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Int. J. Mol. Sci. 2017, 18(6), 1225; doi:10.3390/ijms18061225

Comparing Proteolytic Fingerprints of Antigen-Presenting Cells during Allergen Processing

Department of Molecular Biology, University of Salzburg, Salzburg 5020, Austria
Biomay AG, Vienna 1090, Austria
Department of Medicine, Faculty of Medicine, Chulalongkorn University, Bangkok 10330, Thailand
These authors contributed equally to this work.
Author to whom correspondence should be addressed.
Academic Editor: Denis Girard
Received: 27 April 2017 / Revised: 23 May 2017 / Accepted: 31 May 2017 / Published: 8 June 2017
(This article belongs to the Special Issue Proteolysis in Allergic Sensitization and Th2 Response)
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Endolysosomal processing has a critical influence on immunogenicity as well as immune polarization of protein antigens. In industrialized countries, allergies affect around 25% of the population. For the rational design of protein-based allergy therapeutics for immunotherapy, a good knowledge of T cell-reactive regions on allergens is required. Thus, we sought to analyze endolysosomal degradation patterns of inhalant allergens. Four major allergens from ragweed, birch, as well as house dust mites were produced as recombinant proteins. Endolysosomal proteases were purified by differential centrifugation from dendritic cells, macrophages, and B cells, and combined with allergens for proteolytic processing. Thereafter, endolysosomal proteolysis was monitored by protein gel electrophoresis and mass spectrometry. We found that the overall proteolytic activity of specific endolysosomal fractions differed substantially, whereas the degradation patterns of the four model allergens obtained with the different proteases were extremely similar. Moreover, previously identified T cell epitopes were assigned to endolysosomal peptides and indeed showed a good overlap with known T cell epitopes for all four candidate allergens. Thus, we propose that the degradome assay can be used as a predictor to determine antigenic peptides as potential T cell epitopes, which will help in the rational design of protein-based allergy vaccine candidates. View Full-Text
Keywords: allergen proteolysis; Bet v 1; Amb a 1; Der p 1; Der p 2; proteases from dendritic cells; proteases from macrophages; proteases from B cells; degradome assay allergen proteolysis; Bet v 1; Amb a 1; Der p 1; Der p 2; proteases from dendritic cells; proteases from macrophages; proteases from B cells; degradome assay

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Hofer, H.; Weidinger, T.; Briza, P.; Asam, C.; Wolf, M.; Twaroch, T.E.; Stolz, F.; Neubauer, A.; Dall, E.; Hammerl, P.; Jacquet, A.; Wallner, M. Comparing Proteolytic Fingerprints of Antigen-Presenting Cells during Allergen Processing. Int. J. Mol. Sci. 2017, 18, 1225.

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