Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 58, Issue 51, Pages 18697-18702Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201911875
Keywords
fucose; Dectin-1; IgG; molecular recognition; N-glycan
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Funding
- JSPS KAKENHI [15H05836, 16H01885, 15H04810, 16H05924]
- Progetto POR SATIN
- Progetto POR Campania Oncoterapia
- PRIN-MIUR 2017 Glytunes project
- COST Action INNOGLY [CA18103]
- European Commission [H2020-MSCA- 814102- SWEET CROSSTALK]
- 2018 Amsterdam Infection and Immunity Institute Fellowship
- JSPS Bilateral Open Partnership Joint Research Projects
- Osaka University's International Joint Research Promotion Program
- Grants-in-Aid for Scientific Research [15H04810] Funding Source: KAKEN
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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-beta-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.
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