Search results for "Nonstructural proteins"

showing 10 items of 100 documents

Candidate Targets for Hepatitis C Virus-Specific Antiviral Therapy

1997

The hepatitis C virus (HCV) was identified as the major causative agent of posttransfusion and community-acquired non-A, non-B hepatitis throughout the world. It is an enveloped virus with a plus-strand RNA genome encoding a polyprotein of about 3,010 amino acids. This polyprotein is cleaved co- and posttranslationally into mature viral proteins by host cell signal peptidases and 2 viral enzymes designated the NS2-3 proteinase and the NS3/4A proteinase complex. It is assumed that virus replication takes place in a membrane-associated complex containing at least 2 viral enzymatic activities: the NS3 nucleoside triphosphatase (NTPase)/helicase and the NS5B RNA-dependent RNA polymerase (RdRp).…

Models MolecularvirusesHepatitis C virusHepacivirusViral Nonstructural ProteinsBiologyVirus Replicationmedicine.disease_causechemistry.chemical_compoundViral life cycleViral envelopeVirologyRNA polymeraseEndopeptidasesmedicineHumansNS5BNS3DNA Helicasesvirus diseasesRNAbiochemical phenomena metabolism and nutritionRNA-Dependent RNA PolymeraseVirologydigestive system diseasesCysteine EndopeptidasesInfectious DiseaseschemistryViral replicationIntervirology
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Interferon-alpha inhibits hepatitis C virus subgenomic RNA replication by an MxA-independent pathway.

2001

Hepatitis C virus (HCV) persists in the majority of infected individuals and is a major cause of chronic hepatitis, liver cirrhosis and hepatocellular carcinoma. Chronic hepatitis C is currently treated with interferon (IFN)-α or with a combination of IFN-α and ribavirin. The availability of an HCV replicon system (Lohmann et al., Science 285, 110–113, 1999) allowed the investigation of the effects of IFN on genuine HCV replication in cultured cells. It is shown here that IFN-α inhibits subgenomic HCV RNA replication in HuH-7 human hepatoma cells. Immunofluorescence, Western blot and Northern blot analysis revealed that levels of both HCV protein and replicon RNA were reduced after treatme…

Myxovirus Resistance ProteinsHepatitis C virusHepacivirusBiologyViral Nonstructural Proteinsmedicine.disease_causeAntiviral Agentschemistry.chemical_compoundInterferonGTP-Binding ProteinsVirologymedicineTumor Cells CulturedHumansRepliconNorthern blotSubgenomic mRNADose-Response Relationship DrugRibavirinvirus diseasesRNAInterferon-alphaProteinsVirologyMolecular biologydigestive system diseasesNS2-3 proteasechemistryRNA ViralRepliconmedicine.drugThe Journal of general 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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Combined Therapy of Interferon Plus Ribavirin Promotes Multiple Adaptive Solutions in Hepatitis C Virus

2009

Hepatitis C virus (HCV) presents several regions involved potentially in evading antiviral treatment and host immune system. Two regions, known as PKR-BD and V3 domains, have been proposed to be involved in resistance to interferon. Additionally, hypervariable regions in the envelope E2 glycoprotein are also good candidates to participate in evasion from the immune system. In this study, we have used a cohort of 22 non-responder patients to combined therapy (interferon alpha-2a plus ribavirin) for which samples obtained just before initiation of therapy and after 6 or/and 12 months of treatment were available. A range of 25-100 clones per patient, genome region and time sample were obtained…

PKR-BDHVR1HVR2HepacivirusHepatitis C virusMolecular Sequence DataHepacivirusInterferon alpha-2Viral Nonstructural Proteinsmedicine.disease_causeHVR3Antiviral AgentsViruschemistry.chemical_compoundImmune systemViral Envelope ProteinsInterferonVirologyDrug Resistance ViralRibavirinmedicineHumansAmino Acid SequenceTreatment FailureNS5AbiologyRibavirinInterferon-alphabiology.organism_classificationVirologyHepatitis CRecombinant ProteinsHypervariable regionInfectious DiseaseschemistryImmunologyMutationDrug Therapy CombinationV3 domainmedicine.drug
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Deciphering the Potential of Pre and Pro-Vitamin D of Mushrooms against Mpro and PLpro Proteases of COVID-19: An In Silico Approach

