Allergy to Salsola Kali in a Salsola incanescens-rich area: role of extensive cross allergenicity.
ABSTRACT Pollens from the Salsola spp. are an important source of respiratory allergy in tropical countries. Our aim was to characterize the IgE binding proteins of S. incanescens pollen extract and study its cross-reactivity with S. kali pollen allergens.
Prick tests with S. kali and S. incanescens pollen extracts were performed on eight respiratory allergy patients from Mashhad, Northeast Iran. The antigenic profiles and IgE-binding patterns of S. kali and S. incanescens pollen extracts were compared by SDS-PAGE and Western blotting, using individual sera from the salsola pollen-sensitive patients. Cross-reactivity of proteins in the two weeds was assessed by IgE- immunoblotting inhibition.
S. kali and S. incanescens pollen extracts showed similar IgE-binding profiles in Western blotting. The IgE binding components of 39, 45, 66 and 85 kDa were detected in both pollen extracts. Furthermore, inhibition of the immunoblots revealed extensive inhibition of IgE binding to proteins and a close relationship between these two weeds allergens.
S. incanescens pollen is a potent allergen source with several IgE binding components that shows a close allergenic relationship with S. kali. Our results suggest that in S. incanescens-rich areas, S. kali pollen extracts could be used as a diagnostic reagent for allergic patients to S. incanescens pollen.
SourceAvailable from: Mohammad Ali Assarehzadegan[Show abstract] [Hide abstract]
ABSTRACT: ackground: Pollens from mesquite (Prosopis juliflora) are potent allergen responsible for causing immediate hypersensitivity reactions in susceptible people fromin tropical countries. Objective: This study aimed to clone, express and purify the mesquite pollen profilin (Pro j 2) as well as evaluating its nucleotide sequence homology in order to predict allergenic cross-reactivity with profilins of common allergenic plants. Methods: Immunoblotting assay and specific ELISA were applied to determine the immunoreactivity of sera from 35 patients who were allergic to mesquite pollen. The mesquite profilin-coding sequence was cloned into PTZ57R/T vector and amplified. The cDNA of mesquite pollen profilin was then expressed in Escherichia coli using pET-21b (+) vector and puriﬁed by one-step Ni2+ aﬃnity chromatography. IgE binding capacity of the recombinant mesquite profiling (rPro j 2) was analyzed by specific ELISA, immunoblotting, and inhibition assays. Results: cDNA nucleotide sequencing revealed an open reading frame of 399bp encoding for 133 aminoacid residues which belonging to the profilin family. Seventeen patients (17/35, 48.57%) had significant specific IgE level for rPro j 2. Immunodetection and inhibition assays indicated that puriﬁed rPro j 2 might be similar as that in the crude extract. Conclusion: Pro j 2, as a new allergen from mesquite pollen, was produced in E. coli with an IgE-reactivity similar to that of its natural counterpart. The amino acid sequences homology analysis of mesquite profilin and several profilin molecules from other plants showed high degree of cross-reactivity among plant-derived profilins from unrelated families.Asian Pacific journal of allergy and immunology / launched by the Allergy and Immunology Society of Thailand 06/2015; 33(2). DOI:10.12932/AP0507.33.2.2015 · 1.26 Impact Factor
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ABSTRACT: Many pieces of evidence such as the synchraneity of seasonal variation in allergic symptoms with the rhythm of plant pollination suggest that pollen is one of the most probable causes of allergy. The aim of this study was the studying of pollens allergenicity in Chenopodium album and Chenopodium botrys. C. album and C. botrys grows commonly in different parts of the Iran. Pollens of these were collected from area of Tehran, Karaj city and around Kandovan. Pollens were extracted using phosphate-buffered saline, PH 7.4. Male guinea pigs were sensitized and treated with C.album and C. botrys pollen extracts and skin prick tests were performed on guinea pigs and quantified on the basis of wheal diameter. After treatment with pollen extracts, the guinea pigs blood was obtained directly from the heart and sera from samples were stored at-20ºc until analyzed. During the skin prick test, the allergenic sensitivity was observed for C.album pollen grains, with an average wheal diameter of about 4 cm and for C. botrys pollen grains, with an average wheal diameter of about 2/5 cm. Results of blood smears were seen that, the numbers of eosinophils, neutrophils and amount of IgE were increased in the animals treated with pollen extracts than in the control group.
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ABSTRACT: 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 IgEimmunoblotting. 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 66kDa. However, there were other IgE reactive protein bands among the patients' sera with molecular weights of 10, 15, 35, 45, 55 and 85kDa. 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.Iranian journal of allergy, asthma, and immunology 02/2015; 14(1):74-82. · 1.01 Impact Factor