Mori Daiki, Shibata Kensuke, Yamasaki Sho
Division of Molecular Immunology, Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan.
Department of Molecular Immunology, Medical Mycology Research Center, Chiba University, Chiba, Japan.
PLoS One. 2017 Jan 3;12(1):e0169562. doi: 10.1371/journal.pone.0169562. eCollection 2017.
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.
C型凝集素受体（CLRs）识别病原体衍生的配体和触发保护性免疫反应的异常自身物质。然而，CLRs识别的自身配体的确切性质仍有待确定。在这里，我们发现，使用表达Dectin-2的报告细胞，Dectin-2可识别骨髓来源的树突状细胞（BMDCs）。这种活性受到过量甘露糖以及Dectin-2中甘露糖结合基序突变的抑制。β-葡萄糖醛酸酶（Gusb）被鉴定为与Dectin-2结合的一种蛋白质，Gusb中N-糖基化位点的突变会损害Gusb与Dectin-2的结合。在巨噬细胞系中过表达Gusb赋予了刺激表达Dectin-2的报告细胞的能力。我们的研究表明，具有甘露糖相关结构的糖基化蛋白可被Dectin-2识别。
