C-Type Lectin Receptor Dectin-2 Binds to an Endogenous Protein β-Glucuronidase on Dendritic Cells

• Published in: PloS one 2017-01, Vol.12 (1), p.e0169562-e0169562
• Main Authors: Mori, Daiki, Shibata, Kensuke, Yamasaki, Sho
• Format: Article
• Language: English
• Subjects: Animals; Binding; Biology and Life Sciences; Bone marrow; Bone Marrow Cells - metabolism; Cloning; CRISPR; Dendritic cells; Dendritic Cells - immunology; Dendritic Cells - metabolism; Flow Cytometry; Genotype; Glucuronidase - metabolism; Glycosylation; HEK293 Cells; Heparan sulfate; Humans; Immune response; Immunology; Lectins; Lectins, C-Type - metabolism; Ligands; Macrophages; Macrophages - metabolism; Mannose; Mannose - chemistry; Medicine and Health Sciences; Mice; Mice, Inbred C57BL; Mice, Transgenic; Mutation; Phosphorylation; Physical Sciences; Plasmids - metabolism; Protein Binding; Protein Domains; Protein structure; Proteins; Receptors
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0169562

C-type lectin receptors (CLRs) recognize pathogen-derived ligands and abnormal self that trigger protective immune responses. However, the precise nature of self ligands recognized by CLRs remains to be determined. Here, we found that Dectin-2 recognizes bone marrow-derived dendritic cells (BMDCs) using Dectin-2-expressing reporter cells. This activity was inhibited by an excessive amount of mannose, and by the mutation of mannose-binding motif in Dectin-2. β-glucuronidase (Gusb) was identified as a protein bound to Dectin-2 and mutations of N-glycosylation sites in Gusb impaired the binding of Gusb to Dectin-2. Overexpression of Gusb in a macrophage cell line conferred an ability to stimulate Dectin-2-expressing reporter cells. Our study suggests that a glycosylated protein with mannose-related structure is recognized by Dectin-2.