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  • 1
    Digitale Medien
    Digitale Medien
    Oxford, UK : Munksgaard International Publishers
    Allergy 58 (2003), S. 0 
    ISSN: 1398-9995
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Background: Millet has been reported to induce not very frequent but severe anaphylactic reactions following ingestion. Seven individuals who all kept cage birds experienced allergic reactions after ingestion of millet-containing food.Methods: We investigated the immunoglobulin E (IgE)-reactivity of these individuals to millet employing immunoblotting, RAST and skin prick tests. As the sensitization possibly occurred via the inhalant route we investigated millet-specific IgE levels of 16 additional sera from bird keepers with proven atopy, in retrospect.Results: All patients who had experienced reactions after ingestion of millet displayed millet-specific IgE. Sixty-three percent of the atopic bird keepers possessed millet-specific IgE. By means of immunoblotting three major allergens in millet extract were detected.Conclusions: Our results indicate that millet plays an important role as inhalant allergen for atopic bird keepers. A sensitization to millet may subsequently also elicit food allergy.
    Materialart: Digitale Medien
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  • 2
    ISSN: 1398-9995
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Background:  Germins and the related germin-like proteins (GLPs) are glycoproteins expressed in many plants in response to biotic and abiotic stress. To test the potential impact of germins and GLPs, recombinant germin from Triticum aestivum (tGermin) and GLPs from Arabidopsis thaliana (tGLP), both produced in transformed tobacco plants, were used.Methods:  Sera from 82 patients with type I allergy to birch, grass or mugwort pollen and/or wheat were tested in immunoblot for IgE binding to tGermin and tGLP, and the IgE reactivity after chemical and enzymatic deglycosylation was analysed. The biological activity of tGermin and tGLP was determined in a histamine release assay and in skin prick testing (SPT).Results:  In an immunoblotting assay, 24 out of 82 tested sera (29.26%) from allergic patients showed IgE-binding to tGermin, and 18 of these sera (21.95%) displayed also IgE-binding to tGLP. The deglycosylation experiments indicated that glycan moieties contribute significantly to the IgE-binding of tGermin and tGLP. Both tGermins and tGLP induced specifically histamine release in an invitro assay as well as in SPT.Conclusion:  Our in vitro and in vivo findings demonstrate that germin and GLPs are capable to bind IgE most likely via carbohydrate determinants, and represent allergenic molecules.
    Materialart: Digitale Medien
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  • 3
    ISSN: 1365-2222
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Background Allergy to celery is often associated with sensitization to birch and/or mugwort pollen.Objective and methods In a multi-centre study, sera from 23 patients suffering from type I allergy to celery and 15 patients with positive celery RAST but wo clinical sensitization were compared. To examine whether cross-reactivity between celery and mugwort pollen iticludes cross-sensitization to birch pollen allergens, we determined cross-reacting structures in birch pollen, mugwort pollen and celery by means of immunoblotting. Inhibition studies were performed by preincubation of sera with extracts of birch pollen, mugwort pollen, and celery.Results We identified three groups of proteins—homologues of Bet v I and birch profilin (Bet v 2) as well asa group of proteins with a molecular range of 46 to 60 kD—displaying IgE-cross-reactivity, which were shared by birch pollen and celery. Two of these groups of allergens (profilin and the 46 to 60 kD proteins) were also present in mugwort pollen. In this paper we demonstrate that most cross-reacting allergens present in mugwort pollen and celery can also be detected in birch pollen extract.Conclusion Therefore we propose, from a serological point of view, to extend the mugwort-celery syndrome to the birch-mugwort-celery syndrome.
    Materialart: Digitale Medien
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  • 4
    ISSN: 1365-2222
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Background In the last 10 years type-I allergy against proteins from Hevea brasiliensis latex has become an acknowledged medical issue. Fruit-allergic patients represent one risk group for developing latex allergy. Class I chitinases have been identified from chestnut, avocado and banana as relevant allergens. The chitin binding (hevein) domain from these class I chitinases has been postulated to bear the important IgE binding epitopes.Objective To clone the cDNA of an allergenic latex class I chitinase, to express the recombinant protein and to determine its IgE cross-reactivity with hevein (Hev b 6.02).Methods A full-length cDNA coding for a class I chitinase has been isolated from Hevea latex RNA by reverse transcription followed by PCR. The chitinase encoding sequence has been subcloned into the pMAL expression vector and expressed in E. coli as a fusion protein to maltose binding protein. The highly enriched recombinant protein fraction has been tested for its IgE binding capacity in immunoblots and ELISA. Furthermore, the pathogenesis-related function of the recombinant protein was tested in a fungal growth inhibition assay.Results The Hevea brasiliensis latex chitinase, designated Hev b 11, displays 70% identity to the endochitinase from avocado and its hevein-domain 58% to hevein (Hev b 6.02). The recombinant Hev b 11-maltose binding protein is recognized by latex- and fruit-allergic patients with IgE binding in both, ELISA and immunoblots. Pre-incubation of sera with rHev b 11-maltose binding protein showed an overall 16% inhibition of subsequent binding to rHev b 6.02-maltose binding protein on solid phase. The growth of F. oxysporum was inhibited in a dose dependent manner by addition of rHev b 11-maltose binding protein to the culture.Conclusions Hev b 11, a class I chitinase, is another allergen from Hevea latex with a chitin binding domain and displays a different IgE binding capacity compared with hevein.
