免疫受体酪氨酸激活基序
MHC I级
MHC限制
生物
主要组织相容性复合体
细胞生物学
蛋白质酪氨酸磷酸酶
受体
酪氨酸
人类白细胞抗原
化学
T细胞受体
分子生物学
细胞毒性T细胞
C-C趋化因子受体7型
CD8型
抗原
生物化学
免疫学
SH2域
作者
Mitsunori Shiroishi,Kouhei Tsumoto,Kimie Amano,Yasuo Shirakihara,Marco Colonna,Veronique M. Braud,David S. Allan,A. Tariro Makadzange,Sarah Rowland-Jones,Benjamin E. Willcox,E Y Jones,P. Anton van der Merwe,Izumi Kumagai,Katsumi Maenaka
标识
DOI:10.1073/pnas.1431057100
摘要
Ig-like transcript 4 (ILT4) (also known as leukocyte Ig-like receptor 2, CD85d, and LILRB2) is a cell surface receptor expressed mainly on myelomonocytic cells, whereas ILT2 (also known as leukocyte Ig-like receptor 1, CD85j, and LILRB1) is expressed on a wider range of immune cells including subsets of natural killer and T cells. Both ILTs contain immunoreceptor tyrosine-based inhibitory receptor motifs in their cytoplasmic tails that inhibit cellular responses by recruiting phosphatases such as SHP-1 (Src homology 2 domain containing tyrosine phosphatase 1). Although these ILTs have been shown to recognize a broad range of classical and nonclassical human MHC class I molecules (MHCIs), their precise binding properties remain controversial. We have used surface plasmon resonance to analyze the interaction of soluble forms of ILT4 and ILT2 with several MHCIs. Although the range of affinities measured was quite broad (Kd = 2-45 microM), some interesting differences were observed. ILT2 generally bound with a 2- to 3-fold higher affinity than ILT4 to the same MHCI. Furthermore, ILT2 and ILT4 bound to HLA-G with a 3- to 4-fold higher affinity than to classical MHCIs, suggesting that ILT/HLA-G recognition may play a dominant role in the regulation of natural killer, T, and myelomonocytic cell activation. Finally, we show that ILT2 and ILT4 effectively compete with CD8 for MHCI binding, raising the possibility that ILT2 modulates CD8+ T cell activation by blocking the CD8 binding as well as by recruiting inhibitory molecules through its immunoreceptor tyrosine-based inhibitory receptor motif.
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