The Experts below are selected from a list of 10155 Experts worldwide ranked by ideXlab platform
Erika Jensenjarolim - One of the best experts on this subject based on the ideXlab platform.
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m cell targeting with aleuria aurantia lectin as a novel approach for oral allergen immunotherapy
The Journal of Allergy and Clinical Immunology, 2004Co-Authors: Franziska Rothwalter, Isabella Scholl, Andrea Weissenbock, Renate Fuchs, Otto Scheiner, Eva Untersmayr, Franz Gabor, George Boltznitulescu, Erika JensenjarolimAbstract:BACKGROUND: The extent and quality of the immune response to orally applied allergens may critically depend on the precise site of uptake at the intestinal mucosa. OBJECTIVE: The aim of this study was to construct allergen vehicles optimized for oral allergen immunotherapy. METHODS: By using a murine model, we examined the immunomodulatory effect of birch Pollen Proteins entrapped in poly(D,L-lactide-co-glycolide) microspheres, which were specifically targeted to enterocytes or to M cells, in an ongoing T h 2 response. BALB/c mice express different carbohydrates on these 2 cell types. To target the sialylic residues on murine enterocytes, we functionalized microspheres with wheat germ agglutinin (WGA) and, to target alpha-L-fucose on M cells, with a lectin from Aleuria aurantia (AAL), the orange peel mushroom. RESULTS: Both WGA and AAL functionalization enhanced binding to human Caco2 cells substantially, which express sialylic and, as carcinoma cells, also alpha-L-fucose residues. Different groups of BALB/c mice were first sensitized to birch Pollen and subsequently fed with birch Pollen-loaded functionalized (WGA microspheres, AAL microspheres) or nonfunctionalized, birch Pollen extract-loaded particles. When mice were fed with AAL microspheres, birch Pollen-specific IgG2a, but not IgG1 or IgE, increased significantly. As expected, in a 3 H-thymidin assay, their splenocytes proliferated specifically on birch Pollen stimulation. Both targeting strategies, using WGA or AAL, induced IL-10 as well as IL-4 production. However, in AAL microsphere-treated mice, IFN-gamma synthesis was significantly increased, which may be responsible for the significant IgG2a production in this group. CONCLUSION: Our data indicate that targeting M cells by using AAL-coated allergen vehicles may be a promising strategy for oral allergen immunotherapy.
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original articles m cell targeting with aleuria aurantia lectin as a novel approach for oral allergen immunotherapy
2004Co-Authors: Franziska Rothwalter, Renate Fuchs, Otto Scheiner, Eva Untersmayr, Franz Gabor, George Boltznitulescu, Erika JensenjarolimAbstract:Background: The extent and quality of the immune response to orally applied allergens may critically depend on the precise site of uptake at the intestinal mucosa. Objective: The aim of this study was to construct allergen vehicles optimized for oral allergen immunotherapy. Methods: By using a murine model, we examined the immunomodulatory effect of birch Pollen Proteins entrapped in poly(D,L-lactide-co-glycolide) microspheres, which were specifically targeted to enterocytes or to M cells, in an ongoing TH2 response. BALB/c mice express different carbohydrates on these 2 cell types. To target the sialylic residues on murine enterocytes, we functionalized microspheres with wheat germ agglutinin (WGA) and, to target a-L-fucose on M cells, with a lectin from Aleuria aurantia (AAL), the orange peel mushroom. Results: Both WGA and AAL functionalization enhanced binding to human Caco2 cells substantially, which express sialylic and, as carcinoma cells, also a-L-fucose residues. Different groups of BALB/c mice were first sensitized to birch Pollen and subsequently fed with birch Pollen-loaded
Vernonica E Franklintong - One of the best experts on this subject based on the ideXlab platform.
