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NK cells: tuned by peptide?

NK cells: tuned by peptide?
NK cells: tuned by peptide?
Natural killer cells express multiple receptors for major histocompatibility complex (MHC) class I, including the killer cell immunoglobulin-like receptors (KIRs) and the C-type lectin-like CD94:NKG2 receptors. The KIR locus is extremely polymorphic, paralleling the diversity of its classical MHC class I ligands. Similarly, the conservation of the NKG2 family of receptors parallels the conservation of MHC-E, the ligand for CD94:NKG2A/C/E. Binding of both CD94:NKG2 heterodimers and KIR to their respective MHC class I ligand is peptide dependent, and despite the evolution of these receptors, they have retained the property of peptide selectivity. Such peptide selectivity affects these two systems in different ways. HLA-E binding non-inhibitory peptides augment inhibition at CD94:NKG2A, while HLA-C binding non-inhibitory peptides antagonize inhibition at KIR2DL2/3, implying that KIRs are specialized to respond positively to changes in peptide repertoire. Thus, while specific KIRs, such as KIR2DL3, are associated with beneficial outcomes from viral infections, viral peptides augment inhibition at CD94:NKGA. Conversely, NKG2A-positive NK cells sense MHC class I downregulation more efficiently than KIRs. Thus, these two receptor:ligand systems appear to have complementary functions in recognizing changes in MHC class I.
0105-2896
214-227
Das, J.
52f0f425-6ceb-4bf6-a1ed-14045ce04ab1
Khakoo, S.I.
6c16d2f5-ae80-4d9b-9100-6bfb34ad0273
Das, J.
52f0f425-6ceb-4bf6-a1ed-14045ce04ab1
Khakoo, S.I.
6c16d2f5-ae80-4d9b-9100-6bfb34ad0273

Das, J. and Khakoo, S.I. (2015) NK cells: tuned by peptide? Immunological Reviews, 267 (1), 214-227. (doi:10.1111/imr.12315). (PMID:26284480)

Record type: Article

Abstract

Natural killer cells express multiple receptors for major histocompatibility complex (MHC) class I, including the killer cell immunoglobulin-like receptors (KIRs) and the C-type lectin-like CD94:NKG2 receptors. The KIR locus is extremely polymorphic, paralleling the diversity of its classical MHC class I ligands. Similarly, the conservation of the NKG2 family of receptors parallels the conservation of MHC-E, the ligand for CD94:NKG2A/C/E. Binding of both CD94:NKG2 heterodimers and KIR to their respective MHC class I ligand is peptide dependent, and despite the evolution of these receptors, they have retained the property of peptide selectivity. Such peptide selectivity affects these two systems in different ways. HLA-E binding non-inhibitory peptides augment inhibition at CD94:NKG2A, while HLA-C binding non-inhibitory peptides antagonize inhibition at KIR2DL2/3, implying that KIRs are specialized to respond positively to changes in peptide repertoire. Thus, while specific KIRs, such as KIR2DL3, are associated with beneficial outcomes from viral infections, viral peptides augment inhibition at CD94:NKGA. Conversely, NKG2A-positive NK cells sense MHC class I downregulation more efficiently than KIRs. Thus, these two receptor:ligand systems appear to have complementary functions in recognizing changes in MHC class I.

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Published date: September 2015
Organisations: Clinical & Experimental Sciences

Identifiers

Local EPrints ID: 390023
URI: https://eprints.soton.ac.uk/id/eprint/390023
ISSN: 0105-2896
PURE UUID: 5b608b3a-51bb-46b6-b87d-126f55fbd040

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Date deposited: 17 Mar 2016 12:32
Last modified: 17 Jul 2017 19:31

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