Search

Your search keyword '"Scheiblhofer, Sandra"' showing total 13 results
Start Over Author "Scheiblhofer, Sandra" Journal journal of allergy and clinical immunology
13 results on '"Scheiblhofer, Sandra"'

2. Fold stability during endolysosomal acidification is a key factor for allergenicity and immunogenicity of the major birch pollen allergen

Author

Machado, Yoan, Freier, Regina, Scheiblhofer, Sandra, Thalhamer, Theresa, Mayr, Melissa, Briza, Peter, Grutsch, Sarina, Ahammer, Linda, Fuchs, Julian E., Wallnoefer, Hannes G., Isakovic, Almedina, Kohlbauer, Vera, Hinterholzer, Arthur, Steiner, Markus, Danzer, Martin, Horejs-Hoeck, Jutta, Ferreira, Fatima, Liedl, Klaus R., Tollinger, Martin, Lackner, Peter, Johnson, Christopher M., Brandstetter, Hans, Thalhamer, Josef, and Weiss, Richard

Subjects
NMR, Nuclear magnetic resonance, Protein Folding, molecular allergology, Immunology, Endosomes, endolysosomal degradation, Bet v 1, SEC-MALS, Size exclusion chromatography coupled to multiangle light scattering, Animals, Immunology and Allergy, antigen processing and presentation, MOLECULAR ALLERGOLOGY, Allergic sensitization, moDC, Monocyte-derived dendritic cell, Mice, Inbred BALB C, RBL, Rat basophil leukemia, Protein Stability, FTIR, Fourier transform infrared spectroscopy, ALLERGIC SENSITIZATION, Allergens, Antigens, Plant, Hydrogen-Ion Concentration, Immunoglobulin E, CD, Circular dichroism, Immunoglobulin G, Mutation, structural stability, Mechanisms of Allergy and Clinical Immunology, Pollen, Female, DSC, Differential scanning calorimetry
Abstract

Background The search for intrinsic factors, which account for a protein's capability to act as an allergen, is ongoing. Fold stability has been identified as a molecular feature that affects processing and presentation, thereby influencing an antigen's immunologic properties. Objective We assessed how changes in fold stability modulate the immunogenicity and sensitization capacity of the major birch pollen allergen Bet v 1. Methods By exploiting an exhaustive virtual mutation screening, we generated mutants of the prototype allergen Bet v 1 with enhanced thermal and chemical stability and rigidity. Structural changes were analyzed by means of x-ray crystallography, nuclear magnetic resonance, and molecular dynamics simulations. Stability was monitored by using differential scanning calorimetry, circular dichroism, and Fourier transform infrared spectroscopy. Endolysosomal degradation was simulated in vitro by using the microsomal fraction of JAWS II cells, followed by liquid chromatography coupled to mass spectrometry. Immunologic properties were characterized in vitro by using a human T-cell line specific for the immunodominant epitope of Bet v 1 and in vivo in an adjuvant-free BALB/c mouse model. Results Fold stabilization of Bet v 1 was pH dependent and resulted in resistance to endosomal degradation at a pH of 5 or greater, affecting presentation of the immunodominant T-cell epitope in vitro. These properties translated in vivo into a strong allergy-promoting TH2-type immune response. Efficient TH2 cell activation required both an increased stability at the pH of the early endosome and efficient degradation at lower pH in the late endosomal/lysosomal compartment. Conclusions Our data indicate that differential pH-dependent fold stability along endosomal maturation is an essential protein-inherent determinant of allergenicity.

Published
2016
Full Text
View/download PDF

3. Context matters: TH2 polarization resulting from pollen composition and not from protein-intrinsic allergenicity

Author

Aglas, Lorenz, primary, Gilles, Stefanie, additional, Bauer, Renate, additional, Huber, Sara, additional, Araujo, Galber R., additional, Mueller, Geoffrey, additional, Scheiblhofer, Sandra, additional, Amisi, Marie, additional, Dang, Hieu-Hoa, additional, Briza, Peter, additional, Bohle, Barbara, additional, Horejs-Hoeck, Jutta, additional, Traidl-Hoffmann, Claudia, additional, and Ferreira, Fatima, additional

