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

研究成果: ジャーナルへの寄稿学術誌査読

7 被引用数 (Scopus)

抄録

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.

本文言語英語
論文番号e83037
ジャーナルeLife
11
DOI
出版ステータス出版済み - 12月 2022
外部発表はい

!!!All Science Journal Classification (ASJC) codes

  • 神経科学一般
  • 生化学、遺伝学、分子生物学一般
  • 免疫学および微生物学一般

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