Search results for "Cell Surface"

showing 10 items of 201 documents

Polyalbumin receptors, hepatitis B surface antigen (HBsAg), and HBsAg/IgM complexes in HBsAg positive patients with and without delta superinfection.

1985

Receptors for polymerized human albumin are found at high litres during high-level hepatitis B virus (HBV) replication and in small amounts in chronic low-level infection. Complexes between hepatitis B surface antigen (HBsAg) and IgM without specificity for HbsAg are expressed in a pattern similar to that of receptors. Anti-albumin antibodies could be involved in their formation. Delta infection depresses the synthesis of gene products of HBV. To assess whether delta modifies the expression of receptors on HBsAg and the level of HBsAg/IgM complexes, and if anti-albumin antibodies are actually part of the complex, we tested sera from 86 subjects with acute and chronic HBV infection. Our find…

HBsAgRadioimmunoassayEnzyme-Linked Immunosorbent AssayReceptors Cell SurfaceSerum Albumin HumanAntigen-Antibody ComplexHepatitis b surface antigenmedicine.disease_causeVirologymedicineHumansReceptorSerum AlbuminHepatitis B virusHepatitis B Surface AntigensbiologyAlbuminvirus diseasesReceptors AlbuminHepatitis BVirologydigestive system diseasesTiterInfectious DiseasesViral replicationImmunoglobulin MImmunologyAcute DiseaseChronic Diseasebiology.proteinAntibodyJournal of medical virology
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Reduced membrane-bound alkaline phosphatase does not affect binding of Vip3Aa in a Heliothis virescens resistant colony

2020

The Vip3Aa insecticidal protein from Bacillus thuringiensis (Bt) is produced by specific transgenic corn and cotton varieties for efficient control of target lepidopteran pests. The main threat to this technology is the evolution of resistance in targeted insect pests and understanding the mechanistic basis of resistance is crucial to deploy the most appropriate strategies for resistance management. In this work, we tested whether alteration of membrane receptors in the insect midgut might explain the &gt

HELIOTHIS-VIRESCENSInsecticidesHealth Toxicology and Mutagenesislcsh:MedicinePROTEIN0601 Biochemistry and Cell BiologyToxicologyBiotecnologiaInsecticide ResistanceBacillus thuringiensisSITES0303 health sciencesbiologyChemistryfood and beveragesPlants Genetically ModifiedLepidopteraBiochemistryFood Science & TechnologyInsect ProteinsAlkaline phosphatase1115 Pharmacology and Pharmaceutical Sciencestobacco budwormLife Sciences & BiomedicineSPODOPTERA-FRUGIPERDA MIDGUTProtein BindingEXPRESSIONBrush borderBacillus thuringiensisCRY1ACArticleVESICLES03 medical and health sciencesBACILLUS-THURINGIENSISBacterial ProteinsDownregulation and upregulationinsecticidal proteinsCell surface receptor<i>Bacillus thuringiensis</i>AnimalsCROPS030304 developmental biologyScience & TechnologyGenetically modified maizeHeliothis virescens030306 microbiologylcsh:RfungiMembrane ProteinsMidgutAlkaline Phosphatasebiology.organism_classificationTOXIN RESISTANCEinsect resistanceProteïnes
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Isolation of a hemin and hemoglobin binding outer membrane protein of Vibrio vulnificus biotype 2 (serogroup E)

2006

The eel pathogen Vibrio vulnificus biotype 2 (serogroup E) is able to use hemin (Hm) or hemoglobin (Hb) as the sole iron source for growth in vitro and in vivo. The mechanism of heme-iron acquisition in this bacterium requires a direct interaction through binding sites on the bacterial surface (constitutive outer membrane proteins). Using affinity chromatography techniques, a unique protein of around 36.5 kDa was isolated from cell envelopes of E86 strain regardless of the affinity ligand used, hemoglobin or hemin. This protein was purified from both iron-enriched and iron-restricted grown cells. These results support the hypothesis that in this pathogen Hm- and Hb-iron acquisition is media…

