Multiple roles of Bet v 1 ligands in allergen stabilization and modulation of endosomal protease activity

• DOI: 10.1111/all.13948
• Publication Date: 2019-06-23T00:49:37Z
• Authors: Wai Tuck Soh; Lorenz Aglas; Geoffrey A. Mueller; Stefanie Gilles; Richard Weiss; Sandra Scheiblhofer; Sara Huber; Tamara Scheidt; Peter M. Thompson; Peter Briza; Robert E. London; Claudia Traidl‐Ho...; Chiara Cabrele; Hans Brandstetter; Fatima Ferreira
• Keywords: Cysteine protease; Cathepsin S

Over 100 million people worldwide suffer from birch pollen allergy. Bet v 1 has been identified as the major allergen. However, molecular mechanisms of allergic sensitization, including roles and other components extract, remain incompletely understood. Here, we examined how known pollen-derived molecules influence endolysosomal processing 1, thereby shaping its allergenicity.We analyzed biochemical immunological interaction ligands with 1. We then investigated proteolytic by endosomal extracts in presence absence ligands, followed a detailed kinetic analysis individual proteases well T-cell epitope presentation BMDCs.We E1 phytoprostanes novel ligands. Pollen-derived enhanced resistance affecting degradation kinetics preferential cleavage sites cathepsin S legumain. exhibited dual role stabilizing inhibiting protease activity.Bet can serve transporter pollen-derived, bioactive compounds. When carried to endolysosome, such compounds modulate activity, cysteine cathepsins. unveil paradigm shift an allergen-centered view more systemic that includes host enzymes.