Cutting edge:: The minor histocompatibility antigen H60 peptide interacts with both H-2Kb and NKG2D

被引:25
作者
Cerwenka, A
O'Callaghan, CA
Hamerman, JA
Yadav, R
Ajayi, W
Roopenian, DC
Joyce, S
Lanier, LL
机构
[1] Univ Calif San Francisco, Dept Microbiol & Immunol, San Francisco, CA 94143 USA
[2] Univ Calif San Francisco, Inst Canc Res, San Francisco, CA 94143 USA
[3] Vanderbilt Univ, Sch Med, Dept Microbiol & Immunol, Nashville, TN 37232 USA
[4] CALTECH, Div Biol, Pasadena, CA 91125 USA
[5] Jackson Lab, Bar Harbor, ME 04609 USA
关键词
D O I
10.4049/jimmunol.168.7.3131
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
Minor histocompatibility Ags elicit cell-mediated immune responses and graft rejection in individuals receiving MHC-matched tissues. 1160 represents a dominant Ag that elicits a strong CTL response in C57BL/6 mice immunized against BALB.B. An 8-aa peptide in the H60 protein is presented by H-2K(b) and this is recognized by the TCR as an alloantigen. The intact H60 glycoprotein is a ligand for the costimulatory NKG2D receptor that is expressed by activated CD8(+) T cells. Thus, H60 may provide both an allogeneic peptide and its own costimulation. We show that mutation of an H-2K(b)-binding anchor residue in the 1160 peptide completely abrogates binding of H60 glycoprotein to NKG2D and a synthetic H60 peptide partially blocks the binding of NKG2D to its ligand. Ligands of the human NKG2D receptor are remarkably polymorphic, suggesting that these may also serve as minor histocompatibility Ags.
引用
收藏
页码:3131 / 3134
页数:4
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