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a potential signaling role for profilin in Pollen of papaver rhoeas
The Plant Cell, 1998Co-Authors: Susan R Clarke, Christopher J Staiger, Bryan C Gibbon, Vernonica E FranklintongAbstract:Regulation of Pollen tube growth is known to involve alterations in intracellular calcium levels and phosphoinositide signaling, although the mechanisms involved are unclear. However, it appears likely that pollination events involve a complex interplay between signaling pathways and components of the actin cytoskeleton in Pollen. In many eukaryotic cells, actin binding Proteins function as stimulus-response modulators, translating signals into alterations in the cytoplasmic architecture. In this study, we examined whether profilin, which is a member of this class of signaling intermediate, might play a similar role in Pollen. We have analyzed the functional properties of native profilin from Pollen of Papaver rhoeas and have investigated the effects of profilin on the phosphorylation of Pollen Proteins in vitro by adding a slight excess of profilin to cytosolic Pollen extracts. We present clear evidence that profilin interacts with soluble Pollen components, resulting in dramatic alterations in the phosphorylation of several Proteins. We also show, albeit in vitro, the involvement of profilin in modulating the activity of a signaling component(s) affecting protein phosphorylation. Our data, which suggest that Pollen profilin can regulate actin-based cytoskeletal protein assembly and protein kinase or phosphatase activity, indicate a possible role for the involvement of profilin in signaling pathways that may regulate Pollen tube growth.
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increased phosphorylation of a 26 kd Pollen protein is induced by the self incompatibility response in papaver rhoeas
The Plant Cell, 1996Co-Authors: J J Rudd, F C H Franklin, Janet M Lord, Vernonica E FranklintongAbstract:We have investigated whether specific protein phosphorylation events are induced in Papaver rhoeas Pollen as a consequence of the self-incompatibility (SI) response. Pollen grown in vitro in the presence of 32P-orthophosphate was challenged with biologically active recombinant S Proteins, and Pollen Proteins were extracted and analyzed. The results provide strong evidence that the increased phosphorylation of a 26-kD protein of pl 6.2, p26, is specifically induced by the SI response. This phosphorylation event occurs in living Pollen tubes and was observed specifically when Pollen was challenged with S Proteins that are incompatible with the S alleles carried by the Pollen and not when Pollen was challenged with compatible or incompatible heat-denatured S Proteins. Further characterization demonstrated that p26 comprises two phosphoProteins, p26.1 and p26.2, that are found in soluble and microsomal fractions, respectively. Increased phosphorylation of p26.1 is implicated in the SI response and appears to be Ca2+ and calmodulin dependent. These data argue for the involvement of a Ca2+-dependent protein kinase requiring calmodulin-like domains, whose activation comprises an intracellular signal mediating the SI response in P. rhoeas Pollen.
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gametophytic self incompatibility in papaver rhoeas l
Sexual Plant Reproduction, 1992Co-Authors: Vernonica E Franklintong, Christopher F H FranklinAbstract:We have developed an in vitro system whereby we can reproduce the self-incompatibility (SI) reactions ofP. rhoeas in Pollen grown in vitro, using stigmatic extracts. This has enabled us to investigate a number of aspects of SI, which would otherwise be difficult. On the stigma side of the reaction, the in vitro system has enabled us to characterize and partially purify the stigmatic S-component, following S-specific activity. It has also enabled us to establish that, in contrast to the S-linked glycoprotein ofNicotiana alata, no detectable ribonuclease activity correlates with the presence of the functional stigmatic S-gene product in this species. Turning to look at the Pollen side, we have used the in vitro system to study the metabolic events occurring in the Pollen ofP. rhoeas as a consequence of the SI reaction. We have determined that it requires both de novo glyco-sylation and RNA transcription for full inhibition of Pollen-tube growth during the SI reaction. Transcription products of Pollen SI response genes, which are produced specificially in an incompatible reaction, have been identified. These Pollen response genes have been cloned and are currently being characterized. Since the extracellular Pollen-stigma interaction results directly in gene transcription in the Pollen, it seems likely that a signal transduction mechanism may be operating in the SI response. The in vitro system has allowed us to begin to investigate this possibility. We have detected rapid and transient phosphorylation of certain Pollen Proteins, together with changes in phosphatase activity during the SI reaction. These studies provide evidence for a role for signal transduction in the SI reaction. Thus, our in vitro system has enabled us to begin to examine, not only stigma and Pollen components, but also the interaction between them in the SI reaction.
