ArticleImmunogenetics2011
Rhesus macaque KIR bind human MHC class I with broad specificity and recognize HLA-C more effectively than HLA-A and HLA-B.
Article in Immunogenetics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
15 citing papers in PubMed, 18 citations in OpenAlex.
- Expanded NK cells used for adoptive cell therapy maintain diverse clonality and contain long-lived memory-like NK cell populations.Molecular therapy oncolytics · 2023Article
- HLA Alleles BFrontiers in immunology · 2021Article
- Two to Tango: Co-evolution of Hominid Natural Killer Cell Receptors and MHC.Frontiers in immunology · 2019Review
- Conservation, Extensive Heterozygosity, and Convergence of Signaling Potential All Indicate a Critical Role for KIR3DL3 in Higher Primates.Frontiers in immunology · 2019Article
- Deciphering the killer-cell immunoglobulin-like receptor system at super-resolution for natural killer and T-cell biology.Immunology · 2017Review
- The production of KIR-Fc fusion proteins and their use in a multiplex HLA class I binding assay.Journal of immunological methods · 2015Article
- Co-evolution of MHC class I and variable NK cell receptors in placental mammals.Immunological reviews · 2015Review
- TLR/NCR/KIR: Which One to Use and When?Frontiers in immunology · 2014Review
- Virus encoded MHC-like decoys diversify the inhibitory KIR repertoire.PLoS computational biology · 2013Article
- Degenerate recognition of MHC class I molecules with Bw4 and Bw6 motifs by a killer cell Ig-like receptor 3DL expressed by macaque NK cells.Journal of immunology (Baltimore, Md. : 1950) · 2012Article
- Characterisation of mouse monoclonal antibodies against rhesus macaque killer immunoglobulin-like receptors KIR3D.Immunogenetics · 2012Article
- Mutation at positively selected positions in the binding site for HLA-C shows that KIR2DL1 is a more refined but less adaptable NK cell receptor than KIR2DL3.Journal of immunology (Baltimore, Md. : 1950) · 2012Article
- Human-specific evolution of killer cell immunoglobulin-like receptor recognition of major histocompatibility complex class I molecules.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- Review: Immunogenetics of human placentation.Placenta · 2012Review
- Diverse functionality among human NK cell receptors for the C1 epitope of HLA-C: KIR2DS2, KIR2DL2, and KIR2DL3.Frontiers in immunology · 2012Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Human killer cell immunoglobulin-like receptors (KIR) recognize A3/11, Bw4, C1, and C2 epitopes carried by mutually exclusive subsets of human leukocyte antigen (HLA)-A, -B, and -C allotypes. Chimpanzee and orangutan have counterparts to HLA-A, -B, and -C, and KIR that recognize the A3/11, Bw4, C1, and C2 epitopes, either individually or in combination. Because rhesus macaque has counterparts of HLA-A and -B, but not HLA-C, we expected that rhesus KIR would better recognize HLA-A and -B, than HLA-C. Comparison of the interactions of nine rhesus KIR3D with 95 HLA isoforms, showed the KIR have broad specificity for HLA-A, -B, and -C, but vary in avidity. Considering both the strength and breadth of reaction, HLA-C was the major target for rhesus KIR, followed by HLA-B, then HLA-A. Strong reactions with HLA-A were restricted to the minority of allotypes carrying the Bw4 epitope, whereas strong reactions with HLA-B partitioned between allotypes having and lacking Bw4. Contrasting to HLA-A and -B, every HLA-C allotype bound to the nine rhesus KIR. Sequence comparison of high- and low-binding HLA allotypes revealed the importance of polymorphism in the helix of the α(1) domain and the peptide-binding pockets. At peptide position 9, nonpolar residues favor binding to rhesus KIR, whereas charged residues do not. Contrary to expectation, rhesus KIR bind more effectively to HLA-C, than to HLA-A and -B. This property is consistent with major histocompatibility complex (MHC)-C having evolved in hominids to be a generally superior ligand for KIR than MHC-A and MHC-B.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.