TY - JOUR
T1 - The lectin-like NK cell receptor Ly-49A recognizes a carbohydrate- independent epitope on its MHC class I ligand
AU - Matsumoto, Naoki
AU - Ribaudo, Randall K.
AU - Abastado, Jean Pierre
AU - Margulies, David H.
AU - Yokoyama, Wayne M.
N1 - Funding Information:
We thank Michael Brown and Jonathan Heusel for helpful discussions, and Hamish Smith for critical review of this manuscript. This work was supported by grants from the National Institutes of Health and by funds from the Barnes-Jewish Hospital Foundation. N. M. was supported by a fellowship from the Eastern Missouri Chapter of the Arthritis Foundation. W. M. Y. is an Investigator of the Howard Hughes Medical Institute.
PY - 1998/2
Y1 - 1998/2
N2 - The mouse NK inhibitory Ly-49A receptor specifically interacts with a peptide-induced conformational determinant on its MHC class I ligand, H- 2D(d). In addition, it binds the polysaccharide fucoidan, consistent with its C-type lectin homology and the hypothesis that Ly-49A interacts with carbohydrates on D(d). Herein, however, we demonstrate that Ly-49A recognizes D(d) mutants lacking N-glycosylation. Fucoidan competes for binding with anti-Ly-49A antibodies that inhibit Ly-49A-D(d) interaction, and blocks apparent Ly-49A binding to unglycosylated D(d). We confirm that Ly-49A recognizes the α1 and amino-terminal α2 domains of D(d) by analysis of recombinant H-2K(d)-H-2D(d) molecules. These studies indicate that Ly-49A recognizes carbohydrate-independent epitope(s) on D(d) and suggest that Ly- 49A has two distinct ligands, carbohydrate and MHC class I.
AB - The mouse NK inhibitory Ly-49A receptor specifically interacts with a peptide-induced conformational determinant on its MHC class I ligand, H- 2D(d). In addition, it binds the polysaccharide fucoidan, consistent with its C-type lectin homology and the hypothesis that Ly-49A interacts with carbohydrates on D(d). Herein, however, we demonstrate that Ly-49A recognizes D(d) mutants lacking N-glycosylation. Fucoidan competes for binding with anti-Ly-49A antibodies that inhibit Ly-49A-D(d) interaction, and blocks apparent Ly-49A binding to unglycosylated D(d). We confirm that Ly-49A recognizes the α1 and amino-terminal α2 domains of D(d) by analysis of recombinant H-2K(d)-H-2D(d) molecules. These studies indicate that Ly-49A recognizes carbohydrate-independent epitope(s) on D(d) and suggest that Ly- 49A has two distinct ligands, carbohydrate and MHC class I.
UR - https://www.scopus.com/pages/publications/0032006214
U2 - 10.1016/S1074-7613(00)80476-8
DO - 10.1016/S1074-7613(00)80476-8
M3 - Article
C2 - 9492005
AN - SCOPUS:0032006214
SN - 1074-7613
VL - 8
SP - 245
EP - 254
JO - Immunity
JF - Immunity
IS - 2
ER -