
pmid: 17182537
Abstract Although it is clear that KIR3DL1 recognizes Bw4+ HLA-B, the role of Bw4+ HLA-A allotypes as KIR3DL1 ligands is controversial. We therefore examined the binding of tetrameric HLA-A and –B complexes, including HLA*2402, a common Bw4+ HLA-A allotype, to KIR3DL1*001, *005, *007, and *1502 allotypes. Only Bw4+ tetramers bound KIR3DL1. Three of four HLA-A*2402 tetramers bound one or more KIR3DL1 allotypes and all four KIR3DL1 allotypes bound to one or more HLA-A*2402 tetramers, but with different binding specificities. Only KIR3DL1*005 bound both HLA-A*2402 and HLA-B*5703 tetramers. HLA-A*2402-expressing target cells were resistant to lysis by NK cells expressing KIR3DL1*001 or *005. This study shows that HLA-A*2402 is a ligand for KIR3DL1 and demonstrates how the binding of KIR3DL1 to Bw4+ ligands depends upon the bound peptide as well as HLA and KIR3DL1 polymorphism.
Models, Molecular, Polymorphism, Genetic, HLA-A Antigens, Histocompatibility Antigens Class I, Molecular Sequence Data, HLA-A24 Antigen, Receptors, KIR3DL1, Ligands, Killer Cells, Natural, Receptors, KIR, HLA-B Antigens, 616, Humans, Amino Acid Sequence, Receptors, Immunologic, Peptides, Alleles
Models, Molecular, Polymorphism, Genetic, HLA-A Antigens, Histocompatibility Antigens Class I, Molecular Sequence Data, HLA-A24 Antigen, Receptors, KIR3DL1, Ligands, Killer Cells, Natural, Receptors, KIR, HLA-B Antigens, 616, Humans, Amino Acid Sequence, Receptors, Immunologic, Peptides, Alleles
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