Covalent polyphenol modification of a reactive cysteine in the major apple allergen Mal d 1

Jana Unterhauser,Linda Ahammer,Tobias Rainer,Reiner Eidelpes, Sebastian Führer,Bettina Nothegger,Claudia E Covaciu,Valentina Cova,Anna S Kamenik,Klaus R Liedl,Thomas Müller,Kathrin Breuker,Klaus Eisendle,Norbert Reider,Thomas Letschka,Martin Tollinger

Food Chemistry（2023）

引用 5|浏览12

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摘要

•Mal d 1 is prone to spontaneous covalent modification by polyphenols.•A surface-exposed cysteine residue in Mal d 1 is the primary modification site.•Covalent modification does not perturb or unfold the three-dimensional structure.•An immunorelevant binding epitope on the allergen surface is masked.

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关键词

CSP,ELISA,ESI,FT-ICR,IgE,MTSL,PPO,PRE,PR-10

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