Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

The nonclassical MHC class I molecule human histocompatibility leukocyte antigen (HLA)-G is selectively expressed on fetal trophoblast tissue at the maternal-fetal interface in pregnancy. It has long been suggested that HLA-G may inhibit maternal natural killer (NK) cells through interaction with particular NK cell receptors (KIRs). To investigate interactions of HLA-G, we constructed phycoerythrin-labeled tetrameric complexes of HLA-G refolded with a self-peptide. These HLA-G tetramers failed to bind to NK cells and cells transfected with CD94/NKG2 and killer immunoglobulin-like NK receptors. In contrast, HLA-G tetramers did bind to peripheral blood monocytes, staining a CD16(+)CD14(mid) subset with greater intensity. On transfectants, HLA-G tetramers bound to inhibitory immunoglobulin-like transcript (ILT)2 and ILT4 receptors. However, staining in the presence of antibodies reactive with ILT receptors revealed that the interaction of HLA-G tetramers with blood monocytes was largely due to binding to ILT4. These results suggest that the primary role of HLA-G may be the modulation of myelomonocytic cell behavior in pregnancy.

Original publication

DOI

10.1084/jem.189.7.1149

Type

Journal article

Journal

J Exp Med

Publication Date

05/04/1999

Volume

189

Pages

1149 - 1156

Keywords

Animals, Biopolymers, Cell Line, HLA Antigens, HLA-G Antigens, Histocompatibility Antigens Class I, Humans, Jurkat Cells, Killer Cells, Natural, Lipopolysaccharide Receptors, Macromolecular Substances, Membrane Glycoproteins, Mice, Monocytes, Protein Binding, Protein Conformation, Rats, Receptors, IgG, Receptors, Immunologic, Receptors, KIR, Recombinant Fusion Proteins, Transfection