TY - JOUR
T1 - C-type lectin receptor Dectin-2 binds to an endogenous protein β-glucuronidase on dendritic cells
AU - Mori, Daiki
AU - Shibata, Kensuke
AU - Yamasaki, Sho
N1 - Funding Information:
We thank M. Tanaka for DNA injection; M. Oda for Mass spectrometry; Y. Matsuzaki for DNA sequencing; M. Tanaka and M. Kurata for embryo engineering; Laboratory for technical support for technical supports. 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.
Publisher Copyright:
© 2017 Mori et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
PY - 2017/1
Y1 - 2017/1
N2 - 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.
AB - 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.
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U2 - 10.1371/journal.pone.0169562
DO - 10.1371/journal.pone.0169562
M3 - Article
C2 - 28046067
AN - SCOPUS:85008213286
SN - 1932-6203
VL - 12
JO - PloS one
JF - PloS one
IS - 1
M1 - e0169562
ER -