Otto Scheiner - One of the best experts on this subject based on the ideXlab platform.
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prevalence of ige binding to art v 1 art v 4 and amb a 1 in mugwort allergic patients
International Archives of Allergy and Immunology, 2008Co-Authors: Christina Oberhuber, Otto Scheiner, Nicole Wopfner, Gabriele Gadermaier, Azra Dedic, Bodo Niggemann, Bernhard Maderegger, P Gruber, Fatima Ferreira, Karin HoffmannsommergruberAbstract:Background: Mugwort (Artemisia vulgaris) represents an important source of weed Pollen allergens. The objectives of the present study were (i) to analyze the IgE binding profiles in a group of mugwort-allergic patients, (ii) to identify individual marker allergens crucial for the diagnosis of mugwort allergy and (iii) to identify potential crossreactive allergens present in ragweed (Ambrosia artemisiifolia) Pollen extract. Methods: Sera from 100 pediatric mugwort-allergic patients were analyzed for their IgE binding pattern to natural mugwort and ragweed Pollen Proteins, purified natural and recombinant Art v 1, recombinant Art v 4 and recombinant Amb a 1 using immunoblots and ELISA. Results: 91% of the patients’ sera tested displayed IgE binding to one or more mugwort Pollen allergens in ELISA and 88% were positive in immunoblot. Purified natural Art v 1 was recognized by 79%, the recombinant protein by 39% of the patients tested and purified recombinant Art v 4 by 34% of the patients’ sera. 67% of the sera displayed crossreactive IgE to one or more ragweed Pollen allergens. Recombinant Amb a 1 was noted in only 14% of the mugwort-allergic sera. Conclusions: Allergen-specific in vitro diagnosis was performed in 100 pediatric mugwort-allergic serum samples. Using two allergens (Art v 1 and Art v 4), 91% of the patients could be identified as mugwort Pollen-sensitized patients by IgE in vitro tests. Crossreactivity to ragweed Pollen allergens was demonstrated by in vitro experiments, suggesting a new important and potent allergen source expanding across Europe.
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m cell targeting with aleuria aurantia lectin as a novel approach for oral allergen immunotherapy
The Journal of Allergy and Clinical Immunology, 2004Co-Authors: Franziska Rothwalter, Isabella Scholl, Andrea Weissenbock, Renate Fuchs, Otto Scheiner, Eva Untersmayr, Franz Gabor, George Boltznitulescu, Erika JensenjarolimAbstract:BACKGROUND: The extent and quality of the immune response to orally applied allergens may critically depend on the precise site of uptake at the intestinal mucosa. OBJECTIVE: The aim of this study was to construct allergen vehicles optimized for oral allergen immunotherapy. METHODS: By using a murine model, we examined the immunomodulatory effect of birch Pollen Proteins entrapped in poly(D,L-lactide-co-glycolide) microspheres, which were specifically targeted to enterocytes or to M cells, in an ongoing T h 2 response. BALB/c mice express different carbohydrates on these 2 cell types. To target the sialylic residues on murine enterocytes, we functionalized microspheres with wheat germ agglutinin (WGA) and, to target alpha-L-fucose on M cells, with a lectin from Aleuria aurantia (AAL), the orange peel mushroom. RESULTS: Both WGA and AAL functionalization enhanced binding to human Caco2 cells substantially, which express sialylic and, as carcinoma cells, also alpha-L-fucose residues. Different groups of BALB/c mice were first sensitized to birch Pollen and subsequently fed with birch Pollen-loaded functionalized (WGA microspheres, AAL microspheres) or nonfunctionalized, birch Pollen extract-loaded particles. When mice were fed with AAL microspheres, birch Pollen-specific IgG2a, but not IgG1 or IgE, increased significantly. As expected, in a 3 H-thymidin assay, their splenocytes proliferated specifically on birch Pollen stimulation. Both targeting strategies, using WGA or AAL, induced IL-10 as well as IL-4 production. However, in AAL microsphere-treated mice, IFN-gamma synthesis was significantly increased, which may be responsible for the significant IgG2a production in this group. CONCLUSION: Our data indicate that targeting M cells by using AAL-coated allergen vehicles may be a promising strategy for oral allergen immunotherapy.
