The human and mouse dendritic cell receptor DCIR binds to LRP1 N-glycans containing terminal galactoses, including the α-Gal antigen
Raymond, B. B. A.; Sneperger, T.; Rousset, S.; Gilles, N.; Bally, A.; Stella, A.; Hipgrave Ederveen, A. L.; Marcoux, J.; Trimaglio, G.; Thepaut, M.; Lagarrigue, F.; Burlet-Schiltz, O.; Wuhrer, M.; Fieschi, F.; Demange, P.; Neyrolles, O.; Rombouts, Y.
Show abstract
The dendritic cell immunoreceptor (DCIR) is a C-type lectin receptor expressed by myeloid cells that plays a key immunoregulatory role in a wide range of diseases, from inflammation to cancer. However, the ligand(s) of DCIR remain(s) unknown, hampering our understanding of the exact function of this immune receptor. Here, we found that both human DCIR and mouse DCIR1 bind specifically to the low-density lipoprotein receptor-related protein 1 (LRP1), a heavily glycosylated receptor mediating the clearance of various molecules from the extracellular matrix and apoptotic cells. This interaction is mediated by galactose-terminated biantennary complex-type N-glycans, including those carrying the immunogenic -Gal epitope. Our study provides a deeper understanding of the role of DCIR in immune regulation and its potential impact on a range of immune disorders, highlighting its specificity in ligand recognition which is crucial for developing therapeutic strategies.
Matching journals
The top 5 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- Mapping the SARS-CoV-2 spike glycoprotein-derived peptidome presented by HLA class II on dendritic cells 94%
- Epistasis in the receptor binding domain of contemporary H3N2 viruses that reverted to bind sialylated diLacNAc repeats 94%
- Mechanism and evolutionary origins of Alanine-tail C-degron recognition by E3 ligases Pirh2 and CRL2-KLHDC10 94%
Similar papers in this journal
- Human Dectin-1 is O-glycosylated and serves as a ligand for C-type lectin receptor CLEC-2 96%
- Identification of orphan ligand-receptor relationships using a cell-based CRISPRa enrichment screening platform. 94%
- Structure-guided glyco-engineering of ACE2 for improved potency as soluble SARS-CoV-2 decoy receptor 94%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.