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The Core Fucose on an IgG Antibody is an Endogenous Ligand of Dectin-1.

Yoshiyuki ManabeRoberta MarchettiYohei TakakuraMasahiro NagasakiWataru NiheiTomoyuki TakebeKatsunori TanakaKazuya KabayamaFabrizio ChiodoShinya HanashimaYoshihiro KamadaEiji MiyoshiHari Prasad DulalYoshiki YamaguchiYoshiyuki AdachiNaohito OhnoHiroshi TanakaAlba SilipoKoichi FukaseAntonio Molinaro
Published in: Angewandte Chemie (International ed. in English) (2019)
The core fucose, a major modification of N-glycans, is implicated in immune regulation, such as the attenuation of the antibody-dependent cell-mediated cytotoxicity of antibody drugs and the inhibition of anti-tumor responses via the promotion of PD-1 expression on T cells. Although the core fucose regulates many biological processes, no core fucose recognition molecule has been identified in mammals. Herein, we report that Dectin-1, a known anti-β-glucan lectin, recognizes the core fucose on IgG antibodies. A combination of biophysical experiments further suggested that Dectin-1 recognizes aromatic amino acids adjacent to the N-terminal asparagine at the glycosylation site as well as the core fucose. Thus, Dectin-1 appears to be the first lectin-like molecule involved in the heterovalent and specific recognition of characteristic N-glycans on antibodies.
Keyphrases
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