scholarly journals Effective refolding of MHC class I molecule(Cw7)and killer cell inhibitory receptor(KIR2DL2)and their interaction

2001 ◽  
Vol 41 (supplement) ◽  
pp. S47
Author(s):  
S. Goda ◽  
A. Yokota ◽  
M. Shiroishi ◽  
K. Tsumoto ◽  
K. Maenaka ◽  
...  
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 184 (4) ◽  
pp. 1585-1590 ◽  
Author(s):  
M Peruzzi ◽  
N Wagtmann ◽  
E O Long

Natural killer (NK) cells express a repertoire of killer cell inhibitory receptors (KIR) for major histocompatibility complex (MHC) class I molecules. KIR specificity for MHC class I can be broad, as in the case of a single p70 KIR that can recognize several HLA-B allotypes, including HLA-B*2705. On the other hand, recognition of MHC class I can also be highly specific, as in the case of NK clones that recognize HLA-B*2705 in a peptide-specific manner. Most NK cells express multiple KIR sequences. To determine whether the broad and specific types of HLA-B recognition by NK cells reflect the use of different receptors or a property of a single KIR we analyzed the recognition of HLA-B*2705 by the p70 KIR-11, known to recognize several HLA-B allotypes. Vaccinia virus-mediated expression of KIR-11 in NK clones resulted in inhibition by HLA-B*2705 molecules on wild type but not on target cells deficient in the transporter for antigen presentation (TAP). Two peptides (FRYNGLIHR and RRSKEITVR) loaded onto HLA-B*2705 molecules on TAP-deficient cells provided protection from lysis by NK cells expressing KIR-11 but three other B27-specific peptides did not. As the five peptides bound to HLA-B*2705 with similar stability, these data demonstrate that a single KIR specific for several HLA-B allotypes recognizes a subset of peptides bound to HLA-B*2705.


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