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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science Ltd
    Health & social care in the community 10 (2002), S. 0 
    ISSN: 1365-2524
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background Grass pollen, such as that from timothy grass (Phleum pratense), represents a major cause of type I allergy.Objective To characterize the IgE immune response and to identify the major allergens eliciting an IgE response in a mouse model using pollen extract of P. pratense for sensitization, in order to assess analogies to human hyperreactivity and to gain information on the allergenic potential as determined by the IgE-reactivity kinetics of defined allergens.Methods Balb/c mice were sensitized with pollen extract or with purified natural allergens. Serum IgE levels, the induction of specific IgE antibodies and immediate hypersensitivity were monitored by ELISA, Western blot and a skin test, respectively.Results The sensitized mice mounted a strong IgE response and showed IgE-reactivity first against Phl p 5a and 5b, then Phl p 4 and 13 and lastly against Phl p 6. No IgE response was mounted against Phl p 1. However, all purified fractions examined (Phl p 5a, 5b, 6 and 1) induced specific IgE and showed similar kinetics of IgE induction as pollen extract (first Phl p 5a and 5b, then Phl p 6). Skin test experiments demonstrated positive reactivity only in sensitized mice.Conclusion The IgE reactivity induced by the major allergens in Balb/c mice was very similar to that found in allergic patients, with the exception of Phl p 1. The kinetics of the specific IgE response was comparable using either pollen extract or the purified major allergens, indicating that the intrinsic properties of the allergens are of importance rather than their proportionate amounts in pollen extract. This model should prove to be suitable for investigations regarding the mechanisms of induction and manifestation of timothy grass pollen allergy and for the evaluation of therapeutic strategies.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The knowledge of IgE-binding epitopes on allergen molecules is important for better understanding allergen–antibody interactions and, thus, for developing new strategies for immunotherapy.Our purpose was to more precisely define the number and structure of IgE-binding epitopes of a paradigmatic major grass pollen allergen.We performed an IgE-binding epitope mapping of rHol l 5, a group V pollen allergen of velvet grass (Holcus lanatus), with overlapping fragments (length between 15 and 186 amino acids), which were expressed in E. coli as MBP fusion proteins. Using sera of 65 grass pollen allergic patients, the fragments were analysed by immunoblotting for IgE reactivity. Specificity of antibody binding was confirmed by competitive blot inhibition assays.At least four different continuous IgE-binding epitopes were identified on small fragments (about 30 amino acids), and at least five different discontinuous IgE-binding epitopes on larger fragments, which were destroyed by further fragmentation. The fragments were differentially recognized by individual patients' sera. By investigating IgE-binding to one of the small fragments in more detail, we found further epitope regions on this fragment. It was noteworthy that IgE reactivity to small fragments was weak compared to large fragments or to the complete molecule. Competitive blot inhibition experiments showed that binding of IgE antibodies to the small fragments was specific but with lower avidity than to the complete rHol l 5.rHol l 5 harbours multiple discontinuous as well as continuous IgE-binding epitopes spread over the whole molecule, which were individually recognized by IgE antibodies from different patients. Low avidity of IgE antibodies to small fragments suggests that the continuous epitope regions do not represent the complete epitope and are most probably parts of discontinuous epitopes.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1438-2385
    Keywords: Key words Hazelnut allergens ; Cross-reactivity ; Cross-reactive carbohydrate determinants ; Heat-stable allergens ; Rat basophil leukaemia cell assay
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  Hazelnuts (HNs), widely distributed in sweets, provoke one of the most frequent pollen-associated food allergies. In this study HN allergens were investigated and immunologically characterized, focussing on their heat stability and cross-reactivity with known allergenic structures. Therefore, 27 sera from HN-allergic patients and 28 sera from children with positive CAP classes for HN and birch pollen were submitted to immunoblot and immunoblot inhibition. The major HN allergen was found to present a molecular mass of about 17–18 kDa, and to share IgE epitopes with Bet v 1, the major birch pollen allergen. This allergen was recognized by IgE of 93% of our HN-allergic patients and by 79% of sensitized children. A 48 kDa glycoprotein was identified as a minor HN allergen with cross-reactive carbohydrate determinants. The major N-glycan species was determined by matrix-assisted laser desorption mass spectrometry to be Man3XylGlcNAc2. IgE binding to this protein was detected in sera of 41% of the allergic patients and 61% of the children. Partial N-terminal sequencing demonstrated similarity to legume storage proteins. The IgE reactivity of this structure was partially resistant to heating. The rat basophil leukaemia cell mediator release assay was used for estimation of cross-sensitization between HN and birch pollen, confirming the finding that HNs contain a heat-resistant allergenicity without cross-reactivity to birch pollen allergens.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Hydrobiologia 424 (2000), S. 91-99 
    ISSN: 1573-5117
    Keywords: Cyanobacteria ; eutrophication ; Irish lakes ; carbon dioxide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A synoptic survey of the distribution and abundance of occurrence of bloom-forming Cyanobacteria in 55 lakes in the Republic of Ireland revealed strong positive correlations with the traditional trophic gradient. Analysis of the data shows that the perceived trophic state may be correctly viewed as a function of phosphorus availability. The distribution of dominant bloom-forming Cyanobacteria is strongly related to the geology of the catchments and the incidence of significant bicarbonate buffering.
    Type of Medium: Electronic Resource
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