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  • 1.
    Bulone, Vincent
    et al.
    KTH, Superseded Departments, Biotechnology.
    Rademaker, G. J.
    Pergantis, S.
    Krogstad-Johnsen, T.
    Smedstad-Paulsen, B.
    Thomas-Oates, J.
    Characterisation of horse dander allergen glycoproteins using amino acid and glycan structure analyses - A mass spectrometric method for glycan chain analysis of glycoproteins separated by two-dimensional electrophoresis2000In: International Archives of Allergy and Immunology, ISSN 1018-2438, E-ISSN 1423-0097, Vol. 123, no 3, p. 220-227Article in journal (Refereed)
    Abstract [en]

    Separation of horse dander allergens using two-dimensional PAGE resulted in the identification of 16 proteins that react with allergic patient sera. A sensitive method has been developed for analysing the structures of the glycan chains of individual glycoprotein allergens transferred to blots following two-dimensional PAGE, and has allowed the structural identification of the glycan chains of the most abundant isoforms of Equ c 1, a glycosylated horse dander major allergen. The method involves separation of the allergens by two-dimensional PAGE, transfer to polyvinylidene difluoride membranes, release of the glycan chains using peptide N-glycosidase F, permethylation and mass spectrometric analysis of the derivatised glycans. The amino acid compositions of the 16 horse dander allergens separated by two-dimensional PAGE have been determined, allowing the identification of the various isoforms of Equ c 1. These results also confirmed that the two non-glycosylated major allergens, Equ c 2.0101 and Equ c 2.0102, belong to the lipocalin family, and support the idea that these two allergens are most probably isoforms of the same protein. The glycan structures identified using the mass spectrometric method are common biantennary and triantennary glycan chains. These carbohydrate moieties may have a role in the binding of IgE; however, it is more likely that the overall glycoprotein structure involving both the glycan and protein moieties, rather than the structure of the glycan chains alone, is responsible for eliciting allergic responses.

  • 2.
    Gafvelin, G
    et al.
    Karolinska institutet.
    Thunberg, Sarah
    Karolinska Institutet.
    Kronqvist, M
    Karolinska institutet.
    Gronlund, H
    Karolinska institutet.
    Gronneberg, R
    Karolinska institutet.
    Troye-Blomberg, M
    Karolinska institutet.
    Akdis, M
    SIAF, switzerland.
    Fiebig, H
    Allergopharma, Germany.
    Purohit, A
    Hôpitaux Universitaires de Strasbourg, France.
    Horak, F
    Medical University of Vienna, Austria.
    Reisinger, J
    Medical University of Vienna, Austria.
    Niederberger, V
    Medical University of Vienna, Austria.
    Akdis, C A
    SIAF Switzerland.
    Cromwell, O
    Allergopharma, Germany.
    Pauli, G
    Hôpitaux Universitaires de Strasbourg, France.
    Valenta, R
    Medical University of Vienna, Austria.
    van Hage, M
    Karolinska institutet.
    Cytokine and antibody responses in birch-pollen-allergic patients treated with genetically modified derivatives of the major birch pollen allergen Bet v 12005In: International Archives of Allergy and Immunology, ISSN 1018-2438, E-ISSN 1423-0097, Vol. 138, no 1, p. 59-66Article in journal (Refereed)
    Abstract [en]

