Structural basis for cross-reactivity and conformation fluctuation of the major beech pollen allergen Fag s 1

Fag s 1 is a member of the Pathogen Related protein family 10 (PR-10) and can elicit cross-reaction with IgE antibodies produced against the birch pollen allergen Bet v 1. The Nuclear Magnetic Resonance (NMR) structure of Fag s 1 is presented along with its dynamic properties. It shares 66% identity...

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Autores principales: Moraes, Adolfo H., Asam, Claudia, Almeida, Fabio C. L., Wallner, Michael, Ferreira, Fatima, Valente, Ana Paula
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2018
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6043577/
https://www.ncbi.nlm.nih.gov/pubmed/30002383
http://dx.doi.org/10.1038/s41598-018-28358-1
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author Moraes, Adolfo H.
Asam, Claudia
Almeida, Fabio C. L.
Wallner, Michael
Ferreira, Fatima
Valente, Ana Paula
author_facet Moraes, Adolfo H.
Asam, Claudia
Almeida, Fabio C. L.
Wallner, Michael
Ferreira, Fatima
Valente, Ana Paula
author_sort Moraes, Adolfo H.
collection PubMed
description Fag s 1 is a member of the Pathogen Related protein family 10 (PR-10) and can elicit cross-reaction with IgE antibodies produced against the birch pollen allergen Bet v 1. The Nuclear Magnetic Resonance (NMR) structure of Fag s 1 is presented along with its dynamic properties. It shares 66% identity with Bet v 1 and exhibits the expected three α-helices and seven β-sheets arranged as a semi-beta barrel and exposing the residues mapped as the Bet v 1 IgE epitope. The structural dynamics of Fag s 1 were monitored on the fast and intermediate timescales, using relaxation rates. The complex dynamics of Fag s 1 are closely related to the internal cavity, and they modulate IgE and ligand binding.
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spelling pubmed-60435772018-07-15 Structural basis for cross-reactivity and conformation fluctuation of the major beech pollen allergen Fag s 1 Moraes, Adolfo H. Asam, Claudia Almeida, Fabio C. L. Wallner, Michael Ferreira, Fatima Valente, Ana Paula Sci Rep Article Fag s 1 is a member of the Pathogen Related protein family 10 (PR-10) and can elicit cross-reaction with IgE antibodies produced against the birch pollen allergen Bet v 1. The Nuclear Magnetic Resonance (NMR) structure of Fag s 1 is presented along with its dynamic properties. It shares 66% identity with Bet v 1 and exhibits the expected three α-helices and seven β-sheets arranged as a semi-beta barrel and exposing the residues mapped as the Bet v 1 IgE epitope. The structural dynamics of Fag s 1 were monitored on the fast and intermediate timescales, using relaxation rates. The complex dynamics of Fag s 1 are closely related to the internal cavity, and they modulate IgE and ligand binding. Nature Publishing Group UK 2018-07-12 /pmc/articles/PMC6043577/ /pubmed/30002383 http://dx.doi.org/10.1038/s41598-018-28358-1 Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as 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. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Moraes, Adolfo H.
Asam, Claudia
Almeida, Fabio C. L.
Wallner, Michael
Ferreira, Fatima
Valente, Ana Paula
Structural basis for cross-reactivity and conformation fluctuation of the major beech pollen allergen Fag s 1
title Structural basis for cross-reactivity and conformation fluctuation of the major beech pollen allergen Fag s 1
title_full Structural basis for cross-reactivity and conformation fluctuation of the major beech pollen allergen Fag s 1
title_fullStr Structural basis for cross-reactivity and conformation fluctuation of the major beech pollen allergen Fag s 1
title_full_unstemmed Structural basis for cross-reactivity and conformation fluctuation of the major beech pollen allergen Fag s 1
title_short Structural basis for cross-reactivity and conformation fluctuation of the major beech pollen allergen Fag s 1
title_sort structural basis for cross-reactivity and conformation fluctuation of the major beech pollen allergen fag s 1
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6043577/
https://www.ncbi.nlm.nih.gov/pubmed/30002383
http://dx.doi.org/10.1038/s41598-018-28358-1
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