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original articles m cell targeting with aleuria aurantia lectin as a novel approach for oral allergen immunotherapy
2004Co-Authors: Franziska Rothwalter, Renate Fuchs, Otto Scheiner, Eva Untersmayr, Franz Gabor, George Boltznitulescu, Erika JensenjarolimAbstract:Background: The extent and quality of the immune response to orally applied allergens may critically depend on the precise site of uptake at the intestinal mucosa. Objective: The aim of this study was to construct allergen vehicles optimized for oral allergen immunotherapy. Methods: By using a murine model, we examined the immunomodulatory effect of birch Pollen Proteins entrapped in poly(D,L-lactide-co-glycolide) microspheres, which were specifically targeted to enterocytes or to M cells, in an ongoing TH2 response. BALB/c mice express different carbohydrates on these 2 cell types. To target the sialylic residues on murine enterocytes, we functionalized microspheres with wheat germ agglutinin (WGA) and, to target a-L-fucose on M cells, with a lectin from Aleuria aurantia (AAL), the orange peel mushroom. Results: Both WGA and AAL functionalization enhanced binding to human Caco2 cells substantially, which express sialylic and, as carcinoma cells, also a-L-fucose residues. Different groups of BALB/c mice were first sensitized to birch Pollen and subsequently fed with birch Pollen-loaded
Ćirković-veličković Tanja - One of the best experts on this subject based on the ideXlab platform.
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In-depth quantitative profiling of post-translational modifications of Timothy grass Pollen allergome in relation to environmental oxidative stress
'Elsevier BV', 2019Co-Authors: Smiljanić Katarina, Burazer, Lidija M., Prodić Ivana, Apostolović Danijela, Cvetković Anka, Veljović Đorđe, Mutić Jelena, Van Hage Marianne, Ćirković-veličković TanjaAbstract:An association between pollution (e.g., from traffic emissions) and the increased prevalence of respiratory allergies has been observed. Field-realistic exposure studies provide the most relevant assessment of the effects of the intensity and diversity of urban and industrial contamination on Pollen structure and allergenicity. The significance of in-depth post-translational modification (PTM) studies of Pollen proteomes, when compared with studies on other aspects of pollution and altered Pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. We undertook a comprehensive comparative analysis of multiple polluted and environmentally preserved Phleum pratense (Timothy grass) Pollen samples using scanning electron microscopy, in-depth PTM profiling, determination of organic and inorganic pollutants, analysis of the release of sub-Pollen particles and phenols/Proteins, and analysis of proteome expression using high resolution tandem mass spectrometry. In addition, we used quantitative enzyme-linked immunosorbent assays (ELISA) and immunoglobulin E (IgE) immunoblotting. An increased phenolic content and release of sub-Pollen particles was found in Pollen samples from the polluted area, including a significantly higher content of mercury, cadmium, and manganese, with irregular long spines on Pollen grain surface structures. Antioxidative defense-related enzymes were significantly upregulated and seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in Pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected several Timothy Pollen allergens; Phl p 6, in particular, exhibited several different oxidative modifications. The expression of Phl p 6, 12, and 13 allergens were downregulated in polluted Pollen, and IgE binding to Pollen extract was substantially lower in the 18 patients studied, as measured by quantitative ELISA. Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed to modification of Timothy Pollen allergens and suggested that heavy metals are primarily responsible for oxidative stress effects observed in Pollen Proteins
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Immunoproteomic characterization of Ambrosia artemisiifolia Pollen allergens in canine atopic dermatitis
