Search results for " cell surface"

showing 10 items of 154 documents

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 & 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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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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In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges

2020

Flexible spikes The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein enables viral entry into host cells by binding to the angiotensin-converting enzyme 2 (ACE2) receptor and is a major target for neutralizing antibodies. About 20 to 40 spikes decorate the surface of virions. Turoňová et al. now show that the spike is flexibly connected to the viral surface by three hinges that are well protected by glycosylation sites. The flexibility imparted by these hinges may explain how multiple spikes act in concert to engage onto the flat surface of a host cell. Science, this issue p. 203

In situElectron Microscope TomographyGlycanGlycosylationFlexibility (anatomy)virusesProtein domainPneumonia ViralHingeMolecular Dynamics SimulationBiologylaw.inventionBetacoronavirusProtein DomainslawTarget identificationmedicineHumansPandemicsResearch ArticlesHost cell surfaceMultidisciplinarySARS-CoV-2R-ArticlesCryoelectron MicroscopyBiochemCOVID-19MicrobioResearch HighlightCell biologymedicine.anatomical_structureSpike Glycoprotein Coronavirusbiology.proteinRecombinant DNASpike (software development)Protein MultimerizationStructural biologyCoronavirus InfectionsResearch ArticleScience (New York, N.y.)
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In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges

2020

AbstractThe spike (S) protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is required for cell entry and is the major focus for vaccine development. We combine cryo electron tomography, subtomogram averaging and molecular dynamics simulations to structurally analyze Sin situ. Compared to recombinant S, the viral S is more heavily glycosylated and occurs predominantly in a closed pre-fusion conformation. We show that the stalk domain of S contains three hinges that give the globular domain unexpected orientational freedom. We propose that the hinges allow S to scan the host cell surface, shielded from antibodies by an extensive glycan coat. The structure of native S contr…

In situHost cell surfaceGlycanFlexibility (anatomy)biologyChemistrySevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)HingeComputational biologymedicine.anatomical_structuremedicinebiology.proteinCryo-electron tomographySpike (software development)
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Binding analyses of Cry1Ab and Cry1Ac with membrane vesicles from Bacillus thuringiensis-resistant and -susceptible Ostrinia nubilalis.

2004

The binding properties of Bacillus thuringiensis toxins to brush border membrane vesicles of Dipel-resistant and -susceptible Ostrinia nubilalis larvae were compared using ligand-toxin immunoblot analysis, surface plasmon resonance (SPR), and radiolabeled toxin binding assays. In ligand-toxin immunoblot analysis, the number of Cry1Ab or Cry1Ac toxin binding proteins and the relative toxin binding intensity were similar in vesicles from resistant and susceptible larvae. Surface plasmon resonance with immobilized activated Cry1Ab toxin indicated that there were no significant differences in binding with fluid-phase vesicles from resistant and susceptible larvae. Homologous competition assays …

InsectaTime FactorsBrush borderBacterial ToxinsImmunoblottingBiophysicsBacillus thuringiensisReceptors Cell SurfacePlasma protein bindingBiologyMothsmedicine.disease_causeLigandsBiochemistryBinding CompetitiveCell membraneHemolysin ProteinsBacterial ProteinsBacillus thuringiensismedicineAnimalsBinding sitePest Control BiologicalMolecular BiologyBinding SitesBacillus thuringiensis ToxinsDose-Response Relationship DrugMicrovilliToxinVesiclefungiCell Membranefood and beveragesCell BiologySurface Plasmon Resonancebiology.organism_classificationMolecular biologyEndotoxinsKineticsmedicine.anatomical_structureCry1AcBiochemistryInsect ProteinsProtein BindingBiochemical and biophysical research communications
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