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(09)00098-3
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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
人巨细胞病毒糖蛋白，UL 16，结合到一个新的分子家族，ULBP的两个成员，和MHC I类同源物，小鼠。ULBP是属于扩展的MHC I类家族的GPI连接的糖蛋白，但仅与小鼠有远亲关系。ULBP和MICE分子是活化受体NKG 2D/DAP 10的配体，这种相互作用被可溶性形式的UL 16阻断。ULBP刺激NK细胞产生细胞因子和趋化因子，并且ULBP在NK细胞抗性靶细胞中的表达赋予对NK细胞细胞毒性的易感性。通过UL 16掩蔽NK细胞对ULBP或MIC抗原的识别提供了一种潜在的机制，通过该机制，人巨细胞病毒感染的细胞可以逃避免疫系统的攻击。
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.