Oligomerization and tyrosine nitration enhance the allergenic potential of the birch and grass pollen allergens Bet v 1 and Phl p 5

Janine Fröhlich-Nowoisky; Nadine Bothen; Anna T Backes; Michael G Weller; Ulrich Pöschl

doi:10.3389/falgy.2023.1303943

Oligomerization and tyrosine nitration enhance the allergenic potential of the birch and grass pollen allergens Bet v 1 and Phl p 5

Front Allergy. 2023 Dec 5:4:1303943. doi: 10.3389/falgy.2023.1303943. eCollection 2023.

Authors

Janine Fröhlich-Nowoisky¹, Nadine Bothen¹, Anna T Backes¹, Michael G Weller², Ulrich Pöschl¹

Affiliations

¹ Multiphase Chemistry Department, Max Planck Institute for Chemistry, Mainz, Germany.
² Division 1.5 - Protein Analysis, Federal Institute for Materials Research and Testing (BAM), Berlin, Germany.

Abstract

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.

Keywords: Bet v 1; Phl p 5; air pollution; allergy; dimers; nitration; oligomers; peroxynitrite.

Publication types

Review

Grants and funding

The author(s) declare financial support was received for the research, authorship, and/or publication of this article.