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NMR resonance assignments of a hypoallergenic isoform of the major birch pollen allergen Bet v 1
In Northern America and Europe a great number of people are suffering from birch pollen allergy and pollen related food allergies. The trigger for these immunological reactions is the 17.5 kDa major birch pollen allergen Bet v 1, which belongs to the family of PR-10 (pathogenesis-related) proteins....
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Netherlands
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5594047/ https://www.ncbi.nlm.nih.gov/pubmed/28808910 http://dx.doi.org/10.1007/s12104-017-9754-7 |
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author | Ahammer, Linda Grutsch, Sarina Wallner, Michael Ferreira, Fatima Tollinger, Martin |
author_facet | Ahammer, Linda Grutsch, Sarina Wallner, Michael Ferreira, Fatima Tollinger, Martin |
author_sort | Ahammer, Linda |
collection | PubMed |
description | In Northern America and Europe a great number of people are suffering from birch pollen allergy and pollen related food allergies. The trigger for these immunological reactions is the 17.5 kDa major birch pollen allergen Bet v 1, which belongs to the family of PR-10 (pathogenesis-related) proteins. In nature, Bet v 1 occurs as a mixture of various isoforms that possess different immunological properties despite their high sequence identities. Bet v 1.0102 (Bet v 1d), which is investigated here, is a hypoallergenic isoform of Bet v 1 and a potential candidate for allergen-specific immunotherapy. We assigned the backbone and side chain (1)H, (13)C and (15)N resonances of this protein and predicted its secondary structure. The NMR-chemical shift data indicate that Bet v 1.0102 is composed of three α-helices and a seven stranded β-sheet, in agreement with the known structure of the hyperallergenic isoform Bet v 1.0101 (Bet v 1a). Our resonance assignments create the foundation for detailed characterization of the dynamic properties of Bet v 1 isoforms by NMR relaxation measurements. |
format | Online Article Text |
id | pubmed-5594047 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Springer Netherlands |
record_format | MEDLINE/PubMed |
spelling | pubmed-55940472017-09-26 NMR resonance assignments of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 Ahammer, Linda Grutsch, Sarina Wallner, Michael Ferreira, Fatima Tollinger, Martin Biomol NMR Assign Article In Northern America and Europe a great number of people are suffering from birch pollen allergy and pollen related food allergies. The trigger for these immunological reactions is the 17.5 kDa major birch pollen allergen Bet v 1, which belongs to the family of PR-10 (pathogenesis-related) proteins. In nature, Bet v 1 occurs as a mixture of various isoforms that possess different immunological properties despite their high sequence identities. Bet v 1.0102 (Bet v 1d), which is investigated here, is a hypoallergenic isoform of Bet v 1 and a potential candidate for allergen-specific immunotherapy. We assigned the backbone and side chain (1)H, (13)C and (15)N resonances of this protein and predicted its secondary structure. The NMR-chemical shift data indicate that Bet v 1.0102 is composed of three α-helices and a seven stranded β-sheet, in agreement with the known structure of the hyperallergenic isoform Bet v 1.0101 (Bet v 1a). Our resonance assignments create the foundation for detailed characterization of the dynamic properties of Bet v 1 isoforms by NMR relaxation measurements. Springer Netherlands 2017-08-14 2017 /pmc/articles/PMC5594047/ /pubmed/28808910 http://dx.doi.org/10.1007/s12104-017-9754-7 Text en © The Author(s) 2017 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Article Ahammer, Linda Grutsch, Sarina Wallner, Michael Ferreira, Fatima Tollinger, Martin NMR resonance assignments of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 |
title | NMR resonance assignments of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 |
title_full | NMR resonance assignments of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 |
title_fullStr | NMR resonance assignments of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 |
title_full_unstemmed | NMR resonance assignments of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 |
title_short | NMR resonance assignments of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 |
title_sort | nmr resonance assignments of a hypoallergenic isoform of the major birch pollen allergen bet v 1 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5594047/ https://www.ncbi.nlm.nih.gov/pubmed/28808910 http://dx.doi.org/10.1007/s12104-017-9754-7 |
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