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The Journal of Immunology, 2003, 171: 5337-5344.
Copyright © 2003 by The American Association of Immunologists

Reciprocal Transfer of Class I MHC Allele Specificity between Activating Ly-49P and Ly-49W Receptors by Exchange of {beta}4–{beta}5 Loop Residues 1

Brian J. Ma, Elizabeth T. Silver, Bart Hazes and Kevin P. Kane2

Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta, Canada

Receptors of the Ly-49 multigene family regulate rodent NK cell functions. Ly-49Rs are highly polymorphic and exist in either activating or inhibitory forms. Examples of both Ly-49 receptor types have been shown to recognize class I MHC ligands. Ly-49Rs can distinguish between class I alleles, but the molecular basis of this discrimination is unknown. Two activating receptors, Ly-49P and Ly-49W, differ in class I recognition, recognizing H-2Dd, or H-2Dd and Dk, respectively. In this report, we demonstrate that specificity for H-2Dk can be transferred from Ly-49W to Ly-49P by substituting 3 aa predicted to reside in the {beta}4–{beta}5 loop of Ly-49W into Ly-49P. Replacement of these same residues of Ly-49W with corresponding residues in Ly-49P eliminates H-2Dk recognition while still preserving H-2Dd recognition. Further mutagenesis indicates that all 3 aa facilitate optimal class I specificity exchange. These results provide the first evidence for a specific site on Ly-49Rs, the {beta}4–{beta}5 loop, in determining class I MHC allele specificity.




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