    Materialart: Digitale Medien
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  • 5
    ISSN: 1365-2222
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Background Type I allergy represents a severe health problem in industrialized countries where up to 20% of the population suffer froin allergic rhinitis, conjunctivitis and allergic asthma bronchiale and in severe cases from anaphylaxis. leading to death.Objective The aim of this study was to evaluate recombinant Bet v I, the major birch pollen allergen for in vivo and in vitro diagnosis of birch pollen allergy.Methods A group of 51 birch pollen allergic patients and eight non-allergic control individuals were tested for birch pollen allergy by skin-prick and intradennal testing, comparing commercial birch pollen extracts with recombinant Bet v I. Quantitative and qualitative serological testing was done with natural and recombinant allergens by radioallergosorbent test (RAST), enzyme-linked immunosorbent assay (ELISA) and immunoblotting.Results Recombinant Bet v I allowed accurate in vivo and in vitro diagnosis of tree pollen allergy in 49/51 patients tested. No false positive results were obtained in any in vitro assay system (ELISA. Westernblot) or by skin testing (skin-prick, intradermal test) with recombinant Bet v I.Conclusion Our results document that recombinant Bet v I produced in bacterial expression systems allows accurate in vitro and in vivo diagnosis of birch pollen allergy in 〉 95% of birch pollen allergic patients.
    Materialart: Digitale Medien
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  • 6
    ISSN: 1365-2222
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Background IgE antibodies specific for the major birch-pollen allergen, Bet v 1, cross-react with homologous allergens in particular foods, e.g. apples, carrots and hazelnuts. In a high number of tree pollen-allergic individuals, this cross-reactivity causes clinical symptoms, commonly known as the ‘birch-fruit-syndrome’.Objective To characterize the T cell response to the Bet v 1-related major allergen in hazelnuts, Cor a 1.04, and its cellular cross-reactivity with Bet v 1 and the homologous hazel pollen allergen, Cor a 1.Methods Using recombinant Cor a 1.04, T cell lines (TCL) and T cell clones (TCC) were established from peripheral blood mononuclear cells of tree pollen-allergic patients with associated food allergy. T cell epitopes were determined using overlapping synthetic peptides in Cor a 1.04-reactive TCL and TCC. In parallel, reactivity to Bet v 1 and Cor a 1 was tested.Results In total, 20 distinct T cell epitopes on the hazelnut allergen were identified. Several Cor a 1.04-specific TCL and TCC reacted with pollen allergens albeit less pronounced than with the hazelnut allergen. Several Cor a 1.04-specific TCC did not react with pollen allergens. Interestingly, these clones were found to react with the Bet v 1-related major allergen in carrots, Dau c 1. The cellular cross-reactivity between both food allergens could be associated with the most frequently recognized T cell epitope of Cor a 1.04, Cor a 1.04142–153.Conclusions The major hazelnut allergen cross-reacts with the major allergens of birch and hazel pollen but apparently contains a relevant T cell epitope not shared with pollen allergens. Our finding may have important implications for the specific immunotherapy of tree pollen-allergic patients suffering from concomitant hazelnut allergy.
