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The Core Fucose on an IgG Antibody is an Endogenous Ligand of Dectin‐1
Author(s) -
Manabe Yoshiyuki,
Marchetti Roberta,
Takakura Yohei,
Nagasaki Masahiro,
Nihei Wataru,
Takebe Tomoyuki,
Tanaka Katsunori,
Kabayama Kazuya,
Chiodo Fabrizio,
Hanashima Shinya,
Kamada Yoshihiro,
Miyoshi Eiji,
Dulal Hari Prasad,
Yamaguchi Yoshiki,
Adachi Yoshiyuki,
Ohno Naohito,
Tanaka Hiroshi,
Silipo Alba,
Fukase Koichi,
Molinaro Antonio
Publication year - 2019
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201911875
Subject(s) - fucose , glycosylation , glycan , antibody , lectin , antibody dependent cell mediated cytotoxicity , chemistry , fucosylation , biochemistry , asparagine , glycoprotein , monoclonal antibody , biology , microbiology and biotechnology , amino acid , immunology
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.