Journal of Leukocyte Biology Myeloid cells, immune suppression, tumor immunology
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Originally published online as doi:10.1189/jlb.0704407 on February 9, 2005

Published online before print February 9, 2005
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(Journal of Leukocyte Biology. 2005;77:644-651.)
© 2005 by Society for Leukocyte Biology

Epitope mapping of Ly-49G and G-like receptors: CK-1 antibody defines a polymorphic site of functional interaction with class I ligand

Mohammed S. Osman, Elizabeth T. Silver, Jay C. Varghese, Chew Shun Chang, Dong-Er Gong, Gerald F. Audette, Bart Hazes and Kevin P. Kane1

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

1 Correspondence: Department of Medical Microbiology and Immunology, 660 Heritage Medical Research Centre, University of Alberta, Edmonton, Alberta, Canada, T6G 2S2. E-mail: kevin.kane{at}ualberta.ca

Ly-49 receptors regulate mouse natural killer cell functions. Members of the polymorphic Ly-49 multigene family recognize specific alleles of major histocompatibility complex class I (MHC I) or MHC I-like proteins. Previous studies have provided insight into the nature of Ly-49A and -C interaction with their high-affinity MHC I ligands, H-2Dd and Kb, respectively. Unlike Ly-49C, recognition of MHC I by Ly-49A is regulated in part by residues within the ß4–ß5 loop of its ectodomain. Ly-49A and -G are within the same Ly-49 subfamily, and both receptors recognize Dd. However, there have been no studies that define specific sites on Ly-49G that mediate class I MHC recognition. The Ly-49G receptors of different inbred mouse strains can differ as a result of amino acid polymorphisms within their ectodomains. In this report, we have generated a novel antibody, CK-1, which recognizes Ly-49GB6 and a Ly-49GB6-like receptor, Ly-49Mnonobese diabetic, but not Ly-49GBALB/c. By exploiting the differences within ectodomains of C57BL/6 and BALB/c Ly-49G allele products, we identified epitopes recognized by the Ly-49G-specific antibodies CK-1 and Cwy-3, whose epitopes mapped within the ß4–ß5 loop and the ß1 strand, respectively, and were nonoverlapping. Although both antibodies specifically recognized the Ly-49GB6 ectodomain, Cwy-3 was unable to block its interaction with MHC I, and CK-1 significantly inhibited it. The importance of residues within the ß4–ß5 loop in Ly-49G recognition demonstrates that its interaction with MHC I is similar to that of Ly-49A but not Ly-49C.

Key Words: Ly-49 receptors • motif • ligand interaction






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