Literature DB >> 81221

Reactivity of ragweed allergens with IgE antibodies. Analyses by leukocyte histamine release and the radioallergosorbent test and determination of cross-reactivity.

C Adolphson, L Goodfriend, G J Gleich.   

Abstract

Five distinct proteins with allergenic activity have been isolated from short ragweed pollen. We initially tested three of these, AgE, AgK, and Ra3, for reactivity with IgE antibodies by leukocyte histamine release and by the radioallergosorbent test (RAST). We found highly significant correlations between the reactivities of these allergens by leukocyte histamine release and by the RAST, consistent with the view that both procedures detected comparable allergenic activity. We next tested the allergenic cross-reactivity of all five ragweed allergens. AgE, AgK, Ra3, Ra4, and Ra5, by RAST inhibition. With solid-phase AgE the only nonhomologous inhibitor was AgK, which cross-reacted weakly and required a 140-fold mass excess of AgK compared to AgE. With solid-phase AgK both AgK and AgE produced significant inhibition; AgE was slightly more potent than the homologous AgK, Ra3 and Ra5 were allergenically unique, because only the homologous allergen produced 50% inhibition. Ra4 was weakly inhibited by AgE, Ra3, and Ra5 when these allergens were added in 300- to 5---fold mass excesses; this weak inhibition may represent either cross-reaction or cross-contamination. We found that RAST inhibition could be used as an assay for the individual ragweed allergens and we demonstrated the presence of all of the allergens in a whole ragweed extract. The sensitivity of the RAST inhibition assay ranged from 10 ng to 100 ng for 50% inhibition. Finally, the solid-phase ragweed allergens were used to determine the frequency of elevated IgE antibody levels in 65 patients with ragweed hay fever. Virtually all of the patients reacted with AgE (97%), while 88% reacted with AgK, 51% reacted with Ra3, 28% reacted with Ra4, and 17% reacted with Ra5. These results highlight the usefulness of the RAST as a specific and sensitive tool for immunochemical studies of allergens.

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Year:  1978        PMID: 81221     DOI: 10.1016/0091-6749(78)90208-7

Source DB:  PubMed          Journal:  J Allergy Clin Immunol        ISSN: 0091-6749            Impact factor:   10.793


  7 in total

Review 1.  Biology of weed pollen allergens.

Authors:  Gabriele Gadermaier; Azra Dedic; Gerhard Obermeyer; Susanne Frank; Martin Himly; Fatima Ferreira
Journal:  Curr Allergy Asthma Rep       Date:  2004-09       Impact factor: 4.806

2.  Sequence conservation predicts T cell reactivity against ragweed allergens.

Authors:  J Pham; C Oseroff; D Hinz; J Sidney; S Paul; J Greenbaum; R Vita; E Phillips; S Mallal; B Peters; A Sette
Journal:  Clin Exp Allergy       Date:  2016-07-26       Impact factor: 5.018

3.  Different patterns of antigen-induced histamine release during immunotherapy in insect venom and pollen allergy.

Authors:  H G Nüsslein; M Kleinlein; B Hemmerlein; J R Kalden
Journal:  Agents Actions       Date:  1986-04

Review 4.  New insights into ragweed pollen allergens.

Authors:  Véronique Bordas-Le Floch; Rachel Groeme; Henri Chabre; Véronique Baron-Bodo; Emmanuel Nony; Laurent Mascarell; Philippe Moingeon
Journal:  Curr Allergy Asthma Rep       Date:  2015-11       Impact factor: 4.806

5.  Antigens and allergens in Dermatophagoïdes farinae mite. I. Immunochemical and physicochemical study of two allergenic fractions from a partially-purified Dermatophagoïdes farinae mite extract.

Authors:  J Le Mao; J P Dandeu; J Rabillon; M Lux; B David
Journal:  Immunology       Date:  1981-10       Impact factor: 7.397

6.  Identification of Novel Short Ragweed Pollen Allergens Using Combined Transcriptomic and Immunoproteomic Approaches.

Authors:  Véronique Bordas-Le Floch; Maxime Le Mignon; Julien Bouley; Rachel Groeme; Karine Jain; Véronique Baron-Bodo; Emmanuel Nony; Laurent Mascarell; Philippe Moingeon
Journal:  PLoS One       Date:  2015-08-28       Impact factor: 3.240

7.  Purification and biochemical characterization of Hel a 6, a cross-reactive pectate lyase allergen from Sunflower (Helianthus annuus L.) pollen.

Authors:  Nandini Ghosh; Gaurab Sircar; Claudia Asam; Martin Wolf; Michael Hauser; Sudipto Saha; Fatima Ferreira; Swati Gupta Bhattacharya
Journal:  Sci Rep       Date:  2020-11-19       Impact factor: 4.379

  7 in total

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