Human Dectin-1 is O-glycosylated and serves as a ligand for C-type lectin receptor CLEC-2

Shojiro Haji, Taiki Ito, Carla Guenther, Miyako Nakano, Takashi Shimizu, Daiki Mori, Yasunori Chiba, Masato Tanaka, Sushil K. Mishra, Janet A. Willment, Gordon D. Brown, Masamichi Nagae, Sho Yamasaki

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)


C-type lectin receptors (CLRs) elicit immune responses upon recognition of glycocon-jugates present on pathogens and self-components. While Dectin-1 is the best-characterized CLR recognizing β-glucan on pathogens, the endogenous targets of Dectin-1 are not fully understood. Herein, we report that human Dectin-1 is a ligand for CLEC-2, another CLR expressed on plate-lets. Biochemical analyses revealed that Dectin-1 is a mucin-like protein as its stalk region is highly O-glycosylated. A sialylated core 1 glycan attached to the EDxxT motif of human Dectin-1, which is absent in mouse Dectin-1, provides a ligand moiety for CLEC-2. Strikingly, the expression of human Dectin-1 in mice rescued the lethality and lymphatic defect resulting from a deficiency of Podo-planin, a known CLEC-2 ligand. This finding is the first example of an innate immune receptor also functioning as a physiological ligand to regulate ontogeny upon glycosylation.

Original languageEnglish
Article numbere83037
Publication statusPublished - Dec 2022
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General Neuroscience
  • General Biochemistry,Genetics and Molecular Biology
  • General Immunology and Microbiology


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