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Updated: Jun 24, 2026

Development and Functional Characterization of Murine Tolerogenic Dendritic Cells
Published on: May 18, 2018
Ly49Q ligand expressed by activated B cells induces plasmacytoid DC maturation
Makiko Toma-Hirano1, Sahori Namiki, Yasue Shibata
1Department of Otolaryngology - Head and Neck Surgery, Graduate School of Medicine, University of Tokyo, Tokyo, Japan.
Insights
Mouse plasmacytoid dendritic cells (pDCs) use Ly49Q to recognize clustered H-2K(b) on activated B cells. This interaction promotes pDC maturation, highlighting a novel immune signaling pathway.
Area of Science:
- Immunology
- Cellular Biology
- Molecular Interactions
Background:
- Ly49Q is a type II C-type lectin on mouse plasmacytoid dendritic cells (pDCs).
- It possesses a carbohydrate recognition domain and an ITIM motif.
- MHC class I molecule H-2K(b) is a known ligand for Ly49Q.
Purpose of the Study:
- To investigate the interaction between Ly49Q and its ligand H-2K(b) on B cells.
- To determine the role of H-2K(b) clustering in Ly49Q activation.
- To elucidate the impact of this interaction on pDC maturation.
Main Methods:
- Identification of H-2K(b) as a Ly49Q ligand.
- Analysis of H-2K(b) expression and clustering on resting and CpG-stimulated B cells.
- Assessment of co-stimulatory molecule upregulation on pDCs.
- In vitro pDC maturation assays upon anti-Ly49Q antibody binding.
Main Results:
- H-2K(b) is expressed on most hematopoietic cells but activates Ly49Q only on CpG-stimulated B cells.
- Clustered H-2K(b) on activated B cells, not diffusely expressed H-2K(b) on resting B cells, correlates with Ly49Q activation.
- CpG-stimulated B cells upregulate co-stimulatory molecules on pDCs.
- Binding of anti-Ly49Q mAb induces pDC maturation in vitro.
Conclusions:
- Clustered H-2K(b) on activated B cells serves as a ligand for Ly49Q.
- This interaction induces plasmacytoid dendritic cell maturation.
- Suggests a mechanism for B cell-mediated pDC activation and immune response modulation.
Abstract:
Ly49Q, a type II C-type lectin expressed on mouse plasmacytoid DC (pDC), contains a single carbohydrate recognition domain in its extracellular region and an ITIM in its cytoplasmic domain. We have identified the MHC class I molecule H-2K(b) as a Ly49Q ligand, confirming prior reports. Although H-2K(b) is expressed on essentially all hematopoietic cells, we found that only CpG-stimulated B cells were able to activate Ly49Q. This discovery correlated with our finding that although H-2K(b) forms clusters on CpG-activated B cells, it is diffusely expressed on resting B cells. Furthermore, CpG-stimulated, but not resting, B cells up-regulated co-stimulatory molecules on pDC. This finding was confirmed by the fact that binding by anti-Ly49Q mAb to Ly49Q led to pDC maturation in vitro. Our results suggest that clustered H-2K(b) on activated B cells act as ligands for Ly49Q and induce pDC maturation in vitro.
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