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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.
Afiliação
  • Reinmuth-Selzle K; Multiphase Chemistry Department, Max Planck Institute for Chemistry, Mainz, Germany.
  • Bellinghausen I; Department of Dermatology, University Medical Center of the Johannes Gutenberg University, Mainz, Germany.
  • Leifke AL; Multiphase Chemistry Department, Max Planck Institute for Chemistry, Mainz, Germany.
  • Backes AT; Multiphase Chemistry Department, Max Planck Institute for Chemistry, Mainz, Germany.
  • Bothen N; Multiphase Chemistry Department, Max Planck Institute for Chemistry, Mainz, Germany.
  • Ziegler K; Multiphase Chemistry Department, Max Planck Institute for Chemistry, Mainz, Germany.
  • Weller MG; Federal Institute for Materials Research and Testing (BAM), Berlin, Germany.
  • Saloga J; Department of Dermatology, University Medical Center of the Johannes Gutenberg University, Mainz, Germany.
  • Schuppan D; Institute of Translational Immunology, University Medical Center of the Johannes Gutenberg University, Mainz, Germany.
  • Lucas K; Division of Gastroenterology, Beth Israel Deaconess Medical Center, Harvard Medical School, MA, USA.
  • Pöschl U; Multiphase Chemistry Department, Max Planck Institute for Chemistry, Mainz, Germany.
  • Fröhlich-Nowoisky J; Multiphase Chemistry Department, Max Planck Institute for Chemistry, Mainz, Germany.
Front Allergy ; 4: 1066392, 2023.
Article em En | MEDLINE | ID: mdl-36873048
ABSTRACT
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.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Tipo de estudo: Risk_factors_studies Idioma: En Revista: Front Allergy Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Alemanha

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Tipo de estudo: Risk_factors_studies Idioma: En Revista: Front Allergy Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Alemanha