Immunochemical Characterization of Prosopis Juliflora Pollen Allergens and Evaluation of Cross-Reactivity Pattern with the Most Allergenic Pollens in Tropical Areas

• Main Authors: Mohammad-Ali Assarehzadegan, Ali Khodadadi, Akram Amini, Abdol-Hosein Shakurnia, Seyed Saeid Marashi, Hosein Ali-Sadeghi, Farnoosh Zarinhadideh, Najmeh Sepahi
• Format: Article
• Language: English
• Published: Tehran University of Medical Sciences 2015-02-01
• Series: Iranian Journal of Allergy, Asthma and Immunology
• Subjects: Allergen; Cross Reaction; Pollen; Prosopis
• Online Access: https://ijaai.tums.ac.ir/index.php/ijaai/article/view/409

Allergy to Prosopis juliflora (mesquite) pollen is one of the common causes of respiratory allergy in tropical countries. Mesquite is widely used as street trees in towns and ornamental shade trees in parks and gardens throughout arid and semiarid regions of Iran. The inhalation of mesquite pollen and several species of Amaranthus/Chenopodiaceae family is the most important cause of allergic respiratory symptoms in Khuzestan province. This study was designed to evaluate IgE banding proteins of mesquite pollen extract and its IgE cross-reactivity with other allergenic plants. Twenty patients with allergic symptoms and positive skin prick tests (SPT) for mesquite pollen extract participated in the study. Crude pollen extract was prepared from local mesquite trees and used for the evaluation of allergenic profiles of P. juliflora pollen extract by Sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE) and IgE-immunoblotting. There were several protein bands in mesquite pollen extract using SDS-PAGE with the approximate range of molecular weight of 10-85 kDa. The most frequent IgE reactive bands among the patients' sera were approximately 20 and 66 kDa. However, there were other IgE reactive protein bands among the patients' sera with molecular weights of 10, 15, 35, 45, 55 and 85 kDa. Inhibition experiments revealed high IgE cross-reactivity between mesquite and acacia. There are several IgE-binding proteins in P. juliflora pollen extract. Results of this study indicate that proteins with a molecular weight of 10 to 85 kDa are the major allergens in P. juliflora pollen extract.