NDLI: Allelic variation in KIR2DL3 generates a KIR2DL2-like receptor with increased binding to its HLA-C ligand.

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Allelic variation in KIR2DL3 generates a KIR2DL2-like receptor with increased binding to its HLA-C ligand.

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Allelic variation in KIR2DL3 generates a KIR2DL2-like receptor with increased binding to its HLA-C ligand.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Steiner, Noriko Dakshanamurthy, Sivanesan Hou, Lihua Frazier, William R. Hurley, Carolyn Katovich
Description	Country affiliation: United States Author Affiliation: Frazier WR ( Department of Oncology, C.W. Bill Young Marrow Donor Recruitment and Research Program, Georgetown University Medical Center, Washington, DC 20057, USA.)
Abstract	Although extensive homology exists between their extracellular domains, NK cell inhibitory receptors killer Ig-like receptor (KIR) 2DL2001 and KIR2DL3001 have previously been shown to differ substantially in their HLA-C binding avidity. To explore the largely uncharacterized impact of allelic diversity, the most common KIR2DL2/3 allelic products in European American and African American populations were evaluated for surface expression and binding affinity to their HLA-C group 1 and 2 ligands. Although no significant differences in the degree of cell membrane localization were detected in a transfected human NKL cell line by flow cytometry, surface plasmon resonance and KIR binding to a panel of HLA allotypes demonstrated that KIR2DL3005 differed significantly from other KIR2DL3 allelic products in its ability to bind HLA-C. The increased affinity and avidity of KIR2DL3005 for its ligand was also demonstrated to have a larger impact on the inhibition of IFN-Î³ production by the human KHYG-1 NK cell line compared with KIR2DL3001, a low-affinity allelic product. Site-directed mutagenesis established that the combination of arginine at residue 11 and glutamic acid at residue 35 in KIR2DL3005 were critical to the observed phenotype. Although these residues are distal to the KIR/HLA-C interface, molecular modeling suggests that alteration in the interdomain hinge angle of KIR2DL3005 toward that found in KIR2DL2001, another strong receptor of the KIR2DL2/3 family, may be the cause of this increased affinity. The regain of inhibitory capacity by KIR2DL3*005 suggests that the rapidly evolving KIR locus may be responding to relatively recent selective pressures placed upon certain human populations.
ISSN	00221767
e-ISSN	15506606
DOI	10.4049/jimmunol.1300464
Journal	The Journal of Immunology
Issue Number	12
Volume Number	190
Language	English
Publisher	The American Association of Immunologists
Publisher Date	2013-06-15
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Genetic Variation Hla-c Antigens Metabolism Receptors, Kir2dl2 Genetics Receptors, Kir2dl3 African Americans Alleles Amino Acid Sequence Cluster Analysis European Continental Ancestry Group Flow Cytometry Killer Cells, Natural Immunology Ligands Models, Molecular Molecular Sequence Data Mutagenesis, Site-directed Polymerase Chain Reaction Protein Binding Chemistry Research Support, N.i.h., Extramural Research Support, U.s. Gov't, Non-p.h.s. Discipline Immunology
Content Type	Text
Resource Type	Article
Subject	Immunology and Allergy Immunology

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