationvirusesImmunologyMutantSUMO proteinvirus diseasesColocalizationSUMO2BiologyMicrobiologyMolecular biologyVirusCapsidTranscription (biology)Virologyembryonic structuresCellular Microbiology
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Boosting the in situ encapsulation of proteins with MIL-100(Fe): the role of strong Lewis acid centers

2021

Encapsulation of biomolecules using Metal-Organic Frameworks (MOFs) to form stable biocomposites has been demonstrated a valuable strategy for their preservation and controlled release, which has been however restricted to specific electrostatic surface conditions. We present a general in situ strategy that promotes the spontaneous MOF growth onto a broad variety of proteins, for the first time, regardless of their surface nature. We demonstrate that MOFs based on cations exhibiting considerable inherent acidity such as MIL-100(Fe) enable biomolecule encapsulation, including alkaline proteins previously inaccesible by the welldeveloped in situ encapsulation with azolate-based MOFs. In parti…

In situchemistry.chemical_classificationScaffoldchemistryBiomoleculefungiTriggered releaseNanotechnologyBiocompatible materialControlled releaseSurface conditionsEncapsulation (networking)
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Spectroscopic markers of the T-R quaternary transition in human hemoglobin

2004

n questo lavoro, usiamo un protocollo sol-gel per intrappolare e confrontare gli stati quaternari R e T di entrambi i deossigenati (deossiHb) ederivati ​​di ossido di carbonio (HbCO) dell'emoglobina umana. La banda di assorbimento ottico del vicino infrarosso III e lo stretching di CO a infrarossibanda sono utilizzati per rilevare l'effetto della struttura quaternaria sulle proprietà spettrali di deoxyHb e HbCO; confronto con mioglobinaconsente una valutazione dei contributi terziari e quaternari ai turni di banda misurati. La RXLa transizione T è indicata per causare un bluspostamento della banda III di ~ 35 cm?1per deoxyHb e uno spostamento rosso della banda di allungamento CO di soli ~ 0…

InfraredBiophysicsAnalytical chemistryBiochemistryPhase Transitionchemistry.chemical_compoundHemoglobinsSpectroscopy Fourier Transform InfraredHumansFourier transform infrared spectroscopySpectroscopyProtein Structure QuaternaryCarbon MonoxideChemistryOrganic ChemistryNear-infrared spectroscopyBand IIILow temperature spectroscopyTemperatureBand IIICO stretching bandOxygenSol–gel encapsulationCrystallographyKineticsFTIR spectroscopyMyoglobinAbsorption bandProtein quaternary structureBiomarkersProtein Binding
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Antihyperalgesic and analgesic properties of the N-methyl-d-aspartate (NMDA) receptor antagonist neramexane in a human surrogate model of neurogenic …

2006

Abstract NMDA-receptors are a major target in the prevention and treatment of hyperalgesic pain states in neuropathic pain. However, previous studies revealed equivocal results depending on study design and efficacy parameters. We tested the analgesic (generalized reduction of generation and processing of nociceptive signalling) and anti-hyperalgesic (prevention of central sensitization) properties of the NMDA-receptor antagonist neramexane and the potassium channel opener flupirtine in the intradermal capsaicin injection model. Furthermore, we tested the effect on pain summation (wind up). Eighteen healthy subjects received either a single dose of neramexane (40 mg p.o.), flupirtine (100 m…

Injections IntradermalAnalgesicAminopyridinesPainCyclopentanesPharmacologyPlaceboReceptors N-Methyl-D-AspartateDouble-Blind MethodPhysical StimulationHumansMedicineAnalgesicsCross-Over StudiesDose-Response Relationship Drugbusiness.industryNeramexaneTreatment OutcomeAnesthesiology and Pain MedicineAllodyniaNociceptionHyperalgesiaAnesthesiaNeuropathic painHyperalgesiaCapsaicinNervous System Diseasesmedicine.symptomFlupirtinebusinessmedicine.drugEuropean Journal of Pain
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Protection of rabbits against rabbit viral haemorrhagic disease with a vaccinia-RHDV recombinant virus

1996

In order to protect domestic and wild rabbits against RVHD, we constructed a recombinant vaccinia-RHDV virus, using the Copenhagen strain of the vaccinia virus. This recombinant virus expressed the RHDV capsid protein (VP60). Analysis of the expressed product showed that the recombinant protein, which is 60 kDa in size, was antigenic as revealed by its reactions in immunoprecipitation and indirect immunofluorescence with the antibodies raised against RHDV. The recombinant virus induced high level of RHDV specific antibodies in rabbits following immunization. Inoculations by both the intradermal and oral routes allow protection of animals against a challenge with virulent RHDV.

Injections IntradermalHemorrhagic Disease Virus Rabbitviruses[SDV]Life Sciences [q-bio]Administration OralVaccinia virusGenome ViralBiologyAntibodies ViralRecombinant virusVirusCell Linelaw.invention03 medical and health scienceschemistry.chemical_compoundlawAnimalsPoxviridaeOrthopoxvirusComputingMilieux_MISCELLANEOUSCaliciviridae Infections030304 developmental biologyViral Structural ProteinsVaccines Synthetic0303 health sciencesGeneral VeterinaryGeneral Immunology and Microbiology030306 microbiologyPublic Health Environmental and Occupational HealthViral Vaccinesbiology.organism_classificationVirologyCaliciviridae3. Good health[SDV] Life Sciences [q-bio]Infectious DiseaseschemistryCapsidRecombinant DNAMolecular MedicineVACCINATIONRabbitsVaccinia
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