Published
2018
Full Text
View/download PDF

4. Natural protective immunity against grass pollen allergy is maintained by a diverse spectrum of response types

Author

Kurtaj, Almedina, primary, Hillebrand, Christoph, additional, Fichtinger, Gerda, additional, Hattinger, Eva, additional, Lietzenmayer, Melanie, additional, Machado, Yoan, additional, Scheiblhofer, Sandra, additional, Stoecklinger, Angelika, additional, Thalhamer, Theresa, additional, Suessner, Susanne, additional, Danzer, Martin, additional, Keplinger, Sabine, additional, Weinberger, Johannes, additional, Schaller, Susanne, additional, Winkler, Stephan, additional, Gabriel, Christian, additional, Thalhamer, Josef, additional, and Weiss, Richard, additional

Published
2017
Full Text
View/download PDF

5. Allergen microarray detects high prevalence of asymptomatic IgE sensitizations to tropical pollen-derived carbohydrates

Author

Cabauatan, Clarissa R., primary, Lupinek, Christian, additional, Scheiblhofer, Sandra, additional, Weiss, Richard, additional, Focke-Tejkl, Margarete, additional, Bhalla, Prem L., additional, Singh, Mohan B., additional, Knight, Paul A., additional, van Hage, Marianne, additional, Ramos, John Donnie A., additional, and Valenta, Rudolf, additional

Published
2014
Full Text
View/download PDF

6. α-Purothionin, a new wheat allergen associated with severe allergy

Author

Pahr, Sandra, primary, Constantin, Claudia, additional, Papadopoulos, Nikolaos G., additional, Giavi, Stavroula, additional, Mäkelä, Mika, additional, Pelkonen, Anna, additional, Ebner, Christof, additional, Mari, Adriano, additional, Scheiblhofer, Sandra, additional, Thalhamer, Josef, additional, Kundi, Michael, additional, Vrtala, Susanne, additional, Mittermann, Irene, additional, and Valenta, Rudolf, additional

Published
2013
Full Text
View/download PDF

7. Visualization of clustered IgE epitopes on α-lactalbumin

Author

Hochwallner, Heidrun, primary, Schulmeister, Ulrike, additional, Swoboda, Ines, additional, Focke-Tejkl, Margit, additional, Civaj, Vera, additional, Balic, Nadja, additional, Nystrand, Mats, additional, Härlin, Annika, additional, Thalhamer, Josef, additional, Scheiblhofer, Sandra, additional, Keller, Walter, additional, Pavkov, Tea, additional, Zafred, Domen, additional, Niggemann, Bodo, additional, Quirce, Santiago, additional, Mari, Adriano, additional, Pauli, Gabrielle, additional, Ebner, Christof, additional, Papadopoulos, Nikolaos G., additional, Herz, Udo, additional, van Tol, Eric A.F., additional, Valenta, Rudolf, additional, and Spitzauer, Susanne, additional

Published
2010
Full Text
View/download PDF

11. Context matters: T H 2 polarization resulting from pollen composition and not from protein-intrinsic allergenicity.

Author

Aglas L, Gilles S, Bauer R, Huber S, Araujo GR, Mueller G, Scheiblhofer S, Amisi M, Dang HH, Briza P, Bohle B, Horejs-Hoeck J, Traidl-Hoffmann C, and Ferreira F

Subjects
Animals, Cytokines immunology, Female, Humans, Mice, Inbred C57BL, Mice, Transgenic, Allergens immunology, Antigen-Presenting Cells immunology, Antigens, Plant immunology, Plant Proteins immunology, Pollen immunology, Th2 Cells immunology
Published
2018
Full Text
View/download PDF

12. Visualization of clustered IgE epitopes on alpha-lactalbumin.

Author

Hochwallner H, Schulmeister U, Swoboda I, Focke-Tejkl M, Civaj V, Balic N, Nystrand M, Härlin A, Thalhamer J, Scheiblhofer S, Keller W, Pavkov T, Zafred D, Niggemann B, Quirce S, Mari A, Pauli G, Ebner C, Papadopoulos NG, Herz U, van Tol EA, Valenta R, and Spitzauer S

Subjects
Animals, Cattle, Cells, Cultured, Circular Dichroism, Cloning, Molecular, Epitopes, B-Lymphocyte chemistry, Epitopes, B-Lymphocyte metabolism, Escherichia coli genetics, Feasibility Studies, Histamine Release immunology, Humans, Immunoglobulin E blood, Immunoglobulin E immunology, Lactalbumin genetics, Lactalbumin immunology, Lactalbumin isolation & purification, Mass Spectrometry, Microarray Analysis, Milk Hypersensitivity blood, Peptide Fragments chemistry, Peptide Fragments metabolism, Recombinant Proteins genetics, Recombinant Proteins immunology, Recombinant Proteins isolation & purification, Lactalbumin metabolism, Milk Hypersensitivity diagnosis, Milk Hypersensitivity immunology, Recombinant Proteins metabolism
Abstract

