Immune Recognition of Pathogen-Derived Glycolipids Through Mincle
Immune Recognition of Pathogen-Derived Glycolipids Through Mincle
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DOI:
10.1007/978-981-15-1580-4_2
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发表时间:
2020-01-01
期刊:
影响因子:
--
通讯作者:
Yamasaki,Sho
中科院分区:
文献类型:
--
作者:
Miyake,Yasunobu;Yamasaki,Sho
Mincle (macrophageinducibleC-typelectin, Clec4e, Clecsf9) was originally identified as a member of the C-type lectin receptor family in 1999. Then, the function of Mincle to control antifungal immunity by binding toCandida albicanswas reported in 2008. Around the same time, it was reported that Mincle recognized damaged cells and induced sterile inflammation by coupling with the ITAM-adaptor molecule FcRγ. In the following year, a breakthrough discovery reported that Mincle was an essential receptor for mycobacterial cord factor (trehalose-6,6′-dimycolate, TDM). Mincle gained increasing attention immediately after this critical finding. Although our understanding of the recognition ofMycobacteriahas been advanced significantly, it was also revealed that Mincle interacts with pathogens other thanMycobacteria. In addition, endogenous ligands of Mincle were identified recently. Therefore, Mincle is now considered a danger receptor both for self and non-self ligands, so-called damage-associated molecular patterns (DAMPs) and pathogen-associated molecular patterns (PAMPs). This chapter will give an overview of the accumulated knowledge of the multi-task danger receptor Mincle from its discovery to the latest findings.