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Immunochemical Characterization of Acacia Pollen Allergens and Evaluation of Cross-Reactivity Pattern with the Common Allergenic Pollens

Pollen from the Acacia has been reported as an important source of pollinosis in tropical and subtropical regions of the world. The aim of this study was to characterize the IgE binding protein of Acacia farnesiana pollen extract and evaluate cross-reactivity with the most allergenic pollens. In thi...

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Autores principales: Shamsbiranvand, Mohammad-Hosein, Khodadadi, Ali, Assarehzadegan, Mohammad-Ali, Borsi, Seyed Hamid, Amini, Akram
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4052195/
https://www.ncbi.nlm.nih.gov/pubmed/24949020
http://dx.doi.org/10.1155/2014/409056
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author Shamsbiranvand, Mohammad-Hosein
Khodadadi, Ali
Assarehzadegan, Mohammad-Ali
Borsi, Seyed Hamid
Amini, Akram
author_facet Shamsbiranvand, Mohammad-Hosein
Khodadadi, Ali
Assarehzadegan, Mohammad-Ali
Borsi, Seyed Hamid
Amini, Akram
author_sort Shamsbiranvand, Mohammad-Hosein
collection PubMed
description Pollen from the Acacia has been reported as an important source of pollinosis in tropical and subtropical regions of the world. The aim of this study was to characterize the IgE binding protein of Acacia farnesiana pollen extract and evaluate cross-reactivity with the most allergenic pollens. In this study, pollen extract was fractionated by SDS-PAGE and the allergenic profile was determined by IgE-immunoblotting and specific ELISA using forty-two Acacia allergic patients. Potential cross-reactivity among Acacia and selected allergenic plants was evaluated with ELISA and immunoblotting inhibition experiments. There were several resolved protein fractions on SDS-PAGE which ranged from 12 to 85 kDa. Several allergenic protein bands with molecular weights approximately between 12 and 85 kDa were recognized by IgE-specific antibodies from Acacia allergic patients in the immunoblot assay. The inhibition by the Prosopis juliflora pollen extract was more than those by other pollen extracts. Moreover, the wheal diameters generated by the Acacia pollen extract were highly correlated with those of P. juliflora pollen extracts. The findings suggest that several proteins such as 15, 23, 45, and 50 kDa proteins could be used as diagnostic and therapeutic reagents for patients allergic to A. farnesiana and P. juliflora.
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spelling pubmed-40521952014-06-19 Immunochemical Characterization of Acacia Pollen Allergens and Evaluation of Cross-Reactivity Pattern with the Common Allergenic Pollens Shamsbiranvand, Mohammad-Hosein Khodadadi, Ali Assarehzadegan, Mohammad-Ali Borsi, Seyed Hamid Amini, Akram J Allergy (Cairo) Research Article Pollen from the Acacia has been reported as an important source of pollinosis in tropical and subtropical regions of the world. The aim of this study was to characterize the IgE binding protein of Acacia farnesiana pollen extract and evaluate cross-reactivity with the most allergenic pollens. In this study, pollen extract was fractionated by SDS-PAGE and the allergenic profile was determined by IgE-immunoblotting and specific ELISA using forty-two Acacia allergic patients. Potential cross-reactivity among Acacia and selected allergenic plants was evaluated with ELISA and immunoblotting inhibition experiments. There were several resolved protein fractions on SDS-PAGE which ranged from 12 to 85 kDa. Several allergenic protein bands with molecular weights approximately between 12 and 85 kDa were recognized by IgE-specific antibodies from Acacia allergic patients in the immunoblot assay. The inhibition by the Prosopis juliflora pollen extract was more than those by other pollen extracts. Moreover, the wheal diameters generated by the Acacia pollen extract were highly correlated with those of P. juliflora pollen extracts. The findings suggest that several proteins such as 15, 23, 45, and 50 kDa proteins could be used as diagnostic and therapeutic reagents for patients allergic to A. farnesiana and P. juliflora. Hindawi Publishing Corporation 2014 2014-05-18 /pmc/articles/PMC4052195/ /pubmed/24949020 http://dx.doi.org/10.1155/2014/409056 Text en Copyright © 2014 Mohammad-Hosein Shamsbiranvand et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Shamsbiranvand, Mohammad-Hosein
Khodadadi, Ali
Assarehzadegan, Mohammad-Ali
Borsi, Seyed Hamid
Amini, Akram
Immunochemical Characterization of Acacia Pollen Allergens and Evaluation of Cross-Reactivity Pattern with the Common Allergenic Pollens
title Immunochemical Characterization of Acacia Pollen Allergens and Evaluation of Cross-Reactivity Pattern with the Common Allergenic Pollens
title_full Immunochemical Characterization of Acacia Pollen Allergens and Evaluation of Cross-Reactivity Pattern with the Common Allergenic Pollens
title_fullStr Immunochemical Characterization of Acacia Pollen Allergens and Evaluation of Cross-Reactivity Pattern with the Common Allergenic Pollens
title_full_unstemmed Immunochemical Characterization of Acacia Pollen Allergens and Evaluation of Cross-Reactivity Pattern with the Common Allergenic Pollens
title_short Immunochemical Characterization of Acacia Pollen Allergens and Evaluation of Cross-Reactivity Pattern with the Common Allergenic Pollens
title_sort immunochemical characterization of acacia pollen allergens and evaluation of cross-reactivity pattern with the common allergenic pollens
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4052195/
https://www.ncbi.nlm.nih.gov/pubmed/24949020
http://dx.doi.org/10.1155/2014/409056
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