Search results for "Staphylococcal protein"

showing 7 items of 7 documents

Protein�A immunoadsorption therapy for refractory, mitomycin�C?associated thrombotic microangiopathy

2007

BACKGROUND: Mitomycin C–associated thrombotic microangiopathy (TMA) has a poor prognosis with limited therapeutic options. Most patients die within 4 months of diagnosis due to pulmonary or renal failure. Here, a patient resistant to total plasma exchange (TPE) and immunosuppressive therapy with glucocorticoids, rituximab, vincristine, and splenectomy who was successfully treated with protein A immunoadsorption is described. CASE REPORT: A 29-year-old woman developed a TMA after chemotherapy with mitomycin C. She presented with thrombocytopenia, pulmonary edema, hemolytic anemia with presence of schistocytes, and renal failure. Immediate TPE (>120 times) and immunosuppressive therapy with g…

AdultHemolytic anemiamedicine.medical_specialtyThrombotic microangiopathyMitomycinmedicine.medical_treatmentImmunologySplenectomyGastroenterologyInternal medicinemedicineHumansImmunology and AllergyStaphylococcal Protein AImmunoadsorptionImmunosorbent TechniquesSalvage TherapyChemotherapyPurpura Thrombotic Thrombocytopenicbusiness.industryImmunosuppressionHematologymedicine.diseaseSurgerySchistocyteTreatment OutcomeHemolytic-Uremic SyndromeFemaleRituximabbusinessmedicine.drugTransfusion
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Experimental Study of the Oriented Immobilization of Antibodies on Photonic Sensing Structures by Using Protein A as an Intermediate Layer

2018

[EN] A proper antibody immobilization on a biosensor is a crucial step in order to obtain a high sensitivity to be able to detect low target analyte concentrations. In this paper, we present an experimental study of the immobilization process of antibodies as bioreceptors on a photonic ring resonator sensor. A protein A intermediate layer was created on the sensor surface in order to obtain an oriented immobilization of the antibodies, which enhances the interaction with the target antigens to be detected. The anti-bovine serum albumin (antiBSA)-bovine serum albumin (BSA) pair was used as a model for our study. An opto-fluidic setup was developed in order to flow the different reagents and,…

AnalyteMaterials scienceIntegrated photonicsSerum albuminBiosensing TechniquesRing resonator02 engineering and technologylcsh:Chemical technologyBiotecnologia01 natural sciencesBiochemistryAntibodiesArticleAnalytical Chemistry010309 opticsResonatorring resonatorsensorQUIMICA ANALITICATEORIA DE LA SEÑAL Y COMUNICACIONES0103 physical scienceslcsh:TP1-1185Electrical and Electronic EngineeringStaphylococcal Protein AInstrumentationIntegrated photonics; ring resonator; sensor; biosensingSensorDetection limitPhotonsChromatographybiologyBiosensingbusiness.industrySerum Albumin BovineRepeatabilityÒptica021001 nanoscience & nanotechnologyAtomic and Molecular Physics and Opticsbiology.proteinbiosensingPhotonics0210 nano-technologybusinessProtein ABiosensorSensors
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The mechanism of binding staphylococcal protein A to immunoglobin G does not involve helix unwinding.

1996

Structural changes in staphylococcal protein A (SpA) upon its binding to the constant region (Fc) of immunoglobulin G (IgG) have been studied by nuclear magnetic resonance and circular dichroism (CD) spectroscopy. The NMR solution structure of the engineered IgG-binding domain of SpA, the Z domain (an analogue of the B domain of SpA), has been determined by simulated annealing with molecular dynamics, using 599 distance and dihedral angle constraints. Domain Z contains three alpha-helices in the polypeptide segments Lys7 to His18 (helix 1), Glu25 to Asp36 (helix 2), and Ser41 to Ala54 (helix 3). The overall chain fold is an antiparallel three-helical bundle. This is in contrast to the previ…

Models MolecularCircular dichroismProtein FoldingMagnetic Resonance SpectroscopyStereochemistryMolecular Sequence DataPlasma protein bindingDihedral angleBiochemistryProtein Structure SecondaryProtein structureComputer GraphicsAmino Acid SequenceBinding siteStaphylococcal Protein ABinding SitesChemistryCircular DichroismNuclear magnetic resonance spectroscopyRecombinant ProteinsImmunoglobulin Fc FragmentsModels StructuralCrystallographyIgG bindingImmunoglobulin GMutagenesis Site-DirectedProtein foldingProtein BindingBiochemistry
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High-resolution solution NMR structure of the Z domain of staphylococcal protein A

