Unknown

Dataset Information

0

Peptide antagonism as a mechanism for NK cell activation.


ABSTRACT: Inhibition of natural killer (NK) cells is mediated by MHC class I receptors including the killer cell Ig-like receptor (KIR). We demonstrate that HLA-C binding peptides can function as altered peptide ligands for KIR and antagonize the inhibition mediated by KIR2DL2/KIR2DL3. Antagonistic peptides promote clustering of KIR at the interface of effector and target cells, but do not result in inhibition of NK cells. Our data show that, as for T cells, small changes in the peptide content of MHC class I can regulate NK cell activity.

SUBMITTER: Fadda L 

PROVIDER: S-EPMC2890497 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature

altmetric image

Publications

Peptide antagonism as a mechanism for NK cell activation.

Fadda Lena L   Borhis Gwenoline G   Ahmed Parvin P   Cheent Kuldeep K   Pageon Sophie V SV   Cazaly Angelica A   Stathopoulos Stavros S   Middleton Derek D   Mulder Arend A   Claas Frans H J FH   Elliott Tim T   Davis Daniel M DM   Purbhoo Marco A MA   Khakoo Salim I SI  

Proceedings of the National Academy of Sciences of the United States of America 20100503 22


Inhibition of natural killer (NK) cells is mediated by MHC class I receptors including the killer cell Ig-like receptor (KIR). We demonstrate that HLA-C binding peptides can function as altered peptide ligands for KIR and antagonize the inhibition mediated by KIR2DL2/KIR2DL3. Antagonistic peptides promote clustering of KIR at the interface of effector and target cells, but do not result in inhibition of NK cells. Our data show that, as for T cells, small changes in the peptide content of MHC cla  ...[more]

Similar Datasets

| S-EPMC2932735 | biostudies-literature
| S-EPMC7590165 | biostudies-literature
| S-EPMC3740970 | biostudies-literature
| S-EPMC5522033 | biostudies-literature
| S-EPMC3672982 | biostudies-literature
| S-EPMC4165707 | biostudies-literature
| S-EPMC6166863 | biostudies-literature
| S-EPMC3679313 | biostudies-literature
| S-EPMC5445099 | biostudies-literature
| S-EPMC7338465 | biostudies-literature