Hemoglobin bindingIronBlotting WesternReceptors Cell SurfaceVibrio vulnificusBiologyMicrobiologyMicrobiologyHemoglobinschemistry.chemical_compoundAffinity chromatographyGeneticsBinding siteMolecular BiologyHemeVibrioSepharosebiology.organism_classificationchemistryBiochemistryHeminHemoglobinBacterial outer membraneBacterial Outer Membrane ProteinsChromatography LiquidProtein BindingHeminFEMS Microbiology Letters
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The asialoglycoprotein receptor mediates hepatic binding and uptake of natural hepatitis B virus particles derived from viraemic carriers.

1994

As a putative mechanism of hepatitis B virus (HBV) uptake into hepatocytes the interaction between HBV and the hepatic, human-derived asialoglycoprotein receptor (ASGPR) was investigated. Sera from patients with different variations of hepatitis B surface antigen-(HBsAg) positive chronic hepatitis, HBV particles isolated from HBV carriers with high-titre viraemia and commercial HBsAg served as sources of HBV. ASGPR was affinity-purified from human liver. HBV that had bound to isolated ASGPR was either detected by radio-immunoassay using solid-phase bound ASGPR or enzyme immunoassay with biotin-ASGPR bound to immobilized HBV. Furthermore, binding and uptake of purified, 125I-labelled HBV par…

HepatoblastomaHBsAgHepatitis B virusCarcinoma HepatocellularAsialoglycoproteinsReceptors Cell SurfaceAsialoglycoprotein Receptormedicine.disease_causeBinding CompetitiveVirusVirologymedicineTumor Cells CulturedHumansHepatitis B e AntigensViremiaBinding siteHepatitis B virusCOS cellsHepatitis B Surface AntigensbiologyCell MembraneLiver Neoplasmsvirus diseasesBlood ProteinsHepatitis Bmedicine.diseaseHepatitis BVirologyMolecular biologydigestive system diseasesLiverAcute DiseaseCarrier StateChronic Diseasebiology.proteinReceptors VirusAsialoglycoprotein receptorAntibodyThe Journal of general virology
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Autophagy, cathepsin L transport, and acidification in cultured rat fibroblasts.

1992

The mechanisms of enzyme delivery to and acidification of early autophagic vacuoles in cultured fibroblasts were elucidated by cryoimmunoelectron microscopic methods. The cation-independent mannose-6-phosphate receptor (MPR) was used as a marker of the pre-lysosomal compartment, and cathepsin L and an acidotropic amine (3-(2,4-dinitroanilino)-3'-amino-N-methyl-dipropylamine (DAMP), a cytochemical probe for low-pH organelles) as markers of both pre-lysosomal and lysosomal compartments. In addition, cationized ferritin was used as an endocytic marker. In ultrastructural double labeling experiments, the bulk of all the antigens was found in vesicles containing tightly packed membrane material…

HistologyCathepsin LEndocytic cycleFluorescent Antibody TechniqueReceptors Cell SurfaceVacuoleReceptor IGF Type 2Cathepsin LEndopeptidasesOrganelleAutophagyAnimalsMicroscopy ImmunoelectronCells CulturedCathepsinMannosephosphatesbiologyVesicleBiological TransportFibroblastsHydrogen-Ion ConcentrationCathepsinsRatsCell biologyFerritinCysteine EndopeptidasesDinitrobenzenesBiochemistryCytoplasmbiology.proteinAnatomyJournal of Histochemistry &amp; Cytochemistry
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Sodium Solute Symporter and Cadherin Proteins Act as Bacillus thuringiensis Cry3Ba Toxin Functional Receptors in Tribolium castaneum*

