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Chemical modification by peroxynitrite enhances TLR4 activation of the grass pollen allergen Phl p 5
The chemical modification of aeroallergens by reactive oxygen and nitrogen species (ROS/RNS) may contribute to the growing prevalence of respiratory allergies in industrialized countries. Post-translational modifications can alter the immunological properties of proteins, but the underlying mechanis...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9975604/ https://www.ncbi.nlm.nih.gov/pubmed/36873048 http://dx.doi.org/10.3389/falgy.2023.1066392 |
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author | Reinmuth-Selzle, Kathrin Bellinghausen, Iris Leifke, Anna Lena Backes, Anna T. Bothen, Nadine Ziegler, Kira Weller, Michael G. Saloga, Joachim Schuppan, Detlef Lucas, Kurt Pöschl, Ulrich Fröhlich-Nowoisky, Janine |
author_facet | Reinmuth-Selzle, Kathrin Bellinghausen, Iris Leifke, Anna Lena Backes, Anna T. Bothen, Nadine Ziegler, Kira Weller, Michael G. Saloga, Joachim Schuppan, Detlef Lucas, Kurt Pöschl, Ulrich Fröhlich-Nowoisky, Janine |
author_sort | Reinmuth-Selzle, Kathrin |
collection | PubMed |
description | The chemical modification of aeroallergens by reactive oxygen and nitrogen species (ROS/RNS) may contribute to the growing prevalence of respiratory allergies in industrialized countries. Post-translational modifications can alter the immunological properties of proteins, but the underlying mechanisms and effects are not well understood. In this study, we investigate the Toll-like receptor 4 (TLR4) activation of the major birch and grass pollen allergens Bet v 1 and Phl p 5, and how the physiological oxidant peroxynitrite (ONOO(–)) changes the TLR4 activation through protein nitration and the formation of protein dimers and higher oligomers. Of the two allergens, Bet v 1 exhibited no TLR4 activation, but we found TLR4 activation of Phl p 5, which increased after modification with ONOO(–) and may play a role in the sensitization against this grass pollen allergen. We attribute the TLR4 activation mainly to the two-domain structure of Phl p 5 which may promote TLR4 dimerization and activation. The enhanced TLR4 signaling of the modified allergen indicates that the ONOO(–)-induced modifications affect relevant protein-receptor interactions. This may lead to increased sensitization to the grass pollen allergen and thus contribute to the increasing prevalence of allergies in the Anthropocene, the present era of globally pervasive anthropogenic influence on the environment. |
format | Online Article Text |
id | pubmed-9975604 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-99756042023-03-02 Chemical modification by peroxynitrite enhances TLR4 activation of the grass pollen allergen Phl p 5 Reinmuth-Selzle, Kathrin Bellinghausen, Iris Leifke, Anna Lena Backes, Anna T. Bothen, Nadine Ziegler, Kira Weller, Michael G. Saloga, Joachim Schuppan, Detlef Lucas, Kurt Pöschl, Ulrich Fröhlich-Nowoisky, Janine Front Allergy Allergy The chemical modification of aeroallergens by reactive oxygen and nitrogen species (ROS/RNS) may contribute to the growing prevalence of respiratory allergies in industrialized countries. Post-translational modifications can alter the immunological properties of proteins, but the underlying mechanisms and effects are not well understood. In this study, we investigate the Toll-like receptor 4 (TLR4) activation of the major birch and grass pollen allergens Bet v 1 and Phl p 5, and how the physiological oxidant peroxynitrite (ONOO(–)) changes the TLR4 activation through protein nitration and the formation of protein dimers and higher oligomers. Of the two allergens, Bet v 1 exhibited no TLR4 activation, but we found TLR4 activation of Phl p 5, which increased after modification with ONOO(–) and may play a role in the sensitization against this grass pollen allergen. We attribute the TLR4 activation mainly to the two-domain structure of Phl p 5 which may promote TLR4 dimerization and activation. The enhanced TLR4 signaling of the modified allergen indicates that the ONOO(–)-induced modifications affect relevant protein-receptor interactions. This may lead to increased sensitization to the grass pollen allergen and thus contribute to the increasing prevalence of allergies in the Anthropocene, the present era of globally pervasive anthropogenic influence on the environment. Frontiers Media S.A. 2023-02-15 /pmc/articles/PMC9975604/ /pubmed/36873048 http://dx.doi.org/10.3389/falgy.2023.1066392 Text en © 2023 Reinmuth-Selzle, Bellinghausen, Leifke, Backes, Bothen, Ziegler, Weller, Saloga, Schuppan, Lucas, Pöschl and Fröhlich-Nowoisky. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY) (https://creativecommons.org/licenses/by/4.0/) . The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Allergy Reinmuth-Selzle, Kathrin Bellinghausen, Iris Leifke, Anna Lena Backes, Anna T. Bothen, Nadine Ziegler, Kira Weller, Michael G. Saloga, Joachim Schuppan, Detlef Lucas, Kurt Pöschl, Ulrich Fröhlich-Nowoisky, Janine Chemical modification by peroxynitrite enhances TLR4 activation of the grass pollen allergen Phl p 5 |
title | Chemical modification by peroxynitrite enhances TLR4 activation of the grass pollen allergen Phl p 5 |
title_full | Chemical modification by peroxynitrite enhances TLR4 activation of the grass pollen allergen Phl p 5 |
title_fullStr | Chemical modification by peroxynitrite enhances TLR4 activation of the grass pollen allergen Phl p 5 |
title_full_unstemmed | Chemical modification by peroxynitrite enhances TLR4 activation of the grass pollen allergen Phl p 5 |
title_short | Chemical modification by peroxynitrite enhances TLR4 activation of the grass pollen allergen Phl p 5 |
title_sort | chemical modification by peroxynitrite enhances tlr4 activation of the grass pollen allergen phl p 5 |
topic | Allergy |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9975604/ https://www.ncbi.nlm.nih.gov/pubmed/36873048 http://dx.doi.org/10.3389/falgy.2023.1066392 |
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