2022

Vitamin D’s role in combating the SARS-CoV-2 (severe acute respiratory syndrome coronavirus 2), the virus causing COVID-19, has been established in unveiling viable inhibitors of COVID-19. The current study investigated the role of pre and pro-vitamin D bioactives from edible mushrooms against Mpro and PLpro proteases of SARS-CoV-2 by computational experiments. The bioactives of mushrooms, specifically ergosterol (provitamin D2), 7-dehydrocholesterol (provitamin-D3), 22,23-dihydroergocalciferol (provitamin-D4), cholecalciferol (vitamin-D3), and ergocalciferol (vitamin D2) were screened against Mpro and PLpro. Molecular docking analyses of the generated bioactive protease complexes unr…

Pharmaceutical Scienceedible mushroomsMolecular Dynamics SimulationViral Nonstructural ProteinsAnalytical Chemistrypro-vitamin-DErgosterolDrug DiscoveryEndopeptidasespre-vitamin-DHumansProtease InhibitorsPhysical and Theoretical ChemistryVitamin DSARS-CoV-2Organic ChemistryProvitaminsin-silico studiesSettore CHIM/08 - Chimica FarmaceuticaCOVID-19 Drug TreatmentMolecular Docking SimulationChemistry (miscellaneous)Molecular MedicineAgaricalesedible mushrooms; SARS-CoV-2; pre-vitamin-D; pro-vitamin-D; in-silico studiesPeptide HydrolasesMolecules; Volume 27; Issue 17; Pages: 5620
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Human parvovirus B19 induced apoptotic bodies contain altered self-antigens that are phagocytosed by antigen presenting cells.

2013

Human parvovirus B19 (B19V) from the erythrovirus genus is known to be a pathogenic virus in humans. Prevalence of B19V infection has been reported worldwide in all seasons, with a high incidence in the spring. B19V is responsible for erythema infectiosum (fifth disease) commonly seen in children. Its other clinical presentations include arthralgia, arthritis, transient aplastic crisis, chronic anemia, congenital anemia, and hydrops fetalis. In addition, B19V infection has been reported to trigger autoimmune diseases such as systemic lupus erythematosus and rheumatoid arthritis. However, the mechanisms of B19V participation in autoimmunity are not fully understood. B19V induced chronic dise…

Programmed cell deathScienceAntigen-Presenting CellsArthritisApoptosisAutoimmunitySpodopteraViral Nonstructural ProteinsBiologymedicine.disease_causeAutoantigensVirusautoimmuniteettiImmune toleranceAutoimmunityParvoviridae InfectionsPathogenesis03 medical and health sciences0302 clinical medicineImmune systemPhagocytosisImmune ToleranceParvovirus B19 HumanSf9 CellsHuman Parvovirus B19medicineta319AnimalsHumansAntigen-presenting cellself-antigens030304 developmental biology0303 health sciencesMultidisciplinaryQta1182RHep G2 CellsFlow Cytometrymedicine.diseaseVirology3. Good healthImmunologyMicroscopy Electron ScanningMedicineResearch Article030215 immunologyPLoS ONE
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Hepatitis C Virus NS3/4A Protease Inhibitors.