'Elsevier BV', 2013Co-Authors: Ognjenović Jana, Milčić-matić Natalija, Smiljanić Katarina, Vučković Olga, Burazer Lidija, Popović Nikola, Stanić-vučinić Dragana, Ćirković-veličković TanjaAbstract:Canine atopic dermatitis (CAD) is an immune system disorder that affects 10-15% of the canine population. Short ragweed (Ambrosia artemisiifolia) Pollen represents one of the major seasonal sources of allergenic Pollen Proteins in Europe, particularly in the Pannonian valley of the Balkan region. In Serbia, about 66% of atopic dogs showed a positive intradermal skin test with its Pollen extract, which is second to house dust mites. Therefore, characterization of Ambrosia artemisiifolia Pollen components, in terms of defining major and minor allergens that induce clinically manifested allergic reaction in dogs, is important for valid diagnosis and efficient therapy. This study has, for the first time, characterized and identified major Ambrosia artemisiifolia allergens in CAD, using an immunoproteomic approach. To assess the prevalence of specific IgE in electrophoretically separated ragweed Pollen Proteins, individual reactivity of sera from dogs with CAD was analyzed and compared to the reactivity of sera from healthy dogs in the non-reducing conditions, which were found optimal for specific canine IgE detection. A specific IgE band (38 kDa) was recognized as the most dominant allergen in CAD, occurring in 81% of positive dog's sera. 2-D immunoblotting followed by a mass spectrometry peptide fingerprint analyses with pooled canine and human atopic sera, revealed that 38 kDa major Ambrosia atremisiifolia allergens in CAD were all five isoallergens of the Amb a 1 group (antigen E), including the previously named Amb a 2 (antigen K). In contrast to canine sera, human atopic sera also recognized lower mass allergens such as the 13 fragment of Amb a 1 and profilins (Amb a 8 variants). The most prominent ragweed Proteins in CAD, represent, as in humans, variants of all five isoallergens of the Amb a 1 group (pectate lyase): Amb a 1.0101 and its natural variant E1XUL2, Amb a 1.0202, 1.0304, 1.0402 and the natural variant of Amb a 1.0501, E1XUM0, as well as the a fragment of Pollen allergen Amb a 1.0201. (C) 2013 Elsevier B.V. All rights reserved
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Immunoproteomic characterization of Ambrosia artemisiifolia Pollen allergens in canine atopic dermatitis
Elsevier Science Bv Amsterdam, 2013Co-Authors: Ognjenović Jana, Milčić-matić Natalija, Smiljanić Katarina, Popović Nikola, Stanić-vučinić Dragana, Vuckovic Olga, Burazer, Lidija M., Ćirković-veličković TanjaAbstract:Canine atopic dermatitis (CAD) is an immune system disorder that affects 10-15% of the canine population. Short ragweed (Ambrosia artemisiifolia) Pollen represents one of the major seasonal sources of allergenic Pollen Proteins in Europe, particularly in the Pannonian valley of the Balkan region. In Serbia, about 66% of atopic dogs showed a positive intradermal skin test with its Pollen extract, which is second to house dust mites. Therefore, characterization of Ambrosia artemisiifolia Pollen components, in terms of defining major and minor allergens that induce clinically manifested allergic reaction in dogs, is important for valid diagnosis and efficient therapy. This study has, for the first time, characterized and identified major Ambrosia artemisiifolia allergens in CAD, using an immunoproteomic approach. To assess the prevalence of specific IgE in electrophoretically separated ragweed Pollen Proteins, individual reactivity of sera from dogs with CAD was analyzed and compared to the reactivity of sera from healthy dogs in the non-reducing conditions, which were found optimal for specific canine IgE detection. A specific IgE band (38 kDa) was recognized as the most dominant allergen in CAD, occurring in 81% of positive dog's sera. 2-D immunoblotting followed by a mass spectrometry peptide fingerprint analyses with pooled canine and human atopic sera, revealed that 38 kDa major Ambrosia atremisiifolia allergens in CAD were all five isoallergens of the Amb a 1 group (antigen E), including the previously named Amb a 2 (antigen K). In contrast to canine sera, human atopic sera also recognized lower mass allergens such as the 13 fragment of Amb a 1 and profilins (Amb a 8 variants). The most prominent ragweed Proteins in CAD, represent, as in humans, variants of all five isoallergens of the Amb a 1 group (pectate lyase): Amb a 1.0101 and its natural variant E1XUL2, Amb a 1.0202, 1.0304, 1.0402 and the natural variant of Amb a 1.0501, E1XUM0, as well as the a fragment of Pollen allergen Amb a 1.0201
Susan R Clarke - One of the best experts on this subject based on the ideXlab platform.