    Background: Recently, recombinant hypoallergenic derivatives of the major birch pollen allergen, Bet v 1, were used to treat birch-pollen-allergic patients in a double-blind, placebo-controlled, multi-centre immunotherapy study. The aim of this study was to evaluate the effects of vaccination with aluminium-hydroxide-adsorbed recombinant Bet v 1 derivatives versus placebo on T-cell, cytokine and antibody responses in a subgroup of patients. Methods: Blood was drawn from patients of the Swedish centre (n=27; rBet v 1 fragments: n=10; rBet v 1 trimer: n=8, and placebo-aluminium hydroxide: n=9) before the start and after completion of the treatment. PBMC were stimulated with rBet v 1 and analysed for cytokine (IL-4, IL-5, IL-10, IL-12, IL-13 and IFN-gamma)-secreting cells by ELISpot. Bet v 1-specific antibody levels in serum (IgG(1-4), IgE and IgA) were measured by ELISA. Skin prick tests with defined Bet v 1 concentrations were performed before and 10-11 months after the beginning of the study. Results: Bet v 1-specific IgG levels, consisting of IgG 1, IgG 2 and IgG 4, were significantly increased after treatment with recombinant allergen derivatives. Treatment with rBet v 1 trimer led to a significant (p<0.05) reduction of Bet v 1-reactive IL-5- and IL-13-producing cells, reflecting a reduced Th2 response. In addition, a decreased number of Bet v 1-reactive IL-4 producing (p=0.07) and an increase of IL-12-producing (p=0.06) cells was noted in the trimer-treated patients. In contrast to placebo, active treatment resulted in significantly reduced immediate-type skin reactions to Bet v 1 even 10-11 months after treatment. Conclusion: Vaccination with recombinant hypoallergenic Bet v 1 derivatives induces a Bet v 1-specific IgG response and leads to reduced skin reactivity in allergic patients. A reduction of Bet v 1-specific Th2 responses was observed in trimer-treated patients, which may reflect the intrinsic property of this allergen derivative. Copyright (C) 2005 S. Karger AG, Basel.

  • 3.
    Velickovic, Tanja Cirkovic
    et al.
    Faculty of Chemistry, Serbia.
    Thunberg, Sarah
    Karolinska Institutet, Sweden.
    Polovic, Natalija
    Faculty of Chemistry, Serbia.
    Neimert-Andersson, Theresa
    Karolinska Institutet, Sweden.
    Gronlund, Hans
    Karolinska Institutet, Sweden.
    van Hage, Marianne
    Karolinska Institutet, Sweden.
    Gafvelin, Guro
    Karolinska Institutet, Sweden.
    Low levels of endotoxin enhance allergen-stimulated proliferation and reduce the threshold for activation in human peripheral blood cells2008In: International Archives of Allergy and Immunology, ISSN 1018-2438, E-ISSN 1423-0097, Vol. 146, no 1, p. 1-10Article in journal (Refereed)
    Abstract [en]

    Background: Endotoxins, comprised of bacterial cell wall lipopolysaccharides (LPS), have been reported to have both protective and exacerbating effects on the development and maintenance of allergic disease in humans and on markers of allergic inflammation in animal models of allergy. In this study, we investigated the effect of low concentrations of LPS on human peripheral blood mononuclear cells (PBMC) stimulated with the major cat allergen Fel d 1. Methods: Extensive purification of recombinant (r) Fel d 1 yielded essentially endotoxin-free rFel d 1 (0.2 ng LPS/mg protein). PBMCs prepared from 15 subjects having IgE to cat (>0.7 kU(A)/l) and 8 subjects IgE negative to cat were stimulated with 2, 10 or 25 mu g/ml of rFel d 1 in the presence or absence of 50 pg/ml LPS. Proliferation was measured after 7 days of culture and supernatants were analyzed for IFN gamma, IL-5 and IL-10. Results: LPS (50 pg/ml) increased rFel d 1-stimulated proliferation of PBMCs both from subjects IgE-positive and subjects negative to cat allergens. PBMCs from 13 of the subjects did not proliferate in response to stimulation with 2 and 10 mu g/ml rFel d 1 alone but did so in the presence of LPS. Moreover, LPS increased the levels of rFel d 1-stimulated IFN gamma in cultures from cat-negative subjects, IL-5 from cat-positive subjects and IL-10 from both groups. Conclusion: Very low doses of LPS enhance proliferation and decrease the apparent threshold level for cell activation, prompting careful evaluation of allergen stimulated T cell activation in vitro. Copyright (C) 2007 S. Karger AG, Basel.

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