    Materialart: Digitale Medien
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  • 7
    Digitale Medien
    Digitale Medien
    Oxford, UK : Blackwell Publishing Ltd
    Clinical & experimental allergy 27 (1997), S. 0 
    ISSN: 1365-2222
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Background Animal hair/dander proteins frequently cause Type I hypersensitivities. Species-specific and broadly cross-reacting allergens have been characterized in the past.Methods Sera from eight individuals suffering from symptoms due to exposure to deer and deer-derived products were investigated by immunoblotting. Extracts from deer, dog, cat, horse, rabbit and cow, respectively, were tested for IgE-binding. To reveal cross-reactivities patients' sera were preadsorbed with these extracts prior to testing with deer extract.Results Deer allergens with the molecular mass of 22 and 25 kD (major allergens), as well as 60 kD were identified. The 22 and 25 kD allergens are cross-reactive with the corresponding cow allergens.Conclusions Deer allergy is a rare sensitization mainly affecting persons exposed to deer, who displayed an atopie disposition. From our results it can be assumed that this hypersensitivity is partly associated with allergy to cow dander.
    Materialart: Digitale Medien
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  • 8
    Digitale Medien
    Digitale Medien
    Oxford, UK : Blackwell Publishing Ltd
    Clinical & experimental allergy 23 (1993), S. 0 
    ISSN: 1365-2222
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Type I allergy to pollen of the European chestnut (Castanea sativa) represents a major cause of pollinosis in (sub) Mediterranean areas. Using sera from 14 patients with established allergy to pollen of the European chestnut, 13/14 sera (92%) showed IgE-binding to a 22 kD protein, 2/14(14%) displayed additional binding to a 14 kD protein and 1/14 (7%) bound only to the 14 kD protein of European chestnut pollen extract. Two monoclonal mouse antibodies, BIP 1 and BIP 4, directed against different epitopes of Bet v I (the major birch pollen allergen), and a rabbit antibody to recombinant birch profilin (rBet v II) were used to characterize the proteins of the European chestnut pollen. The recombinant birch pollen allergens, r Bet v I and r Bet v II (profilin) were employed to show common allergenic structures on proteins from both birch and European chestnut pollen by IgE-inhibition experiments. Despite the fact that the 22 kD protein displayed a higher molecular weight in comparison to the 17 kD major birch pollen allergen, Bet v I, we could demonstrate reactivity of both monoclonal antibodies, BIP 1 and BIP 4, with this protein. A complete inhibiton of IgE-binding to this 22 kD protein was shown by pre-incubating sera with purified recombinant Set r I. In addition, the 14kD protein could be identified by IgE-inhibition studies with recombinant Bet v II and by using a rabbit anti-profilin antibody as the profilin from pollen of the European chestnut.
    Materialart: Digitale Medien
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  • 9
    Digitale Medien
    Digitale Medien
    Oxford, UK : Blackwell Publishing Ltd
    Clinical & experimental allergy 22 (1992), S. 0 
    ISSN: 1365-2222
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: During the last few years Limulus Amoebocyte Lysate (LAL) has been extensively used to detect minimal amounts of endotoxins of Gram-negative bacteria in products of the pharmaceutical industry, in food stuff, body fluids, house dust and room air. LAL is produced from cells of the haemolymph (amoebocytes) of the horseshoe crab (Limulus polyphemus), which respond with an extremely sensitive clotting system upon contact with endotoxins. In this study we demonstrate by typical case history, positive skin test and ELISA the occurrence of Type I allergy to LAL in a patient suffering from conjunctivitis and rhinitis at work.
    Materialart: Digitale Medien
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  • 10
    Digitale Medien
    Digitale Medien
    Oxford, UK : Blackwell Publishing Ltd
    Clinical & experimental allergy 24 (1994), S. 0 
    ISSN: 1365-2222
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: In this study, sera collected from 50 patients (24 females, 26 males) with Type I allergy to house dust mite (Dermatophagoides pteronyssinus) were investigated for IgE antibodies specific for eight different mite species including storage mites of the families Pyroglyphidae, Glycyphagidae and Acaridae. According to their environment the patients were divided into two groups. Group I consisted of 24 (11 women, 13 men) farmers working and living in rural regions of Austria (Styria. Lower Austria), group II included 26 citizens of Vienna (13 women, 13 men). As expected, RAST investigations revealed a higher rate of sensitization to storage mites in the farmer group. Comparing the two patient groups, sensitization to Lepidoglyphus destructor and Tyrophagus putreus was markedly increased in the farmer group. However, the sensitizalion rate to storage miles was also considerably high in city dwellers. Elevated levels of IgE specific for Euroglyphus maynei were more frequently observed in the urban collective. RAST-inhibition experiments suggest a partial crossreactivity between house dust mites and storage mites. In their living environment, patients with perennial Type I allergy are exposed to multiple different mite-derived allergens in addition to the well-known house dust mite allergens. These allergens lead to sensitization and are therefore of clinical importance.
    Materialart: Digitale Medien
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