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  • 2005-2009  (3)
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  • 1
    Electronic Resource
    Electronic Resource
    Poor association between allergen-specific serum immunoglobulin E levels, skin sensitivity and basophil degranulation: a study with recombinant birch pollen allergen Bet v 1 and an immunoglobulin E detection system measuring immunoglobulin E capable of binding to FcɛRI (2005)
    Oxford, UK : Blackwell Science Ltd
    Clinical & experimental allergy 35 (2005), S. 0 
    Details
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background Results from several studies indicate that the magnitude of immediate symptoms of type I allergy caused by allergen-induced cross-linking of high-affinity Fcɛ receptors on effector cells (mast cells and basophils) is not always associated with allergen-specific IgE levels.Objective To investigate the association of results from intradermal skin testing, basophil histamine release and allergen-specific IgE, IgG1–4, IgA and IgM antibody levels in a clinical study performed in birch pollen-allergic patients (n=18).Methods rBet v 1-specific IgEs were measured by quantitative CAP measurements and by using purified FcɛRI-derived α-chain to quantify IgE capable of binding to effector cells. Bet v 1-specific IgG subclasses, IgA and IgM levels were measured by ELISA, and basophil histamine release was determined in whole blood samples. Intradermal skin testing was performed with the end-point titration method.Results Our study demonstrates on the molecular level that the concentrations of allergen-specific IgE antibodies capable of binding to FcɛRI and biological sensitivities are not necessarily associated. A moderate association was found between cutaneous and basophil sensitivity.Conclusion Our results highlight the quantitative discrepancies and limitations of the present diagnostic tools in allergy, even when using a single allergenic molecule. The quantity of allergen-specific serum IgE is only one component of far more complex cellular systems (i.e. basophil-based tests, skin tests) used as indirect diagnostic tests for IgE-mediated allergic sensitivity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2222.2005.02156.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Comparison of purified Dermatophagoides pteronyssinus allergens and extract by two-dimensional immunoblotting and quantitative immunoglobulin E inhibitions (2005)
    Oxford, UK : Blackwell Science Ltd
    Clinical & experimental allergy 35 (2005), S. 0 
    Details
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background The allergens of the house dust mite (Dermatophagoides pteronyssinus, Der p), one of the most important indoor allergen sources, occur as isoallergens that differ in their amino acid sequence. These variations may influence allergenic activity and thus may have impact on diagnostic tests and specific immunotherapy.Objective We investigated whether single purified recombinant mite allergens contain the IgE epitopes of the natural Der p isoallergens.Methods A panel of purified recombinant (rDer p 2, 5, 7, 8, 10 and 14) and two natural (nDer p 1 and 4) mite allergens were used to establish IgE reactivity profiles of Der p allergic patients and to inhibit IgE reactivity to two-dimensionally separated Der p isoallergens. In addition, we determined the percentage of Der p extract-specific IgE which could be preadsorbed with a mixture of purified mite allergens (nDer p 1, rDer p 2, 5, 7, 8 and 10) from sera of mite-allergic patients (n=18) in a non-denaturing RAST-based inhibition.Results We demonstrate that single recombinant mite allergens inhibit IgE reactivity to the corresponding natural isoallergens. A mixture of purified mite allergens (nDer p 1, rDer p 2, 5, 7, 8 and 10) bound on an average 76% of Der p-specific IgE antibodies.Conclusion The studied recombinant and natural mite allergens contain a large portion of Der p-specific IgE and may be used for diagnostic tests and therapy of Der p allergy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2222.2005.02345.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Development of an in vitro system for the study of allergens and allergen-specific immunoglobulin E and immunoglobulin G: Fcɛ receptor I supercross-linking is a possible new mechanism of immunoglobulin G-dependent enhancement of type I allergic reactions (2005)
    Oxford, UK : Blackwell Publishing
    Clinical & experimental allergy 35 (2005), S. 0 
    Details
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background IgE-dependent activation of mast cells (MCs) is a key pathomechanism of type I allergies. In contrast, allergen-specific IgG Abs are thought to attenuate immediate allergic reactions by blocking IgE binding and by cross-linking the inhibitory Fcγ receptor IIB on MCs.Objectives To establish a defined in vitro system using human MCs to study the biological activity of allergens and to investigate the role of allergen-specific IgE and IgG.Methods Purified human intestinal MCs sensitized with different forms of specific IgE Abs were triggered by monomeric and oligomeric forms of recombinant Bet v 1, the major birch pollen allergen, in the presence or absence of allergen-specific IgG Abs.Results MCs sensitized with an anti-Bet v 1 IgE mAb or sera obtained from birch pollen allergic patients released histamine and sulphidoleukotrienes after exposure to oligomeric Bet v 1. Monomeric Bet v 1 provoked mediator release only in MCs sensitized with patients sera but not in MCs sensitized with anti-Bet v 1 IgE mAb. Interestingly, MC activation could be induced by supercross-linking of monomeric Bet v 1 bound to monovalent IgE on MCs with a secondary allergen-specific IgG pAb. By using IgG F(ab′)2 fragments we provide evidence that this effect is not a result of IgG binding to Fcγ receptors.Conclusion This assay represents a new tool for the in vitro study of MC activation in response to natural and genetically modified allergens. Fcɛ receptor I supercross-linking by allergen-specific IgG Abs provides a possible new mechanism of IgG-dependent enhancement of type I allergic reactions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2222.2005.02248.x
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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