ULBPs, novel MHC class I-related molecules bind to CMV glycoprotein UL16 and stimulate NK cytotoxicity through the NKG2D receptor
ULBPs, novel MHC class I-related molecules bind to CMV glycoprotein UL16 and stimulate NK cytotoxicity through the NKG2D receptor
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DOI：
10.1016/s1074-7613(01)00095-4
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发表时间：
2001-02-01
期刊：
影响因子：
32.4
通讯作者：
Chalupny, NJ
中科院分区：
文献类型：
--
作者：
Cosman, D;Müllberg, J;Chalupny, NJ
人类巨细胞病毒糖蛋白UL16与新型分子家族的两个成员（ULBPS）结合，并与MHC I类同源物小鼠结合。 ULBP是属于延长的MHC I类家族的GPI连接的糖蛋白，但与小鼠只有遥远的关系。 ULBP和小鼠分子是活化受体NKG2D/DAP10的配体，这种相互作用被ul16的可溶形式阻塞。 ULBP刺激NK细胞中的细胞因子和趋化因子产生，而NK细胞靶细胞中ULBP的表达赋予了NK细胞毒性的敏感性。 UL16对NK细胞对ULBP或MIC抗原的掩盖识别提供了一种潜在的机制，通过该机制，人类巨细胞病毒感染的细胞可能会通过免疫系统逃避攻击。
The human cytomegalovirus glycoprotein, UL16, binds to two members of a novel family of molecules, the ULBPs, and to the MHC class I homolog, MICE. The ULBPs are GPI-linked glycoproteins belonging to the extended MHC class I family but are only distantly related to MICE. The ULBP and MICE molecules are ligands for the activating receptor, NKG2D/DAP10, and this interaction is blocked by a soluble form of UL16. The ULBPs stimulate cytokine and chemokine production from NK cells, and expression of ULBPs in NK cell-resistant target cells confers susceptibility to NK cell cytotoxicity. Masking of NK cell recognition of ULBP or MIC antigens by UL16 provides a potential mechanism by which human cytomegalovirus-infected cells might evade attack by the immune system.