| First Author | Haji S | Year | 2022 |
| Journal | Elife | Volume | 11 |
| PubMed ID | 36479973 | Mgi Jnum | J:332219 |
| Mgi Id | MGI:7412465 | Doi | 10.7554/eLife.83037 |
| Citation | Haji S, et al. (2022) Human Dectin-1 is O-glycosylated and serves as a ligand for C-type lectin receptor CLEC-2. Elife 11 |
| abstractText | C-type lectin receptors (CLRs) elicit immune responses upon recognition of glycoconjugates present on pathogens and self-components. While Dectin-1 is the best-characterized CLR recognizing beta-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 platelets. 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 Podoplanin, 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. |
