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Soh, W.T.* ; Aglas, L.* ; Mueller, G.A.* ; Gilles, S. ; Weiss, R.* ; Scheiblhofer, S.* ; Huber, S.* ; Scheidt, T.* ; Thompson, P.M.* ; Briza, P.* ; London, R.E.* ; Traidl-Hoffmann, C. ; Cabrele, C.* ; Brandstetter, H.* ; Ferreira, F.*

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

Allergy 74, 2382–2393 (2019)

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

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Publication type Article: Journal article

Document type Scientific Article

Corresponding Author

Keywords Allergenicity ; Birch Pollen Extract ; E Phytoprostanes 1 ; Ligand Interaction ; Lysosomal Protease Inhibition; Pollen Extracts; Proteins; Receptor; Activation; Phytoprostanes; Identification; Sensitization; Legumain; Bet-v-1; Sites

ISSN (print) / ISBN 0105-4538

e-ISSN 1398-9995

Journal Allergy

Quellenangaben Volume: 74, Issue: 12, Pages: 2382–2393

Publisher Wiley

Publishing Place 111 River St, Hoboken 07030-5774, Nj Usa

Non-patent literature Publications

Reviewing status Peer reviewed

Institute(s) Institute of Environmental Medicine (IEM)