The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Direct Binding and Functional Transfer of NK Cell Inhibitory Receptors Reveal Novel Patterns of HLA-C Allotype Recognition
Open accessAbstract
Cytotoxicity of human NK cells is under negative control of killer cell Ig-like receptors (KIR) specific for HLA class I. To determine the specificity of five KIR containing two Ig domains (KIR2D), direct binding of soluble recombinant KIR2D to a panel of HLA class I transfectants was assayed. One soluble KIR2D, derived from an inhibitory receptor with a long cytoplasmic tail (KIR2DL1), bound to HLA-C allotypes containing asparagine 77 and lysine 80 in the heavy chain, as expected, since these allotypes inhibit lysis by NK cells expressing KIR2DL1. Surprisingly, another KIR2D (KIR2DL2), which inhibits NK lysis of cells expressing HLA-C molecules with serine 77 and asparagine 80, bound to HLA-C allotypes carrying either amino acid motif. Expression of the KIR2DL receptors in NK cells using recombinant vaccinia viruses confirmed these patterns of recognition, and identified KIR2DL3 as another KIR reacting with both groups of HLA-C allotypes. Mutagenesis of amino acid 44 in KIR2DL1 and KIR2DL2 suggested this residue controls the affinity of KIR for the 77/80 motif of HLA-C molecules. Two other soluble KIR2D, derived from noninhibitory receptors with short cytoplasmic tails (KIR2DS), did not bind to any of the HLA class I allotypes tested. One of these receptors (KIR2DS2) is closely related in sequence to KIR2DL2. Substitution of tyrosine 45 with the phenylalanine conserved in other KIR was sufficient to permit specific binding of KIR2DS2 to HLA-C. These results show that KIR2DL receptors are specific for HLA-C, but that recognition of HLA-C allotypes appears more permissive than indicated by previous functional experiments.
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Cites
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HLA-E binds to natural killer cell receptors CD94/NKG2A, B and C
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Recruitment of Tyrosine Phosphatase HCP by the Killer Cell Inhibitory Receptor
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Cited by
Lanier, L. L. (2005) · Annual Review of Immunology · doi:10.1146/annurev.immunol.23.021704.115526 · Cited by 2,769
MHC class I molecules and kirs in human history, health and survival
Parham, P. (2005) · Nature Reviews Immunology · doi:10.1038/nri1570 · Cited by 1,203
Self-citationHiby, S. E., Walker, J. J., O'Shaughnessy, K. M., Redman, C. W. G., Carrington, M., Trowsdale, J., & Moffett, A. (2004) · The Journal of Experimental Medicine · doi:10.1084/jem.20041214 · Cited by 1,121
KIR: Diverse, Rapidly Evolving Receptors of Innate and Adaptive Immunity
Vilches, C., & Parham, P. (2002) · Annual Review of Immunology · doi:10.1146/annurev.immunol.20.092501.134942 · Cited by 986
Self-citationREGULATION OF IMMUNE RESPONSES THROUGH INHIBITORY RECEPTORS
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Metadata
- Authors
- Winter, C. C., Gumperz, J. E., Parham, P., Long, E. O., & Wagtmann, N.
- Venue
- The Journal of Immunology
- Publisher
- Oxford University Press (OUP)
- Published
- 1998-07
- Volume
- 161
- Issue
- 2
- Pages
- 571-577
- ISSN
- 0022-1767 (ISSN-L)
- 1550-6606
- OpenAlex
- W1538843350
- Cited by
- 422
- References
- 30
- FWCI
- 5.14
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Winter, C. C., Gumperz, J. E., Parham, P., Long, E. O., & Wagtmann, N. (1998). Direct Binding and Functional Transfer of NK Cell Inhibitory Receptors Reveal Novel Patterns of HLA-C Allotype Recognition. The Journal of Immunology. https://doi.org/10.4049/jimmunol.161.2.571
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