Oligomerization and tyrosine nitration enhance the allergenic potential of the birch and grass pollen allergens Bet v 1 and Phl p 5.
| Autor: | Fröhlich-Nowoisky J; Multiphase Chemistry Department, Max Planck Institute for Chemistry, Mainz, Germany., Bothen N; Multiphase Chemistry Department, Max Planck Institute for Chemistry, Mainz, Germany., Backes AT; Multiphase Chemistry Department, Max Planck Institute for Chemistry, Mainz, Germany., Weller MG; Division 1.5 - Protein Analysis, Federal Institute for Materials Research and Testing (BAM), Berlin, Germany., Pöschl U; Multiphase Chemistry Department, Max Planck Institute for Chemistry, Mainz, Germany. |
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| Jazyk: | angličtina |
| Zdroj: | Frontiers in allergy [Front Allergy] 2023 Dec 05; Vol. 4, pp. 1303943. Date of Electronic Publication: 2023 Dec 05 (Print Publication: 2023). |
| DOI: | 10.3389/falgy.2023.1303943 |
| Abstrakt: | Protein modifications such as oligomerization and tyrosine nitration alter the immune response to allergens and may contribute to the increasing prevalence of allergic diseases. In this mini-review, we summarize and discuss relevant findings for the major birch and grass pollen allergens Bet v 1 and Phl p 5 modified with tetranitromethane (laboratory studies), peroxynitrite (physiological processes), and ozone and nitrogen dioxide (environmental conditions). We focus on tyrosine nitration and the formation of protein dimers and higher oligomers via dityrosine cross-linking and the immunological effects studied. Competing Interests: The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest. (© 2023 Fröhlich-Nowoisky, Bothen, Backes, Weller and Pöschl.) |
| Databáze: | MEDLINE |
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