0000000000997518

AUTHOR

Lothar Vogel

showing 3 related works from this author

Fresh water, marine and terrestrial cyanobacteria display distinct allergen characteristics.

2017

During the last decades, global cyanobacteria biomass increased due to climate change as well as industrial usage for production of biofuels and food supplements. Thus, there is a need for thorough characterization of their potential health risks, including allergenicity. We therefore aimed to identify and characterize similarities in allergenic potential of cyanobacteria originating from the major ecological environments. Different cyanobacterial taxa were tested for immunoreactivity with IgE from allergic donors and non-allergic controls using immunoblot and ELISA. Moreover, mediator release from human FceR1-transfected rat basophilic leukemia (RBL) cells was measured, allowing in situ ex…

0301 basic medicineCyanobacteriaNostocEnvironmental EngineeringClimate ChangeFresh Water010501 environmental sciencesmedicine.disease_causeImmunoglobulin ECyanobacteria01 natural sciencesEpitopeMicrobiology03 medical and health sciencesAllergenCell Line TumorPhycocyaninmedicineEnvironmental ChemistryAnimalsHumansSeawaterFood scienceWaste Management and Disposal0105 earth and related environmental sciencesBiomass (ecology)biologyPhycobiliproteinAllergensImmunoglobulin Ebiology.organism_classificationPollutionRats030104 developmental biologybiology.proteinThe Science of the total environment
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Allergen-induced IgE-dependent gut inflammation in a human PBMC-engrafted murine model of allergy.

2011

Background Humanized murine models comprise a new tool to analyze novel therapeutic strategies for allergic diseases of the intestine. Objective In this study we developed a human PBMC–engrafted murine model of allergen-driven gut inflammation and analyzed the underlying immunologic mechanisms. Methods Nonobese diabetic (NOD)– scid -γc −/− mice were injected intraperitoneally with human PBMCs from allergic donors together with the respective allergen or not. Three weeks later, mice were challenged with the allergen orally or rectally, and gut inflammation was monitored with a high-resolution video miniendoscopic system, as well as histologically. Results Using the aeroallergens birch or gra…

CD4-Positive T-LymphocytesAllergymedicine.medical_treatmentImmunologyHistamine AntagonistsAdministration OralInflammationNodMice SCIDPlatelet Membrane GlycoproteinsBiologymedicine.disease_causeImmunoglobulin ELymphocyte ActivationReceptors G-Protein-Coupledchemistry.chemical_compoundMiceAllergenimmune system diseasesAdministration RectalAntibody Specificityotorhinolaryngologic diseasesmedicineHypersensitivityImmunology and AllergyAnimalsHumansColitisMice KnockoutReceptors IgEAllergensImmunoglobulin Emedicine.diseaseDisease Models AnimalCytokinechemistryGastritisImmunologybiology.proteinLeukocytes MononuclearCytokinesPollenmedicine.symptomHistamineSpleenThe Journal of allergy and clinical immunology
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Quality and potency profile of eight recombinant isoallergens, largely mimicking total Bet v 1-specific IgE binding of birch pollen.

2019

Background To date, only limited information on structure, expression levels and IgE binding of Bet v 1 variants, which are simultaneously expressed in birch pollen, is available. Objective To analyse and compare structure and serum IgE/IgG binding of rBet v 1 variants to Bet v 1.0101. Methods Recombinant Bet v 1 variants were studied with sera of 20 subjects allergic to birch pollen. Folding, aggregation and solubility of the rBet v 1 variants were analysed to attribute diverging IgE binding to either allergen structure or methodological features. IgE/IgG binding was studied with rBet v 1 in solution or adsorbed to solid phases. Allergen-mediated cross-linking of FceRI receptors was determ…

MaleImmunologyEnzyme-Linked Immunosorbent AssayBasophilImmunoglobulin Emedicine.disease_causeMass Spectrometrylaw.inventionAllergenlawmedicineImmunology and AllergyPotencyAnimalsHumansReceptorBetulaPlant ProteinsbiologyChemistrySpectrum AnalysisRhinitis Allergic SeasonalHypoallergenicAntigens PlantImmunoglobulin EMolecular biologyRecombinant ProteinsRatsmedicine.anatomical_structureIgG bindingImmunoglobulin Gbiology.proteinRecombinant DNAPollenFemaleClinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology
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