Clinical and immunobiochemical characterization of airborne Delonix regia (Gulmohar tree) pollen and cross-reactivity studies with Peltophorum pterocarpum pollen: 2 dominant avenue trees from eastern India
Autor: | Jyotshna Mandal, Swati Gupta-Bhattacharya, Pampa Chakraborty, Indrani Roy, Prasenjit Manna |
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Rok vydání: | 2009 |
Předmět: |
Adult
Male Pulmonary and Respiratory Medicine Adolescent Blotting Western Immunoblotting Immunology India Enzyme-Linked Immunosorbent Assay Cross Reactions Biology medicine.disease_cause Binding Competitive Histamine Release Cross-reactivity Trees Young Adult Forced Expiratory Volume Pollen Botany Hypersensitivity Respiratory Hypersensitivity otorhinolaryngologic diseases medicine Humans Immunology and Allergy Polyacrylamide gel electrophoresis Glycoproteins Plant Proteins Skin Tests Gel electrophoresis Plant Extracts Peltophorum pterocarpum Rhinitis Allergic Seasonal Fabaceae Antigens Plant Immunoglobulin E Middle Aged biology.organism_classification Asthma Staining Sephadex Electrophoresis Polyacrylamide Gel Female Delonix regia |
Zdroj: | Annals of Allergy, Asthma & Immunology. 103:515-524 |
ISSN: | 1081-1206 |
DOI: | 10.1016/s1081-1206(10)60269-4 |
Popis: | Background: Delonix regia and Peltophorum pterocarpum pollen are important aeroallergens for type 1 hypersensitivity in the tropics. The IgE-binding proteins of D regia and their cross-allergenity with P pterocarpum pollen have not been evaluated. Objectives: To isolate and characterize the IgE-binding proteins of D regia pollen for the first time and to investigate the cross-allergenity with P pterocarpum pollen belonging to the same family (Leguminosae). Methods: Allergenic activities were determined by in vivo and in vitro analyses. Pollen extract was fractionated by a combination of 2 columns (diethyl amino ethyl Sephadex and Sephacryl S-200). Protein components were characterized by sodium dodecyl sulfate–polyacrylamide gel electrophoresis, periodic acid–Schiff staining, and immunoblotting. In vitro inhibition tests were performed to evaluate the cross-reactivity. Results: The skin prick test results of the patients with respiratory allergies in Calcutta, India, showed 31.1% positivity with D regia pollen. Nine IgE-reactive protein components were found in the crude extract. An optimum IgE-reactive fraction was resolved into 4 subfractions. Subfraction A, which showed maximum IgE reactivity, contained 2 (96- and 66-kDa) IgE-reactive protein components. The 66-kDa component was found to be glycoprotein. Remarkable cross-reactivity between D regia and P pterocarpum pollen was found on IgE enzyme-linked immunosorbent assay inhibition and dot blotting. Shared IgE-binding components (66, 56, 32, 28, 25, and 23 kDa) were observed between D regia and P pterocarpum pollen extracts, whereas the 96- and 43-kDa components were specific to D regia. Conclusion: The purification of the IgE-binding proteins and the identification of the shared/cross-reactive proteins in these taxonomically related pollen members should be helpful for the diagnosis and therapy of patients susceptible to these pollens. Ann Allergy Asthma Immunol. 2009;103:515–524. |
Databáze: | OpenAIRE |
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