Background: alpha-Lactalbumin (alpha-La) is a major cow's milk (CM) allergen responsible for allergic reactions in infants., Objective: We performed molecular, structural, and immunologic characterization of alpha-La., Methods: Recombinant alpha-lactalbumin (ralpha-La) was expressed in Escherichia coli, purified to homogeneity, and characterized by means of mass spectrometry and circular dichroism, and its allergenic activity was studied by using microarray technology, as well as in a basophil histamine release assay. IgE epitope mapping was performed with synthetic peptides., Results: According to circular dichroism analysis, ralpha-La represented a folded protein with a high thermal stability and refolding capacity. ralpha-La reacted with IgE antibodies from 57.6% of patients with CM allergy (n = 66) and induced the strongest basophil degranulation with sera from patients with CM allergy who had exhibited gastrointestinal symptoms or severe systemic reactions on CM exposure. ralpha-La contained sequential and conformational IgE epitopes. Superposition of IgE-reactive peptides onto the 3-dimensional structure of alpha-La revealed a close vicinity of the N- and C-terminal peptides within a surface-exposed patch., Conclusions: ralpha-La can be used for the diagnosis of patients with severe allergic reactions to CM and serves as a paradigmatic tool for the development of therapeutic strategies for CM allergy., (Copyright (c) 2010 American Academy of Allergy, Asthma & Immunology. Published by Mosby, Inc. All rights reserved.)

Published
2010
Full Text
View/download PDF

13. Immunization with a low-dose replicon DNA vaccine encoding Phl p 5 effectively prevents allergic sensitization.

Author

Gabler M, Scheiblhofer S, Kern K, Leitner WW, Stoecklinger A, Hauser-Kronberger C, Alinger B, Lechner B, Prinz M, Vrtala S, Valenta R, Thalhamer J, and Weiss R

Subjects
Animals, Cell Line, Tumor, Cells, Cultured, Dose-Response Relationship, Immunologic, Female, Injections, Intradermal, Mice, Mice, Inbred BALB C, Plant Proteins administration & dosage, RNA-Dependent RNA Polymerase genetics, RNA-Dependent RNA Polymerase immunology, Sindbis Virus enzymology, Sindbis Virus genetics, Sindbis Virus immunology, Th1 Cells immunology, Vaccines, DNA administration & dosage, Viral Vaccines administration & dosage, Viral Vaccines genetics, Viral Vaccines immunology, Plant Proteins genetics, Plant Proteins immunology, Replicon immunology, Respiratory Hypersensitivity immunology, Respiratory Hypersensitivity prevention & control, Vaccines, DNA immunology
Abstract

Background: Replicase-based DNA vaccines stimulate T(H)1-biased immune responses at ultralow doses and induce self-removal of transfected cells through apoptosis. Both aspects are important requirements for efficient and safe DNA-based immunotherapy of type I allergies., Objective: A Sindbis virus replicon-based DNA vaccine encoding the major timothy grass pollen allergen Phl p 5 was evaluated for its antiallergic potential compared with a conventional DNA vaccine in a BALB/c mouse model of allergy., Methods: Mice were intradermally prevaccinated with plasmid DNA, followed by sensitization and intranasal allergen provocation with recombinant Phl p 5. In vitro proliferation and cytokine secretion was measured in splenocyte cultures. Distribution of IgG1, IgG2a, and IgE antibody subclasses was determined by means of ELISA. IgE-mediated degranulation was measured with the basophil release assay. Bronchoalveolar lavage fluid was analyzed for eosinophils, IL-4, IL-5, IL-13, and IFN-gamma. Mucus production, inflammatory infiltrates, and epithelial damage were determined in lung sections., Results: Both vaccines induced T(H)1-biased immune responses, resulting in suppression of functional IgE, reduction of eosinophilia in bronchoalveolar lavage fluid, and alleviation of lung pathology. However, immunization with the replicon DNA vaccine elicited these effects at a 100-fold lower dose compared with the conventional DNA vaccine., Conclusions: The increased immunogenicity of replicon-based DNA vaccines allows for application of extremely low doses, thereby eliminating the concerns associated with conventional DNA vaccines, which have to be administered at milligram amounts to induce immune reactions in human subjects., Clinical Implications: Their high safety profile makes replicon-based DNA vaccines promising candidates for treatment of type I allergies in the clinic.

Published
2006
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results