2008

Chronic hepatitis C virus infection is a global problem worldwide due to the lack of an effective therapy (the current standard of care treatment is effective in about 40-50% of the cases), and the difficulties in developing a protective vaccine. Chronic infection progresses to end-stage liver disease and liver failure in a considerable number of infected individuals. Once liver function is compromised, the only reliable therapeutic intervention is liver transplantation. Unfortunately, re-infection of the graft is unavoidable, and a new chronic hepatitis is early established in transplant recipients, that can result in graft loss. Thus, there is an urgent need for new, specifically targeted…

ProlineHepatitis B virus DNA polymerasevirusesmedicine.medical_treatmentHepacivirusLiver transplantationViral Nonstructural ProteinsAntiviral AgentsLiver diseaseDrug DiscoveryDrug Resistance ViralmedicinePharmacology (medical)NS3Proteasebusiness.industryvirus diseasesGeneral Medicinemedicine.diseasedigestive system diseasesNS2-3 proteaseChronic infectionInfectious DiseasesImmunologyLiver functionbusinessOligopeptidesRecent patents on anti-infective drug discovery
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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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SAR of novel benzothiazoles targeting an allosteric pocket of DENV and ZIKV NS2B/NS3 proteases

2021

In recent years, dengue virus (DENV) and Zika virus (ZIKV), both mosquito-borne members of the Flaviviridae family, have emerged as intercontinental health issues since their vectors have spread from their tropical origins to temperate climate zones due to climate change and increasing globalization. DENV and ZIKV are positive-sense, single-stranded RNA viruses, whose genomes consist of three structural (capsid, membrane precursor, envelope) and seven non-structural (NS) proteins, all of which are initially expressed as a single precursor polyprotein. For virus maturation, the polyprotein processing is accomplished by host proteases and the viral NS2B/NS3 protease complex, whose inhibitors …

Proteasesvirusesmedicine.medical_treatmentClinical BiochemistryAllosteric regulationPharmaceutical ScienceViral Nonstructural ProteinsDengue virusmedicine.disease_causeBiochemistryStructure-Activity RelationshipViral ProteinsFlaviviridaeAllosteric RegulationDrug DiscoveryVirus maturationmedicineHumansProtease InhibitorsBenzothiazolesMolecular BiologyNS3ProteaseDose-Response Relationship DrugMolecular StructurebiologyChemistrySerine EndopeptidasesOrganic Chemistrybiochemical phenomena metabolism and nutritionbiology.organism_classificationVirologyCapsidMolecular MedicineBioorganic & Medicinal Chemistry
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Complex formation between the NS3 serine-type proteinase of the hepatitis C virus and NS4A and its importance for polyprotein maturation

1995

Processing of the hepatitis C virus polyprotein is mediated by host cell signalases and at least two virally encoded proteinases. Of these, the serine-type proteinase encompassing the amino-terminal one-third of NS3 is responsible for cleavage at the four sites carboxy terminal of NS3. The activity of this proteinase is modulated by NS4A, a 54-amino-acid polyprotein cleavage product essential for processing at the NS3/4A, NS4A/4B, and NS4B/5A sites and enhancing cleavage efficiency between NS5A and NS5B. Using the vaccinia virus-T7 hybrid system to express hepatitis C virus polypeptides in BHK-21 cells, we studied the role of NS4A in proteinase activation. We found that the NS3 proteinase a…

Protein ConformationRecombinant Fusion ProteinsvirusesGenetic VectorsMolecular Sequence DataImmunologyVaccinia virusHepacivirusProtein Sorting SignalsViral Nonstructural ProteinsBiologyKidneyTransfectionCleavage (embryo)MicrobiologyAntibodiesCell LineSerineEpitopesViral Proteinschemistry.chemical_compoundProtein structureProteinase 3CricetinaeVirologyAnimalsAmino Acid SequenceProtein PrecursorsNS5BPeptide sequenceNS3Sequence Homology Amino AcidSerine Endopeptidasesvirus diseasesbiochemical phenomena metabolism and nutritiondigestive system diseasesNS2-3 proteaseBiochemistrychemistryInsect ScienceProtein Processing Post-TranslationalAlgorithmsRNA HelicasesResearch ArticleJournal of Virology
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