Search results for "Envelope protein"

showing 10 items of 99 documents

Sulphoevernan, a polyanionic polysaccharide, and the narcissus lectin potently inhibit human immunodeficiency virus infection by binding to viral env…

1990

Sulphoevernan is a sulphated alpha-1----3, 1----4 polyglucan (Mr 20,000) with a helical structure. This compound effectively inhibits both human immunodeficiency virus type 1 (HIV-1) and type 2 infection of cells in vitro at concentrations around 0.5 micrograms/ml. Moreover, the compound completely inhibits HIV-1-induced syncytium formation at a concentration of 1 microgram/ml. Competition experiments with 35S-labelled sulphoevernan revealed that the mannose-specific lectin from Narcissus pseudonarcissus prevented binding of sulphoevernan to HIV-1, whereas the antibody OKT4A did not reduce the amount of sulphoevernan bound to MT-2 cells. These data indicate that the non-cytotoxic polymer su…

Antiviral AgentsVirusCell LineViral envelopeViral Envelope ProteinsIn vivoPolysaccharidesVirologyLectinsMurine leukemia virusHumansGlucansSyncytiumbiologyLectinbiology.organism_classificationVirologyIn vitroHIV-2biology.proteinHIV-1AntibodyPlant LectinsZidovudineCell DivisionProtein BindingThe Journal of general virology
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DNA-mediated immunization to hepatitis B virus envelope proteins: preS antigen secretion enhances the humoral response.

1999

In order to design optimized DNA vectors as genetic vaccines against infections with the hepatitis B virus (HBV) we investigated if secretion or retention of the viral antigens has an influence on the quality and quantity of the humoral immune response. Intramuscular injection of plasmid DNA encoding the HBV large L envelope protein, known to be retained within host cells, induced only a weak response in mice whereas a vector expressing the secretion-competent small S envelope protein elicited strong and sustained immunity. Immunization with rearranged envelope genes further demonstrated that secretion affects the magnitude of the immune response. In situ expression of modified small and mi…

Biologymedicine.disease_causeEpitopeVirusMiceImmune systemAntigenAdjuvants ImmunologicViral Envelope ProteinsmedicineVaccines DNAAnimalsHepatitis B VaccinesHepatitis B AntibodiesProtein PrecursorsHepatitis B virusMice Inbred BALB CHepatitis B Surface AntigensGeneral VeterinaryGeneral Immunology and MicrobiologyImmunogenicityPublic Health Environmental and Occupational HealthVirologyMolecular biologyInfectious DiseasesHumoral immunityCOS Cellsbiology.proteinMolecular MedicineFemaleAntibodyVaccine
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Membrane topology of gp41 and amyloid precursor protein: Interfering transmembrane interactions as potential targets for HIV and Alzheimer treatment

2009

AbstractThe amyloid precursor protein (APP), that plays a critical role in the development of senile plaques in Alzheimer disease (AD), and the gp41 envelope protein of the human immunodeficiency virus (HIV), the causative agent of the acquired immunodeficiency syndrome (AIDS), are single-spanning type-1 transmembrane (TM) glycoproteins with the ability to form homo-oligomers. In this review we describe similarities, both in structural terms and sequence determinants of their TM and juxtamembrane regions. The TM domains are essential not only for anchoring the proteins in membranes but also have functional roles. Both TM segments contain GxxxG motifs that drive TM associations within the li…

BiophysicsHIV InfectionsBiologyGp41BiochemistryArticleTransmembrane segmentAmyloid beta-Protein PrecursorMembranes (Biologia)Alzheimer DiseaseAmyloid precursor proteinAnimalsHumansSenile plaqueschemistry.chemical_classificationCell MembraneMembraneHIVCell Biologygp41HIV Envelope Protein gp41Transmembrane proteinVirusCell biologyTransmembrane domainchemistryBiochemistryAmyloid precursor proteinMembrane topologyAlzheimerHIV-1biology.proteinGlycoproteinSequence motifBiochimica et Biophysica Acta (BBA) - Biomembranes
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T-cell receptor transfer into human T cells with ecotropic retroviral vectors

2014

Adoptive T-cell transfer for cancer immunotherapy requires genetic modification of T cells with recombinant T-cell receptors (TCRs). Amphotropic retroviral vectors (RVs) used for TCR transduction for this purpose are considered safe in principle. Despite this, TCR-coding and packaging vectors could theoretically recombine to produce replication competent vectors (RCVs), and transduced T-cell preparations must be proven free of RCV. To eliminate the need for RCV testing, we transduced human T cells with ecotropic RVs so potential RCV would be non-infectious for human cells. We show that transfection of synthetic messenger RNA encoding murine cationic amino-acid transporter 1 (mCAT-1), the re…