2013

Understanding how Bacillus thuringiensis (Bt) toxins interact with proteins in the midgut of susceptible coleopteran insects is crucial to fully explain the molecular bases of Bt specificity and insecticidal action. In this work, aminopeptidase N (TcAPN-I), E-cadherin (TcCad1), and sodium solute symporter (TcSSS) have been identified by ligand blot as putative Cry3Ba toxin-binding proteins in Tribolium castaneum (Tc) larvae. RNA interference knockdown of TcCad1 or TcSSS proteins resulted in decreased susceptibility to Cry3Ba toxin, demonstrating the Cry toxin receptor functionality for these proteins. In contrast, TcAPN-I silencing had no effect on Cry3Ba larval toxicity, suggesting that th…

ImmunoblottingMolecular Sequence DataReceptors Cell SurfacePlasma protein bindingBiologyCD13 Antigensmedicine.disease_causeBiochemistrySodium-solute symporterdigestive systemMicrobiologyEpitopesHemolysin ProteinsBacterial ProteinsBacillus thuringiensisparasitic diseasesmedicineAnimalsAmino Acid SequenceReceptorMolecular BiologyPeptide sequenceTriboliumBinding SitesBacillus thuringiensis ToxinsSequence Homology Amino AcidSymportersCadherinToxinfungiSodiumCell Biologybiology.organism_classificationCadherinsEndotoxinsBiochemistrySymporterbacteriaInsect ProteinsRNA InterferenceProtein Binding
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Selective Uptake of Cylindrical Poly(2-Oxazoline) Brush-AntiDEC205 Antibody-OVA Antigen Conjugates into DEC-Positive Dendritic Cells and Subsequent T…

2014

To achieve specific cell targeting by various receptors for oligosaccharides or antibodies, a carrier must not be taken up by any of the very many different cells and needs functional groups prone to clean conjugation chemistry to derive well-defined structures with a high biological specificity. A polymeric nanocarrier is presented that consists of a cylindrical brush polymer with poly-2-oxazoline side chains carrying an azide functional group on each of the many side chain ends. After click conjugation of dye and an anti-DEC205 antibody to the periphery of the cylindrical brush polymer, antibody-mediated specific binding and uptake into DEC205(+) -positive mouse bone marrow-derived dendri…

ImmunoconjugatesOvalbuminPolymersT-LymphocytesT cellMolecular Sequence DataReceptors Cell SurfacePeptideLymphocyte ActivationCatalysisMinor Histocompatibility AntigensMicechemistry.chemical_compoundAntigenAntigens CDmedicineSide chainAnimalsLectins C-TypeAmino Acid SequenceReceptorOxazolesCells Culturedchemistry.chemical_classificationbiologyOrganic ChemistryDendritic CellsGeneral Chemistrymedicine.anatomical_structurechemistryBiochemistrybiology.proteinBiophysicsAzideAntibodyConjugateChemistry - A European Journal
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Myxoma virus Leukemia-associated protein is responsible for major histocompatibility complex class I and Fas-CD95 down-regulation and defines scrapin…

2002

ABSTRACTDown-modulation of major histocompatibility class I (MHC-I) molecules is a viral strategy for survival in the host.Myxoma virus, a member of thePoxviridaefamily responsible for rabbit myxomatosis, can down-modulate the expression of MHC-I molecules, but the viral factor(s) has not been described. We cloned and characterized a gene coding for an endoplasmic reticulum (ER)-resident protein containing an atypical zinc finger and two transmembrane domains, which we called myxoma virus leukemia-associated protein (MV-LAP). MV-LAP down-regulated surface MHC-I and Fas-CD95 molecules upon transfection; the mechanism probably involves an exacerbation of endocytosis and was lost when the ER r…

