Search results for "ns3"

showing 10 items of 23 documents

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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Proline-Based Allosteric Inhibitors of Zika and Dengue Virus NS2B/NS3 Proteases

2019

The NS2B/NS3 serine proteases of the Zika and Dengue flaviviruses are attractive targets for the development of antiviral drugs. We report the synthesis and evaluation of a new, proline-based compound class that displays allosteric inhibition of both proteases. The structural features relevant for protease binding and inhibition were determined to establish them as new lead compounds for flaviviral inhibitors. Based on our structure-activity relationship studies, the molecules were further optimized, leading to inhibitors with submicromolar IC50 values and improved lipophilic ligand efficiency. The allosteric binding site in the proteases was probed using mutagenesis and covalent modificati…

ProteasesProlineProtein ConformationAllosteric regulationViral Nonstructural ProteinsDengue virusmedicine.disease_causeAntiviral Agents01 natural sciencesDengueSerineStructure-Activity RelationshipViral Proteins03 medical and health sciencesAllosteric RegulationCatalytic DomainDrug DiscoverymedicineHumansStructure–activity relationshipProtease Inhibitors030304 developmental biology0303 health sciencesNS3Ligand efficiencyZika Virus InfectionChemistryProtease bindingSerine EndopeptidasesZika VirusDengue Virus0104 chemical sciencesMolecular Docking Simulation010404 medicinal & biomolecular chemistryBiochemistryA549 CellsMolecular MedicineAllosteric SitePeptide HydrolasesProtein BindingJournal of Medicinal Chemistry
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Modulation of Hepatitis C Virus NS5A Hyperphosphorylation by Nonstructural Proteins NS3, NS4A, and NS4B

1999

NS5A of the hepatitis C virus (HCV) is a highly phosphorylated protein involved in resistance against interferon and required most likely for replication of the viral genome. Phosphorylation of this protein is mediated by a cellular kinase(s) generating multiple proteins with different electrophoretic mobilities. In the case of the genotype 1b isolate HCV-J, in addition to the basal phosphorylated NS5A (designated pp56), a hyperphosphorylated form (pp58) was found on coexpression of NS4A (T. Kaneko, Y. Tanji, S. Satoh, M. Hijikata, S. Asabe, K. Kimura, and K. Shimotohno, Biochem. Biophys. Res. Commun. 205:320‐326, 1994). Using a comparative analysis of two full-length genomes of genotype 1b…

virusesHepatitis C virusHepacivirusMolecular Sequence DataImmunologyGene ExpressionReplicationHyperphosphorylationGenome ViralHepacivirusViral Nonstructural Proteinsmedicine.disease_causeMicrobiologyCell LineInterferonCricetinaeVirologymedicineAnimalsHumansPhosphorylationNS5ANS3Base SequencebiologyPestivirusvirus diseasesRNAbiochemical phenomena metabolism and nutritionbiology.organism_classificationVirologyMolecular biologydigestive system diseasesAmino Acid SubstitutionInsect ScienceDNA Viralmedicine.drugJournal of Virology
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Recombinant virus-like particles as a carrier of B- and T-cell epitopes of hepatitis C virus (HCV)

2005

The major aim of the project was the development of virus-like particles (VLP) displaying B- and T-cell epitopes of hepatitis C virus (HCV) proteins. To this end, hepatitis B virus core (HBc) particles were used as a carrier of HCV epitopes. Fragments of HCV genes encoding core (aa 98) and NS3 (aa 155) proteins were fused to the 3' terminus of the truncated HBV core gene. All recombinant plasmids led to relatively high levels of expression of chimeric proteins in E. coli, which resulted in the formation of complete "mature" VLP. Chimeric HBc/HCV VLPs were purified by combination of gel filtration and sucrose gradient centrifugation, and used for immunogenicity studies in mice. All variants …

ImmunogenT-LymphocytesvirusesHepacivirusBiologyRecombinant virusEpitopeVirusEpitopesMiceVirus-like particleAnimalsCell ProliferationB-LymphocytesMice Inbred BALB CNS3General VeterinaryGeneral Immunology and MicrobiologyImmunogenicityVirionPublic Health Environmental and Occupational Healthvirus diseasesVirologyMolecular biologydigestive system diseasesHBcAgInfectious DiseasesMolecular MedicineElectrophoresis Polyacrylamide GelFemaleVaccine
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New developments in the management of hepatitis C virus infection: focus on boceprevir

2012

Chronic hepatitis C virus infection is an important public health problem, and the standard treatment (combination of pegylated interferon-α and ribavirin) has an effectiveness rate of only 40%-50%. Novel virus-specific drugs have recently been designed, and multiple compounds are under development. The approval for the clinical use of direct-acting antivirals in 2011 (boceprevir [BOC] and telaprevir, viral NS3 protease inhibitors) has increased recovery rates by up to 70%. Therefore, a highly effective treatment has been envisioned for the first time. This paper focuses on BOC and the implementation of new BOC-based treatment regimes.