CD4-Positive T-LymphocytesAdoptive cell transfermedicine.medical_treatmentGenetic enhancementGenetic VectorsReceptors Antigen T-CellCD8-Positive T-LymphocytesBiologyImmunotherapy AdoptiveJurkat cellsVesicular stomatitis Indiana virusCell LineJurkat CellsMiceTransduction (genetics)Viral Envelope ProteinsCancer immunotherapyTransduction GeneticGeneticsmedicineAnimalsHumansRNA MessengerMolecular BiologyCationic Amino Acid Transporter 1Membrane GlycoproteinsHEK 293 cellsT-cell receptorTransfectionAdoptive TransferVirologyElectroporationHEK293 CellsRetroviridaeLeukemia Virus Gibbon ApeMolecular MedicinePlasmidsGene Therapy
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Inhibition of human immunodeficiency virus-1 infection by human conglutinin-like protein: in vitro studies.

1992

The lectin-like protein analogous to bovine conglutinin was purified from human serum. The carbohydrate-binding ability of conglutinin-like protein was inhibited by D-mannose, N-acetylglucosamine and L-fucose as well as by mannan-containing oligosaccharides. By applying a lectin-based ELISA system it was demonstrated that conglutinin-like protein binds to human immunodeficiency virus-1 (HIV-1) glycoprotein 120 (gp120) via its carbohydrate binding site. In vitro experiments with T-lymphoblastoid CEM cells revealed that conglutinin-like protein abolishes infection by HIV-1; a 50% cytoprotective concentration of 23.9 micrograms/ml was measured. These findings demonstrate that human conglutinin…

Cancer ResearchMolecular Sequence DataCarbohydratesImmunoglobulinsEnzyme-Linked Immunosorbent AssayHIV Envelope Protein gp120Mannose-Binding LectinVirusChromatography AffinityArticleViral ProteinsConglutininProtein A/GHumansImmunoconglutininsBinding siteKey wordsConglutinin‐like proteinchemistry.chemical_classificationAcquired Immunodeficiency SyndromebiologyHIV‐1Immunization PassiveLectinMolecular biologyMannanIn vitrogp120OncologychemistryCarbohydrate Sequencebiology.proteinHIV-1Protein GGlycoproteinCarrier ProteinsLectinJapanese journal of cancer research : Gann
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Protein targeting to the plasma membrane of adult skeletal muscle fiber: an organized mosaic of functional domains.

2001

The plasma membrane of differentiated skeletal muscle fibers comprises the sarcolemma, the transverse (T) tubule network, and the neuromuscular and muscle-tendon junctions. We analyzed the organization of these domains in relation to defined surface markers, beta-dystroglycan, dystrophin, and caveolin-3. These markers were shown to exhibit highly organized arrays along the length of the fiber. Caveolin-3 and beta-dystroglycan/dystrophin showed distinct, but to some extent overlapping, labeling patterns and both markers left transverse tubule openings clear. This labeling pattern revealed microdomains over the entire plasma membrane with the exception of the neuromuscular and muscle-tendon j…

Caveolin 3Muscle Fibers SkeletalNeuromuscular JunctionMuscle ProteinsProtein Sorting Signalsmedicine.disease_causeCaveolinsT-tubuleDystrophinMiceMembrane MicrodomainsViral Envelope ProteinsProtein targetingmedicineMyocyteAnimalsDystroglycansMuscle SkeletalGlycoproteinsSarcolemmaMembrane GlycoproteinsbiologyCell MembraneSkeletal muscleCell BiologyMolecular biologyTransport proteinCell biologyRatsCytoskeletal ProteinsProtein Transportmedicine.anatomical_structureTubulebiology.proteinFemaleDystrophinExperimental cell research
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Two mutations in gB-1 and gD-1 of herpes simplex virus type 1 are involved in the "fusion from without" phenotype in different cell types.

1996

Previous studies have shown that certain strains of herpes simplex viruses type 1 (HSV-1) are able to induce “fusion from without” (FFWO) which means no transcription or translation of the viral genome happens. The main determinants for FFWO in BHK cells are mutations in the C-terminal part of gB-1. But single mutations in this part of the genome are not sufficient to transfer the FFWO phenotype also to Vero cells. Here, we report that FFWO of HSV strains indeed need additional mutations in the N-terminal part of gD in order to produce the FFWO phenotype in BHK and Vero cells. By marker transfer we are able to show that loss of mutations in the N-terminal part of gD influences the ability t…

Cell typevirusesCellMolecular Sequence DataGenome ViralHerpesvirus 1 HumanBiologymedicine.disease_causeTransfectionGiant CellsVirusCell LineViral Envelope ProteinsTranscription (biology)VirologyCricetinaeChlorocebus aethiopsGeneticsmedicineBaby hamster kidney cellAnimalsHumansAmino Acid SequenceMolecular BiologyVero CellsBase SequenceGeneral MedicineVirologyPhenotypemedicine.anatomical_structureHerpes simplex virusPhenotypeDNA ViralMutationVero cellVirus genes
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Hexapeptides that interfere with HIV-1 fusion peptide activity in liposomes block GP41-mediated membrane fusion