ImmunologyMolecular Sequence DataDown-RegulationMyxoma virusReceptors Cell SurfaceMajor histocompatibility complexEndoplasmic ReticulumMicrobiologyVirusCell Line03 medical and health sciencesViral ProteinsMyxomatosis InfectiousVirologymedicineAnimalsFACTEUR VIRALPoxviridaeAGRONOMIEAmino Acid Sequencefas ReceptorComputingMilieux_MISCELLANEOUS030304 developmental biology[SDV.MP.VIR] Life Sciences [q-bio]/Microbiology and Parasitology/Virology0303 health sciencesBIOTECHNOLOGIEMyxomatosisbiologyBase SequenceVirulence030302 biochemistry & molecular biologyHistocompatibility Antigens Class IMyxoma virusMembrane ProteinsER retentionSequence Analysis DNAbiology.organism_classificationmedicine.diseaseVirology3. Good healthCTL*Lytic cycleInsect Science[SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virologybiology.proteinPathogenesis and ImmunityReceptors VirusRabbitsT-Lymphocytes Cytotoxic
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A central role for Notch in effector CD8(+) T cell differentiation.

2014

Activated CD8(+) T cells choose between terminal effector cell (TEC) or memory precursor cell (MPC) fates. We found that the signaling receptor Notch controls this 'choice'. Notch promoted the differentiation of immediately protective TECs and was correspondingly required for the clearance of acute infection with influenza virus. Notch activated a major portion of the TEC-specific gene-expression program and suppressed the MPC-specific program. Expression of Notch was induced on naive CD8(+) T cells by inflammatory mediators and interleukin 2 (IL-2) via pathways dependent on the metabolic checkpoint kinase mTOR and the transcription factor T-bet. These pathways were subsequently amplified d…

ImmunologyNotch signaling pathwayMice TransgenicCell SeparationBiologyAdaptive ImmunityCD8-Positive T-LymphocytesEffector cellLymphocyte ActivationReal-Time Polymerase Chain ReactionArticlememoryMiceOrthomyxoviridae InfectionsCell surface receptorT-Lymphocyte SubsetsTransduction GeneticPrecursor cellImmunology and AllergyCytotoxic T cellAnimalsGeneticsReceptors NotchEffectorCell DifferentiationFlow CytometryAdoptive TransferTEC3. Good healthCell biologyMice Inbred C57BLeffectorCD8 T cellMPCInfluenza A virusinflammationTranscriptomeCD8Nature immunology
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Human Siglec-10 can bind to vascular adhesion protein-1 and serves as its substrate

2009

AbstractLeukocytes migrate from the blood into areas of inflammation by interacting with various adhesion molecules on endothelial cells. Vascular adhesion protein-1 (VAP-1) is a glycoprotein expressed on inflamed endothelium where it plays a dual role: it is both an enzyme that oxidizes primary amines and an adhesin that is involved in leukocyte trafficking to sites of inflammation. Although VAP-1 was identified more than 15 years ago, the counterreceptor(s) for VAP-1 on leukocytes has remained unknown. Here we have identified Siglec-10 as a leukocyte ligand for VAP-1 using phage display screenings. The binding between Siglec-10 and VAP-1 was verified by different adhesion assays, and this…

ImmunologyReceptors Cell SurfaceInflammationCHO CellsPlasma protein bindingBiologyLigandsBiochemistryMice03 medical and health sciencesCricetulus0302 clinical medicinePeptide LibraryVascular BiologyCricetinaeLectinsLeukocyte TraffickingCell AdhesionmedicineAnimalsHumansEndotheliumLymphocytesProtein Structure QuaternaryCell adhesion030304 developmental biologyMice Knockout0303 health sciencesCell adhesion moleculeSoluble cell adhesion moleculesSIGLECCell BiologyHematologyAdhesionrespiratory systembacterial infections and mycosesRecombinant Proteinsrespiratory tract diseasesChemotaxis LeukocyteBiochemistry030220 oncology & carcinogenesisAmine Oxidase (Copper-Containing)medicine.symptomCell Adhesion MoleculesProtein BindingBlood
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