Search results for "Viruses"

showing 10 items of 1182 documents

HBV core particles as a carrier for B cell/T cell epitopes.

2001

In the middle 80s, recombinant hepatitis B virus cores (HBc) gave onset to icosahedral virus-like particles (VLPs) as a basic class of non-infectious carriers of foreign immunological epitopes. The recombinant HBc particles were used to display immunodominant epitopes of hepatitis B, C, and E virus, human rhinovirus, papillomavirus, hantavirus, and influenza virus, human and simian immunodeficiency virus, bovine and feline leukemia virus, foot-and-mouth disease virus, murine cytomegalovirus and poliovirus, and other virus proteins, as well as of some bacterial and protozoan protein epitopes. Practical applicability of the HBc particles as carriers was enabled by their ability to high level …

Models MolecularAntigenicityHepatitis B virusvirusesMolecular Sequence DataMolecular ConformationEpitopes T-LymphocyteBiologymedicine.disease_causeFeline leukemia virusVirusEpitopeAntigenVirologymedicineAnimalsHumansAmino Acid SequenceAntigens ViralHepatitis B virusVaccines SyntheticPoliovirusViral Core Proteinsvirus diseasesViral VaccinesGenetic TherapySimian immunodeficiency virusbiology.organism_classificationVirologyMolecular biologyInfectious DiseasesEpitopes B-LymphocyteIntervirology
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N‐Terminal Modification of Gly‐His‐Tagged Proteins with Azidogluconolactone

2021

Site-specific protein modifications are vital for biopharmaceutical drug development. Gluconoylation is a non-enzymatic, post-translational modification of N-terminal HisTags. We report high-yield, site-selective in vitro α-aminoacylation of peptides, glycoproteins, antibodies, and virus-like particles (VLPs) with azidogluconolactone at pH 7.5 in 1 h. Conjugates slowly hydrolyse, but diol-masking with borate esters inhibits reversibility. In an example, we multimerise azidogluconoylated SARS-CoV-2 receptor-binding domain (RBD) onto VLPs via click-chemistry, to give a COVID-19 vaccine. Compared to yeast antigen, HEK-derived RBD was immunologically superior, likely due to observed diffe…

Models MolecularAzidesCOVID-19 VaccinesGlycosylationvirusesGlycineGluconatesBiochemistryLactoneschemistry.chemical_compoundAntigenHumansHistidineVaccines Virus-Like ParticleSeroconversionMolecular Biologychemistry.chemical_classificationMolecular StructurebiologyChemistryOrganic ChemistryAntibodies NeutralizingBiopharmaceuticalBiochemistrybiology.proteinClick chemistryMolecular MedicineAntibodyGlycoproteinConjugateChemBioChem
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Effective stiffening of DNA due to nematic ordering causes DNA molecules packed in phage capsids to preferentially form torus knots.

2012

Observation that DNA molecules in bacteriophage capsids preferentially form torus type of knots provided a sensitive gauge to evaluate various models of DNA arrangement in phage heads. Only models resulting in a preponderance of torus knots could be considered as close to reality. Recent studies revealed that experimentally observed enrichment of torus knots can be qualitatively reproduced in numerical simulations that include a potential inducing nematic arrangement of tightly packed DNA molecules within phage capsids. Here, we investigate what aspects of the nematic arrangement are crucial for inducing formation of torus knots. Our results indicate that the effective stiffening of DNA by …

Models MolecularBacteriophages/genetics; Capsid/chemistry; DNA Viral/chemistry; Models Molecular; Virus AssemblyvirusesBacteriophageQuantitative Biology::Subcellular Processeschemistry.chemical_compoundCapsidstomatognathic systemLiquid crystalStructural BiologyGeneticsMoleculeBacteriophagesDna viralQuantitative Biology::BiomoleculesbiologyVirus Assemblyfood and beveragesTorusbiology.organism_classificationVirologyQuantitative Biology::GenomicsMathematics::Geometric TopologyStiffeningsurgical procedures operativechemistryCapsidDNA ViralBiophysicsDNANucleic acids research
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Extracellular Albumin and Endosomal Ions Prime Enterovirus Particles for Uncoating That Can Be Prevented by Fatty Acid Saturation

