Abstract
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.
MeSH terms
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Animals
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Bone Marrow Cells / metabolism
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Dendritic Cells / immunology
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Dendritic Cells / metabolism*
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Flow Cytometry
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Genotype
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Glucuronidase / metabolism*
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Glycosylation
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HEK293 Cells
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Humans
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Lectins, C-Type / metabolism*
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Ligands
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Macrophages / metabolism
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Mannose / chemistry
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Mice
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Mice, Inbred C57BL
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Mice, Transgenic
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Mutation
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Plasmids / metabolism
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Protein Binding
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Protein Domains
Substances
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Lectins, C-Type
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Ligands
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dectin-2, mouse
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Glucuronidase
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Mannose
Grants and funding
This work was supported by Grant-in-Aid for Scientific Research (26293099), Grant-in-Aid for Scientific Research on Innovative Areas (26110009) from MEXT, Grants from the Ministry of Health, Labour and Welfare (MHLW), the Research on Development of New Drugs and AMED-CREST, AMED. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.