viral resistanceNS3business.industryvirusesRibavirinHepatitis C virusStandard treatmentprotease inhibitorsReviewmedicine.disease_causeVirologyVirusTelaprevirchemistry.chemical_compoundchemistryBoceprevirHCVantiviral therapyMedicineEffective treatmentbusinessmedicine.drugBiologics: Targets and Therapy
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Determinants of Substrate Specificity in the NS3 Serine Proteinase of the Hepatitis C Virus

1997

AbstractProcessing of the nonstructural polyprotein of the hepatitis C virus (HCV) requires the serine-type proteinase located in the amino-terminal domain of NS3. To identify residues within NS3 determining substrate specificity, a mutation analysis was performed. Using sequence alignments and three-dimensional structure predictions, amino acids assumed to be important for specificity were replaced and the enzymes were tested in an intracellulartrans-processing assay for their effects on cleavage of an NS4B-5B substrate. For some of the substitutions at positions 133, 134, 135, 136, 138, 152, 155, 157, and 169, slightly reduced processing efficiencies were observed but in no case was the s…

Alaninechemistry.chemical_classificationModels MolecularNS3virusesMolecular Sequence DataHepacivirusBiologyViral Nonstructural ProteinsAmino acidSubstrate SpecificitySerinechemistryBiochemistryValineVirologyHumansAmino Acid SequenceThreonineLeucineIsoleucineSequence AlignmentVirology
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Replication of subgenomic hepatitis C virus RNAs in a hepatoma cell line.

1999

An estimated 170 million persons worldwide are infected with hepatitis C virus (HCV), a major cause of chronic liver disease. Despite increasing knowledge of genome structure and individual viral proteins, studies on virus replication and pathogenesis have been hampered by the lack of reliable and efficient cell culture systems. A full-length consensus genome was cloned from viral RNA isolated from an infected human liver and used to construct subgenomic selectable replicons. Upon transfection into a human hepatoma cell line, these RNAs were found to replicate to high levels, permitting metabolic radiolabeling of viral RNA and proteins. This work defines the structure of HCV replicons funct…

Carcinoma HepatocellularVirus CultivationvirusesHepatitis C virusDrug ResistanceGenome ViralHepacivirusBiologyViral Nonstructural Proteinsmedicine.disease_causeTransfectionVirus ReplicationViruschemistry.chemical_compoundmedicineTumor Cells CulturedHumansCloning MolecularNS5ANS5BSubgenomic mRNAGeneticsNS3MultidisciplinaryLiver NeoplasmsVirologyHepatitis CNS2-3 proteaseViral replicationchemistryRNA ViralRepliconGentamicinsScience (New York, N.Y.)
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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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Substrate determinants for cleavage in cis and in trans by the hepatitis C virus NS3 proteinase

1995

Processing of the hepatitis C virus polyprotein is accomplished by a series of cotranslational and posttranslational cleavages mediated by host cell signalases and two virally encoded proteinases. Of these the NS3 proteinase is essential for processing at the NS3/4A, NS4A/4B, NS4B/5A, and NS5A/5B junctions. Processing between NS3 and NS4A occurs in cis, implying an intramolecular reaction mechanism, whereas cleavage at the other sites can also be mediated in trans. Sequence analysis of the amino termini of mature cleavage products and comparisons of amino acid residues around the scissile bonds of various hepatitis C virus isolates identified amino acid residues which might contribute to su…

Cleavage factorvirusesMolecular Sequence DataImmunologyHepacivirusCleavage and polyadenylation specificity factorViral Nonstructural ProteinsBiologyCleavage (embryo)MicrobiologySubstrate SpecificityScissile bondVirologyHumansAmino Acid SequenceAmino AcidsPeptide sequencechemistry.chemical_classificationNS3Cleavage stimulation factorHydrolysisSerine Endopeptidasesbiochemical phenomena metabolism and nutritionAmino acidchemistryBiochemistryMutagenesisInsect ScienceProtein Processing Post-TranslationalRNA HelicasesHeLa CellsResearch ArticleJournal of Virology
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The Medicinal Chemistry of Zika Virus

2021

Arthropod-borne viruses, also known as arboviruses, are transmitted by bites of infected mosquito or tick vectors. In this context, the Flavivirus genus is mainly transmitted by mosquitoes from the Aedes genus, being the Ae. africanus, Ae. aegypti, and Ae. Albopictus species are responsible for transmitting the Zika virus (ZIKV). It is a lipid-enveloped virus constitute of an RNA genome, which is translated into a polyprotein encoding three structural proteins {(capsid (C), membrane (M), and envelope (E)} and seven non-structural proteins (NS1, NS2A, NS2B, NS3, NS4A, NS4B, and NS5). Several biological targets have been identified for developing antiviral agents against ZIKV, which could pre…

FlavivirusNS3biologyCapsidViral entryvirusesContext (language use)biology.organism_classificationMedicinal chemistryGenomeVirusZika virus
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