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signalling and the cytoskeleton of Pollen tubes of papaver rhoeas
Annals of Botany, 2000Co-Authors: Anja Geitmann, Benjamin N Snowman, Susan R Clarke, Christopher J StaigerAbstract:Self-incompatibility (SI) is a genetically controlled system used by many flowering plants to prevent self-pollination, often by the inhibition of Pollen tube growth. The importance of cytosolic free calcium, [Ca2+]i, for the regulation of Pollen tube growth is well known. We have established, using calcium imaging, that the SI response in Papaver rhoeas L. Pollen involves a calcium-mediated intracellular signalling pathway. Tip growth of cells is dependent upon a typical configuration of the actin cytoskeleton, which is controlled by actin binding Proteins. In animal cells, the actin-binding protein, profilin, is thought to act as a key intermediate between signalling pathways and actin rearrangements. Profilin is an abundant component of Pollen. To better understand the signalling cascades that modulate Pollen tip growth and actin dynamics, we are investigating a possible signalling role for profilin. We have demonstrated that profilin modulates the phosphorylation of Pollen Proteins in vitro. This implicates a role for profilin in altering protein kinase or phosphatase activity. Furthermore, we demonstrate for the first time that profilin from Pollen can be phosphorylated in vitro. This provides compelling evidence that profilin interacts with signalling pathways in angiosperms. Finally, we demonstrate that in the SI response, the actin cytoskeleton of incompatible Pollen tubes is dramatically rearranged. Our data strongly support a role for the cytoskeleton and actin-binding Proteins interacting with signalling pathways involved in the regulation of Pollen tube growth.
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a potential signaling role for profilin in Pollen of papaver rhoeas
The Plant Cell, 1998Co-Authors: Susan R Clarke, Christopher J Staiger, Bryan C Gibbon, Vernonica E FranklintongAbstract:Regulation of Pollen tube growth is known to involve alterations in intracellular calcium levels and phosphoinositide signaling, although the mechanisms involved are unclear. However, it appears likely that pollination events involve a complex interplay between signaling pathways and components of the actin cytoskeleton in Pollen. In many eukaryotic cells, actin binding Proteins function as stimulus-response modulators, translating signals into alterations in the cytoplasmic architecture. In this study, we examined whether profilin, which is a member of this class of signaling intermediate, might play a similar role in Pollen. We have analyzed the functional properties of native profilin from Pollen of Papaver rhoeas and have investigated the effects of profilin on the phosphorylation of Pollen Proteins in vitro by adding a slight excess of profilin to cytosolic Pollen extracts. We present clear evidence that profilin interacts with soluble Pollen components, resulting in dramatic alterations in the phosphorylation of several Proteins. We also show, albeit in vitro, the involvement of profilin in modulating the activity of a signaling component(s) affecting protein phosphorylation. Our data, which suggest that Pollen profilin can regulate actin-based cytoskeletal protein assembly and protein kinase or phosphatase activity, indicate a possible role for the involvement of profilin in signaling pathways that may regulate Pollen tube growth.