Isolation and characterization of a novel 98-kd Dermatophagoides farinae mite allergen
Autor: | Ren-Bin Tang, Tsu-Chung Chang, Bo-Liang Lee, Mei-Whey Hung, Horng-Der Shen, Lai-Chen Tsai, Pei-Ling Chao, Kaw Yan Chua, Zo-Nan Chang |
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Rok vydání: | 1998 |
Předmět: |
Male
Allergy Adolescent Molecular Sequence Data Immunology Biology Immunoglobulin E medicine.disease_cause Chromatography Affinity Mice Allergen Antigen Affinity chromatography immune system diseases Lectins medicine Mite Animals Humans Immunology and Allergy Amino Acid Sequence Antigens Dermatophagoides Antigens Child Glycoproteins Mice Inbred BALB C Mites Sequence Homology Amino Acid medicine.diagnostic_test Pyroglyphidae Antibodies Monoclonal Allergens biology.organism_classification medicine.disease respiratory tract diseases Molecular Weight Mannose-Binding Lectins Immunoassay biology.protein Female Plant Lectins |
Zdroj: | Journal of Allergy and Clinical Immunology. 102:295-303 |
ISSN: | 0091-6749 |
Popis: | Background: Exposure to allergens from house dust mites is a significant cause of immediate hypersensitivity. Thus far, the active mite allergens defined are low molecular weight (MW) proteins or glycoproteins. However, other important mite allergens remain to be investigated. In this study a high MW mite antigen with a high IgE-binding activity was characterized. Methods: An anti- Dermatophagoides farinae (Df) monoclonal antibody, mAb642, which recognized a 98-kd allergenic mite protein, was used for affinity chromatography. The purified Df642 was characterized biochemically and immunologically. Results: Competitive ELISA demonstrated that mAb642 was inhibited by the interaction between serum IgE from allergic patients and Df642 antigen in a dose-dependent fashion. The IgE reactivity to both 98-kd and 92-kd components was removed or diminished by preincubation of asthmatic sera with Df642-coated CNBr-activated cellulose-4B gel. Two-dimensional immunoblot analysis revealed that there are at least 4 isoforms of Df642 that represent a minor component in the crude mite extract. The allergenicity of Df642 was assayed by IgE immunoassay with a large panel of 67 sera from asthmatic patients with positive skin reactions, and Df 642 showed positive IgE reactivity with more than 80% of the sera tested. Thus it should be classified as an important allergen. In addition, amino acid sequence analysis revealed that Df642 shares more than 50% homology with paramyosin from invertebrates. Conclusion: We have identified and characterized a 98-kd house dust mite allergen that showed greater than 80% IgE reactivity with sera from patients allergic to mites. This is the first high MW allergen characterized to date, and it shares high sequence homology with paramyosins in invertebrates. (J Allergy Clin Immunol 1998;102:295-303.) |
Databáze: | OpenAIRE |
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