2006

AbstractUpon receptor-mediated activation, the gp41 hydrophobic, conserved fusion peptide inserts into the target membrane and promotes the kind of perturbations required for the progression of the HIV-cell fusion reaction. Using a synthetic combinatorial library we have identified all d-amino acid hexapeptide sequences that inhibited the fusion peptide capacity of perturbing model membranes. Two hexapeptides that effectively inhibited the fusion peptide in these systems were subsequently shown to inhibit cell–cell fusion promoted by gp41 expressed at cell surfaces. These observations might be of importance for understanding the mechanisms underlying fusion peptide activity and suggest new …

CellBiophysicsMembrane fusionCHO CellsGp41BiochemistryFusion peptideMembranes (Biologia)Structural BiologyCricetinaeGeneticsmedicineNuclear fusionAnimalsMolecular BiologyFusion inhibitorFusionLiposomeChemistryLipid bilayer fusionViral fusionCell Biologygp41HIV Envelope Protein gp41Cell biologyMembranemedicine.anatomical_structureBiochemistryLiposomesHIV-1PèptidsPeptidesFusion peptide
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Presentation of an Immunodominant Immediate-Early CD8+ T Cell Epitope Resists Human Cytomegalovirus Immunoevasion.

2013

Control of human cytomegalovirus (HCMV) depends on CD8+ T cell responses that are shaped by an individual's repertoire of MHC molecules. MHC class I presentation is modulated by a set of HCMV-encoded proteins. Here we show that HCMV immunoevasins differentially impair T cell recognition of epitopes from the same viral antigen, immediate-early 1 (IE-1), that are presented by different MHC class I allotypes. In the presence of immunoevasins, HLA-A- and HLA-B-restricted T cell clones were ineffective, but HLA-C*0702-restricted T cell clones recognized and killed infected cells. Resistance of HLA-C*0702 to viral immunoevasins US2 and US11 was mediated by the alpha3 domain and C-terminal region …

Cytomegalovirus InfectionMaleViral DiseasesvirusesCytomegalovirusEpitopes T-LymphocyteNK cellsAdaptive ImmunityCD8-Positive T-LymphocytesMajor Histocompatibility ComplexInterleukin 21Viral Envelope ProteinsCytotoxic T celllcsh:QH301-705.5Antigen PresentationbiologyViral Immune EvasionImmune cellsRNA-Binding ProteinsInnate ImmunityKiller Cells Naturalmedicine.anatomical_structureInfectious DiseasesCytomegalovirus InfectionsMedicineFemaleResearch Articlelcsh:Immunologic diseases. AllergyT cellImmunologyCD1T cells610StreptamerMicrobiologyImmediate-Early ProteinsImmunomodulationViral ProteinsVirologyMHC class IGeneticsmedicineHumansAntigen-presenting cellMolecular BiologyBiologyImmune EvasionHistocompatibility Antigens Class IImmunityMHC restrictionVirologyProtein Structure Tertiarylcsh:Biology (General)Immunologybiology.proteinParasitologylcsh:RC581-607
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Cloning and expression of the complement receptor glycoprotein C from Herpesvirus simiae (herpes B virus): protection from complement-mediated cell l…

2003

Simian herpes B virus (SHBV) is the herpes simplex virus (HSV) homologue for the species MACACA: Unlike in its natural host, and unlike other animal herpesviruses, SHBV causes high mortality in accidentally infected humans. SHBV-infected cells, like those infected with HSV-1 and equine herpesvirus types 1 and 4, express complement C3 receptor activity. To study immunoregulatory functions involved in susceptibility/resistance against interspecies transmission, the SHBV glycoprotein C (gC(SHBV)) gene (encoding 467 aa) was isolated. Sequence analysis revealed amino acid identity with gC proteins from HSV-2 (46.9 %), HSV-1 (44.5 %) and pseudorabies virus (21.2 %). Highly conserved cysteine resi…

Cytotoxicity ImmunologicHerpes B virusvirusesComplement Pathway AlternativeMolecular Sequence DataHerpesvirus 1 CercopithecineComplement receptorBiologyTransfectionmedicine.disease_causeVirusCell LineViral Envelope ProteinsVirologymedicineAnimalsHumansAmino Acid SequenceCloning MolecularPeptide sequenceSequence Analysis DNAbiology.organism_classificationVirologyComplement systemHerpes simplex virusCell cultureComplement C3bReceptors Complement 3bAlternative complement pathwayJournal of General Virology
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