2019

ABSTRACT There is limited information about the molecular triggers leading to the uncoating of enteroviruses under physiological conditions. Using real-time spectroscopy and sucrose gradients with radioactively labeled virus, we show at 37°C, the formation of albumin-triggered, metastable uncoating intermediate of echovirus 1 without receptor engagement. This conversion was blocked by saturating the albumin with fatty acids. High potassium but low sodium and calcium concentrations, mimicking the endosomal environment, also induced the formation of a metastable uncoating intermediate of echovirus 1. Together, these factors boosted the formation of the uncoating intermediate, and the infectiv…

Models MolecularEchovirusHot TemperatureEndosomevirusesImmunologycryoEM structurerasvahapotEndosomesBiologymedicine.disease_causeMicrobiologyDivalentCell Line03 medical and health sciencesVirologyAlbuminsChlorocebus aethiopsExtracellularmedicineAnimalsalbumin030304 developmental biologychemistry.chemical_classificationalbumiinit0303 health sciencesbiokemiaionitenterovirus030302 biochemistry & molecular biologyCryoelectron MicroscopyFatty AcidsFatty acidRNAVirus-Cell InteractionsEnterovirus B HumanenteroviruksetchemistryCapsidvirologia13. Climate actionInsect ScienceBiophysicsCapsid ProteinsuncoatingLow sodium
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Molecular and structural characterization of fluorescent human parvovirus B19 virus-like particles

2005

Although sharing a T = 1 icosahedral symmetry with other members of the Parvoviridae family, it has been suggested that the fivefold channel of the human parvovirus B19 VP2 capsids is closed at its outside end. To investigate the possibility of placing a relatively large protein moiety at this site of B19, fluorescent virus-like particles (fVLPs) of B19 were developed. The enhanced green fluorescent protein (EGFP) was inserted at the N-terminus of the structural protein VP2 and assembly of fVLPs from this fusion protein was obtained. Electron microscopy revealed that these fluorescent protein complexes were very similar in size when compared to wild-type B19 virus. Further, fluorescence cor…

Models MolecularImmunoprecipitationRecombinant Fusion ProteinsvirusesGreen Fluorescent ProteinsBiophysicsFluorescence correlation spectroscopyEndosomesSpodopteraBiologyMicroscopy Atomic ForceBiochemistryFluorescenceCell LineGreen fluorescent proteinParvoviridae InfectionsBimolecular fluorescence complementationCell Line Tumorhemic and lymphatic diseasesParvovirus B19 HumanAnimalsHumansImmunoprecipitationMolecular BiologyParvoviridaeImmune SeraVirus AssemblyVirionvirus diseasesCell Biologybiology.organism_classificationFusion proteinMolecular biologyNanostructuresCell biologyTransport proteinProtein TransportCapsidCapsid Proteins
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Effect of ATP Binding and Hydrolysis on Dynamics of Canine Parvovirus NS1▿ †

2010

ABSTRACT The replication protein NS1 is essential for genome replication and protein production in parvoviral infection. Many of its functions, including recognition and site-specific nicking of the viral genome, helicase activity, and transactivation of the viral capsid promoter, are dependent on ATP. An ATP-binding pocket resides in the middle of the modular NS1 protein in a superfamily 3 helicase domain. Here we have identified key ATP-binding amino acid residues in canine parvovirus (CPV) NS1 protein and mutated amino acids from the conserved A motif (K406), B motif (E444 and E445), and positively charged region (R508 and R510). All mutations prevented the formation of infectious viruse…

Models MolecularParvovirus CaninevirusesImmunologyMolecular Sequence DataPlasma protein bindingViral Nonstructural ProteinsMicrobiologyCell Linechemistry.chemical_compoundAdenosine TriphosphateDogsVirologyAnimalsAmino Acid SequenceBinding siteBinding SitesbiologyHydrolysisDNA replicationHelicaseFluorescence recovery after photobleachingFusion proteinMolecular biologyGenome Replication and Regulation of Viral Gene ExpressionProtein Structure TertiaryViral replicationchemistryBiochemistryAmino Acid SubstitutionInsect Sciencebiology.proteinCatsMutagenesis Site-DirectedSequence AlignmentDNAProtein Binding
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Flavonoids as noncompetitive inhibitors of Dengue virus NS2B-NS3 protease: Inhibition kinetics and docking studies

