Identification of a 53kDa protein, as a new high molecular weight allergen from fraxinusexcelsior (Ash) pollen
Background Fraxinus excelsior (Ash) is a common tree and is important cause of winter–spring pollinosis in many temperate regions in the world. In this study, a high molecular weight allergen from ash pollen was identified. Methods In all, 20 individuals allergic to ash participated in the stud...
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Springer Medizin
2021
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| Online Access: | https://link.springer.com/article/10.1007%2Fs40629-020-00129-3 http://hdl.handle.net/11408/4160 |
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| author | Shoushtari, Maryam Sharif Majd, Ahmad Assarehzadegan, Mohammad-Ali Fanuel, Songwe Moin, Mostafa Nejadsattari, Taher Shoormasti, Raheleh Shokouhi Badalzadeh, Mohsen Tajik, Shaghayegh Fazlollahi, Mohammad Reza Tayebi, Behnoosh Pourpak, Zahra Kardar, Gholam Ali |
| author_facet | Shoushtari, Maryam Sharif Majd, Ahmad Assarehzadegan, Mohammad-Ali Fanuel, Songwe Moin, Mostafa Nejadsattari, Taher Shoormasti, Raheleh Shokouhi Badalzadeh, Mohsen Tajik, Shaghayegh Fazlollahi, Mohammad Reza Tayebi, Behnoosh Pourpak, Zahra Kardar, Gholam Ali |
| author_sort | Shoushtari, Maryam Sharif |
| collection | DSpace |
| description | Background
Fraxinus excelsior (Ash) is a common tree and is important cause of winter–spring pollinosis in many temperate regions in the world. In this study, a high molecular weight allergen from ash pollen was identified.
Methods
In all, 20 individuals allergic to ash participated in the study. Characterization and immunoreactivity of ash pollen proteins was performed using sodium dodecyl sulfate polyacrylamide electrophoresis (SDS-PAGE), two-dimensional (2D) gel electrophoresis and immunoblotting.
Results
Immunoglobulin E (IgE)-binding proteins with apparent molecular mass ranging from 9 to 110 kDa were detected in ash pollen extract. Serum IgE of 7 (35%) patients reacted with a 53-kDa protein band. Analysis of 2D immunoblots showed several IgE-binding proteins. Moreover, mass spectrometry analysis indicated that the 53-kDa allergen was homologous to calreticulin.
Discussion
We defined a novel allergen from F. excelsior pollen with a molecular weight of about 53 kDa. This allergen could be considered as an important high molecular weight allergenic protein for further studies on cross-reactivity and development of diagnostic and therapeutic approaches. |
| format | Article |
| id | ir-11408-4160 |
| institution | My University |
| language | English |
| publishDate | 2021 |
| publisher | Springer Medizin |
| record_format | dspace |
| spelling | ir-11408-41602022-06-27T13:49:06Z Identification of a 53kDa protein, as a new high molecular weight allergen from fraxinusexcelsior (Ash) pollen Shoushtari, Maryam Sharif Majd, Ahmad Assarehzadegan, Mohammad-Ali Fanuel, Songwe Moin, Mostafa Nejadsattari, Taher Shoormasti, Raheleh Shokouhi Badalzadeh, Mohsen Tajik, Shaghayegh Fazlollahi, Mohammad Reza Tayebi, Behnoosh Pourpak, Zahra Kardar, Gholam Ali Ash pollen Allergen 2D electrophoresis IgE immunoblotting Calreticulin Background Fraxinus excelsior (Ash) is a common tree and is important cause of winter–spring pollinosis in many temperate regions in the world. In this study, a high molecular weight allergen from ash pollen was identified. Methods In all, 20 individuals allergic to ash participated in the study. Characterization and immunoreactivity of ash pollen proteins was performed using sodium dodecyl sulfate polyacrylamide electrophoresis (SDS-PAGE), two-dimensional (2D) gel electrophoresis and immunoblotting. Results Immunoglobulin E (IgE)-binding proteins with apparent molecular mass ranging from 9 to 110 kDa were detected in ash pollen extract. Serum IgE of 7 (35%) patients reacted with a 53-kDa protein band. Analysis of 2D immunoblots showed several IgE-binding proteins. Moreover, mass spectrometry analysis indicated that the 53-kDa allergen was homologous to calreticulin. Discussion We defined a novel allergen from F. excelsior pollen with a molecular weight of about 53 kDa. This allergen could be considered as an important high molecular weight allergenic protein for further studies on cross-reactivity and development of diagnostic and therapeutic approaches. 2021-05-11T10:32:19Z 2021-05-11T10:32:19Z 2020 Article 21970378 https://link.springer.com/article/10.1007%2Fs40629-020-00129-3 http://hdl.handle.net/11408/4160 en Allergo Journal International, Vol. 23: p. 233–239 open Springer Medizin |
| spellingShingle | Ash pollen Allergen 2D electrophoresis IgE immunoblotting Calreticulin Shoushtari, Maryam Sharif Majd, Ahmad Assarehzadegan, Mohammad-Ali Fanuel, Songwe Moin, Mostafa Nejadsattari, Taher Shoormasti, Raheleh Shokouhi Badalzadeh, Mohsen Tajik, Shaghayegh Fazlollahi, Mohammad Reza Tayebi, Behnoosh Pourpak, Zahra Kardar, Gholam Ali Identification of a 53kDa protein, as a new high molecular weight allergen from fraxinusexcelsior (Ash) pollen |
| title | Identification of a 53kDa protein, as a new high molecular weight allergen from fraxinusexcelsior (Ash) pollen |
| title_full | Identification of a 53kDa protein, as a new high molecular weight allergen from fraxinusexcelsior (Ash) pollen |
| title_fullStr | Identification of a 53kDa protein, as a new high molecular weight allergen from fraxinusexcelsior (Ash) pollen |
| title_full_unstemmed | Identification of a 53kDa protein, as a new high molecular weight allergen from fraxinusexcelsior (Ash) pollen |
| title_short | Identification of a 53kDa protein, as a new high molecular weight allergen from fraxinusexcelsior (Ash) pollen |
| title_sort | identification of a 53kda protein, as a new high molecular weight allergen from fraxinusexcelsior (ash) pollen |
| topic | Ash pollen Allergen 2D electrophoresis IgE immunoblotting Calreticulin |
| url | https://link.springer.com/article/10.1007%2Fs40629-020-00129-3 http://hdl.handle.net/11408/4160 |
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