NKB1: A Killer Cell Inhibitory Receptor for Class I HLA-B Allotypes

Author(s):  
Annalisa D�Andrea ◽  
Lewis L. Lanier
1997 ◽  
Vol 27 (2) ◽  
pp. 563-567 ◽  
Author(s):  
Marta Carretero ◽  
Claudia Cantoni ◽  
Teresa Bellón ◽  
Cristina Bottino ◽  
Roberto Biassoni ◽  
...  

1997 ◽  
Vol 52 (1) ◽  
pp. 1-11 ◽  
Author(s):  
Neil T. Young ◽  
Mike Bunce ◽  
Peter J. Morris ◽  
Ken I. Welsh

1997 ◽  
Vol 185 (8) ◽  
pp. 1523-1528 ◽  
Author(s):  
Sumati Rajagopalan ◽  
Eric O. Long

Natural killer (NK) cells in mice and humans express a number of structurally diverse receptors that inhibit target cell lysis upon recognition of major histocompatibility complex (MHC) class I molecules expressed on targets. The contribution of peptide to the structural features of class I required for NK cell inhibition appears to vary depending on the type of receptor engaged. Thus, while there is no peptide specificity in NK inhibition mediated by Ly-49A in the mouse, human histocompatibility antigen (HLA)-B*2705–specific NK clones displayed selectivity for peptides. In this report, we examine the role of peptide in the recognition of HLA-C by the defined killer cell inhibitory receptor (KIR) cl42 with established specificity for HLA-Cw4. Binding of soluble KIR cl42 molecules to HLA-Cw4 expressed on transporter associated with antigen presentation (TAP)-deficient RMA-S cells occurred only upon exogenous peptide loading. Moreover, there was peptide selectivity in that certain substitutions at positions 7 and 8 of the nonamer peptide QYDDAVYKL abolished Cw4 interaction with KIR cl42 despite similar surface expression of HLA-C. The specificity of this direct interaction between peptideloaded HLA-Cw4 on RMA-S cells and soluble KIR cl42 correlated with recognition by NK clones in that they were inhibited only by HLA-Cw4 loaded with the appropriate peptides.


1996 ◽  
Vol 48 (4) ◽  
pp. 278-284 ◽  
Author(s):  
J. E. Gumperz ◽  
J. C. M. Paterson ◽  
V. Litwin ◽  
N. Valiante ◽  
L. L. Lanier ◽  
...  

2001 ◽  
Vol 41 (supplement) ◽  
pp. S47
Author(s):  
S. Goda ◽  
A. Yokota ◽  
M. Shiroishi ◽  
K. Tsumoto ◽  
K. Maenaka ◽  
...  

1998 ◽  
Vol 54 (3) ◽  
pp. 433-435 ◽  
Author(s):  
Katsumi Maenaka ◽  
Takeo Juji ◽  
Kenji Tadokoro ◽  
Karl Harlos ◽  
David I. Stuart ◽  
...  

Molecules of the human killer cell inhibitory receptor (KIR) family, which belong to the immunoglobulin superfamily (IgSF), are expressed on the surface of natural killer (NK) cells and some subsets of T cells. These receptors function to mediate the inhibition or activation of cytotoxic activity by recognizing HLA class I molecules on the target cell. The extracellular region of a p58 KIR specific for HLA-Cw1,3,7 (KIR2) has been overproduced in Escherichia coli and purified. The recombinant KIR2 has been crystallized in 9–10% poly(ethylene glycol) methyl ether (average Mr = 8000), 50mM HEPES, 8% ethylene glycol, 0.5% octyl-β-glucoside, pH 7.5, at 294 K using the sitting-drop vapour-diffusion method. Preliminary X-ray diffraction studies reveal the space group to be hexagonal (P6122 or P6522) with lattice constants a = b = 95.3, c = 130.8 Å. A native data set (3 Å resolution) has been collected at the Photon Factory (λ = 1.0 Å).


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