1997

Staphylococcal protein A (SpA) is a cell-wall-bound pathogenicity factor from the bacterium Staphylococcus aureus. Because of their small size and immunoglobulin (IgG)-binding activities, domains of protein A are targets for protein engineering efforts and for the development of computational approaches for de novo protein folding. The NMR solution structure of an engineered IgG-binding domain of SpA, the Z domain (an analog of the B domain of SpA), has been determined by simulated annealing with restrained molecular dynamics on the basis of 671 conformational constraints. The Z domain contains three well-defined alpha-helices corresponding to polypeptide segments Lys7 to Leu17 (helix 1), G…

Models MolecularMagnetic Resonance SpectroscopyProtein ConformationChemistryMolecular Sequence DataProtein engineeringHydrogen-Ion ConcentrationCrystallography X-RayAntiparallel (biochemistry)CrystallographyModels ChemicalStructural BiologyHelixHumansHydrogen–deuterium exchangeAmino Acid SequenceB3 domainStaphylococcal Protein AMolecular BiologyTwo-dimensional nuclear magnetic resonance spectroscopyConformational isomerismHeteronuclear single quantum coherence spectroscopyJournal of Molecular Biology
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Development of type-specific and cross-reactive serological probes for the minor capsid protein of human papillomavirus type 33.

1993

Human papillomavirus type 33 (HPV33) is associated with malignant tumors of the cervix. In an attempt to develop immunological probes for HPV33 infections, antisera against various bacterial fusion proteins carrying sequences of the minor capsid protein encoded by L2 were raised in animals. Antigenic determinants on the HPV33 L2 protein were identified by using truncated fusion proteins and were classified as type specific or cross-reactive with respect to HPV1, -8, -11, -16, and -18. Cross-reactive epitopes map to amino acids 98 to 107 or to amino acids 102 to 112 and 107 to 117, respectively, depending on the fusion protein used for immunization. Antibodies directed toward these epitopes …

Recombinant Fusion ProteinsImmunologyGuinea PigsMolecular Sequence DataPeptideBiologyMicrobiologyEpitopeStructure-Activity RelationshipCapsidAntigenSpecies SpecificityVirologyAnimalsAmino Acid SequenceStaphylococcal Protein APeptide sequenceAntigens ViralPapillomaviridaeGlutathione TransferaseSequence Deletionchemistry.chemical_classificationBase SequenceOncogene Proteins Viralbeta-GalactosidaseMolecular biologyFusion proteinAmino acidchemistryCapsidOligodeoxyribonucleotidesInsect Sciencebiology.proteinCapsid ProteinsRabbitsAntibodySequence AlignmentResearch ArticleJournal of virology
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Specific Binding of Baculoviruses Displaying gp64 Fusion Proteins to Mammalian Cells

2001

Viral vectors displaying specific ligand binding moieties have raised an increasing interest in the area of targeted gene therapy. In this report, we describe baculovirus vectors displaying either a functional single chain antibody fragment (scFv) specific for the carcinoembryonic antigen (CEA) or the synthetic IgG binding domains (ZZ) derived from protein A of Staphylococcus aureus. In addition, the vectors were engineered to incorporate a reporter gene encoding the enhanced green fluorescent protein (EGFP) under the transcriptional regulation of the cytomegalovirus (CMV) IE promoter. Display of the targeting moieties on the viral surface was achieved through fusion to the N-terminus of gp…

Recombinant Fusion ProteinsvirusesGenetic VectorsGreen Fluorescent ProteinsImmunoglobulin Variable RegionBiophysicsSpodopteraTransfectionBiochemistryCell LineGreen fluorescent proteinViral vector03 medical and health sciencesGenes ReporterTransduction GeneticCricetinaeTumor Cells CulturedAnimalsStaphylococcal Protein AMolecular Biology030304 developmental biology0303 health sciencesReporter genebiology030302 biochemistry & molecular biologyAntibodies MonoclonalGenetic TherapyCell BiologyTransfectionFusion proteinMolecular biologyCarcinoembryonic Antigen3. Good healthLuminescent ProteinsMicroscopy FluorescenceIgG bindingbiology.proteinAntibodyProtein ABaculoviridaeViral Fusion ProteinsBiochemical and Biophysical Research Communications
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High Resolution Solution NMR Structure of the Z Domain of Staphylococcal Protein A. Analysis of Secondary Structure for Free Z Domain and Bounded to …

1997

Staphylococcal protein A (SpA) is a cell-wall-bound pathogenicity factor from the bacterium Staphylcoccus aureus. It exhibits tight binding to many IgG, IgA and IgM molecules at site(s) different from antigen-combining site. Because of their small size and immunoglobulin (IgG)-binding activities, domains of protein A are important targets for protein engineering efforts and for the development of computational approaches for de novo protein folding.

biology'de novo' protein foldingChemistryStaphylococcal proteinProtein engineeringbiology.organism_classificationCrystallographyBiochemistryDomain (ring theory)biology.proteinAntibodyProtein AProtein secondary structureBacteria
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