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Production and Use of Recombinant Profilins Amb a 8, Art v 4, Bet v 2, and Phl p 12 for Allergenic Sensitization Studies
Four recombinant (r) allergens (rAmb a 8.0101, rArt v 4.0101, rBet v 2.0101, and rPhl p 12.0101) were successfully produced and used for sensitization studies. The allergens belong to the profilin family which is one of the most numerous allergen families. These four proteins represent allergens ori...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7024262/ https://www.ncbi.nlm.nih.gov/pubmed/31963206 http://dx.doi.org/10.3390/molecules25020369 |
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author | Cudowska, Beata Kapingidza, A. Brenda Pawłowicz, Magdalena Pampuch, Agnieszka Hyduke, Noah Pote, Swanandi Schlachter, Caleb R. Lebensztejn, Dariusz M. Chruszcz, Maksymilian Kowal, Krzysztof |
author_facet | Cudowska, Beata Kapingidza, A. Brenda Pawłowicz, Magdalena Pampuch, Agnieszka Hyduke, Noah Pote, Swanandi Schlachter, Caleb R. Lebensztejn, Dariusz M. Chruszcz, Maksymilian Kowal, Krzysztof |
author_sort | Cudowska, Beata |
collection | PubMed |
description | Four recombinant (r) allergens (rAmb a 8.0101, rArt v 4.0101, rBet v 2.0101, and rPhl p 12.0101) were successfully produced and used for sensitization studies. The allergens belong to the profilin family which is one of the most numerous allergen families. These four proteins represent allergens originating from pollen of weeds (rAmb a 8.0101 and rArt v 4.0101), tree (rBet v 2.0101) and grass (rPhl p 12.0101). The recombinant allergens were characterized using various biochemical and biophysical methods and tested for their ability to bind patient-derived antibodies. One hundred patients aged 2 to 50 years sensitized to pollen and plant-derived food allergens (IgE > 0.35 kU/L) were included. Sensitization to individual allergen sources and components of birch and timothy pollens was evaluated using multiparameter immunoblots. The presence of IgE to pollen-derived recombinant profilins rAmb a 8.0101, rArt v 4.0101, rBet v 2.0101, and rPhl p 12.0101 in serum was evaluated using ELISA method. The presence of IgE against pollen profilins was detected in 20 out of 100 studied patients. High correlation was seen between IgE ELISA results with individual pollen profilins. In summary, it was shown that the recombinant versions of the four allergenic profilins can be used for sensitization studies and for component-resolved allergy diagnostics. |
format | Online Article Text |
id | pubmed-7024262 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-70242622020-03-11 Production and Use of Recombinant Profilins Amb a 8, Art v 4, Bet v 2, and Phl p 12 for Allergenic Sensitization Studies Cudowska, Beata Kapingidza, A. Brenda Pawłowicz, Magdalena Pampuch, Agnieszka Hyduke, Noah Pote, Swanandi Schlachter, Caleb R. Lebensztejn, Dariusz M. Chruszcz, Maksymilian Kowal, Krzysztof Molecules Article Four recombinant (r) allergens (rAmb a 8.0101, rArt v 4.0101, rBet v 2.0101, and rPhl p 12.0101) were successfully produced and used for sensitization studies. The allergens belong to the profilin family which is one of the most numerous allergen families. These four proteins represent allergens originating from pollen of weeds (rAmb a 8.0101 and rArt v 4.0101), tree (rBet v 2.0101) and grass (rPhl p 12.0101). The recombinant allergens were characterized using various biochemical and biophysical methods and tested for their ability to bind patient-derived antibodies. One hundred patients aged 2 to 50 years sensitized to pollen and plant-derived food allergens (IgE > 0.35 kU/L) were included. Sensitization to individual allergen sources and components of birch and timothy pollens was evaluated using multiparameter immunoblots. The presence of IgE to pollen-derived recombinant profilins rAmb a 8.0101, rArt v 4.0101, rBet v 2.0101, and rPhl p 12.0101 in serum was evaluated using ELISA method. The presence of IgE against pollen profilins was detected in 20 out of 100 studied patients. High correlation was seen between IgE ELISA results with individual pollen profilins. In summary, it was shown that the recombinant versions of the four allergenic profilins can be used for sensitization studies and for component-resolved allergy diagnostics. MDPI 2020-01-16 /pmc/articles/PMC7024262/ /pubmed/31963206 http://dx.doi.org/10.3390/molecules25020369 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Cudowska, Beata Kapingidza, A. Brenda Pawłowicz, Magdalena Pampuch, Agnieszka Hyduke, Noah Pote, Swanandi Schlachter, Caleb R. Lebensztejn, Dariusz M. Chruszcz, Maksymilian Kowal, Krzysztof Production and Use of Recombinant Profilins Amb a 8, Art v 4, Bet v 2, and Phl p 12 for Allergenic Sensitization Studies |
title | Production and Use of Recombinant Profilins Amb a 8, Art v 4, Bet v 2, and Phl p 12 for Allergenic Sensitization Studies |
title_full | Production and Use of Recombinant Profilins Amb a 8, Art v 4, Bet v 2, and Phl p 12 for Allergenic Sensitization Studies |
title_fullStr | Production and Use of Recombinant Profilins Amb a 8, Art v 4, Bet v 2, and Phl p 12 for Allergenic Sensitization Studies |
title_full_unstemmed | Production and Use of Recombinant Profilins Amb a 8, Art v 4, Bet v 2, and Phl p 12 for Allergenic Sensitization Studies |
title_short | Production and Use of Recombinant Profilins Amb a 8, Art v 4, Bet v 2, and Phl p 12 for Allergenic Sensitization Studies |
title_sort | production and use of recombinant profilins amb a 8, art v 4, bet v 2, and phl p 12 for allergenic sensitization studies |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7024262/ https://www.ncbi.nlm.nih.gov/pubmed/31963206 http://dx.doi.org/10.3390/molecules25020369 |
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