2014

NS2B-NS3 is a serine protease of the Dengue virus considered a key target in the search for new antiviral drugs. In this study flavonoids were found to be inhibitors of NS2B-NS3 proteases of the Dengue virus serotypes 2 and 3 with IC50 values ranging from 15 to 44 μM. Agathisflavone (1) and myricetin (4) turned out to be noncompetitive inhibitors of dengue virus serotype 2 NS2B-NS3 protease with Ki values of 11 and 4.7 μM, respectively. Docking studies propose a binding mode of the flavonoids in a specific allosteric binding site of the enzyme. Analysis of biomolecular interactions of quercetin (5) with NT647-NHS-labeled Dengue virus serotype 3 NS2B-NS3 protease by microscale thermophoresis…

Models MolecularProteasesSerine Proteinase Inhibitorsvirusesmedicine.medical_treatmentClinical BiochemistryPharmaceutical ScienceDengue virusmedicine.disease_causeAntiviral AgentsBiochemistryStructure-Activity Relationshipchemistry.chemical_compoundDrug DiscoverymedicineMolecular BiologyFlavonoidsSerine proteaseNS3ProteasebiologyMicroscale thermophoresisSerine EndopeptidasesOrganic ChemistryDengue VirusVirologyMolecular Docking SimulationKineticschemistryBiochemistryDocking (molecular)biology.proteinMolecular MedicineMyricetinBioorganic & Medicinal Chemistry
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Evidence for substrate binding-induced zwitterion formation in the catalytic Cys-His dyad of the SARS-CoV main protease.

2014

The coronavirus main protease (M(pro)) represents an attractive drug target for antiviral therapy of coronavirus (CoV) infections, including severe acute respiratory syndrome (SARS). The SARS-CoV M(pro) and related CoV proteases have several distinct features, such as an uncharged Cys-His catalytic dyad embedded in a chymotrypsin-like protease fold, that clearly separate these enzymes from archetypical cysteine proteases. To further characterize the catalytic system of CoV main proteases and to obtain information about improved inhibitors, we performed comprehensive simulations of the proton-transfer reactions in the SARS-CoV M(pro) active site that lead to the Cys(-)/His(+) zwitterionic st…

Models MolecularProteasesStereochemistryvirusesmedicine.medical_treatmentEntropyStatic ElectricityMolecular Dynamics Simulationmedicine.disease_causeBiochemistrySubstrate Specificitychemistry.chemical_compoundViral ProteinsCatalytic DomainmedicineHistidineCysteineHistidineCoronavirus 3C ProteasesCoronaviruschemistry.chemical_classificationProteasebiologyChemistryvirus diseasesActive siteCysteine EndopeptidasesEnzymeBiochemistryZwitterionbiology.proteinCysteineBiochemistry
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Mass Spectrometry and Structural Biology Techniques in the Studies on the Coronavirus-Receptor Interaction

2020

Mass spectrometry and some other biophysical methods, have made substantial contributions to the studies on severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and human proteins interactions. The most interesting feature of SARS-CoV-2 seems to be the structure of its spike (S) protein and its interaction with the human cell receptor. Mass spectrometry of spike S protein revealed how the glycoforms are distributed across the S protein surface. X-ray crystallography and cryo-electron microscopy made huge impact on the studies on the S protein and ACE2 receptor protein interaction, by elucidating the three-dimensional structures of these proteins and their conformational changes. The…

Models MolecularProtein Conformation alpha-HelicalvirusesGene ExpressionPharmaceutical ScienceReviewPlasma protein bindingSevere Acute Respiratory Syndromemedicine.disease_causeAnalytical Chemistry0302 clinical medicineDrug Discovery030212 general & internal medicineReceptorPeptide sequenceCoronavirus0303 health sciencesChemistrySevere acute respiratory syndrome-related coronavirusBiochemistryChemistry (miscellaneous)Host-Pathogen InteractionsSpike Glycoprotein CoronavirusReceptors VirusMolecular MedicineAngiotensin-Converting Enzyme 2Coronavirus InfectionsProtein BindingglycosylationSARS coronavirusPneumonia Viralstructural techniquesSequence alignmentPeptidyl-Dipeptidase AMass spectrometrylcsh:QD241-441Betacoronavirus03 medical and health scienceslcsh:Organic chemistryspike protein-ACE2 interactionmedicineHumansProtein Interaction Domains and MotifsAmino Acid SequencePhysical and Theoretical ChemistryBinding sitePandemics030304 developmental biologyBinding SitesSARS-CoV-2Organic ChemistryCOVID-19MSStructural biologyProtein Conformation beta-StrandSequence AlignmentMolecules
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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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