ArticleProceedings of the National Academy of Sciences of the United States of America1997
The alpha1 domain of HLA-G1 and HLA-G2 inhibits cytotoxicity induced by natural killer cells: is HLA-G the public ligand for natural killer cell inhibitory receptors?
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.
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89 citing papers in PubMed, 347 citations in OpenAlex.
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- Harnessing the immunomodulatory properties of HLA-G for advanced immunotherapies.Frontiers in immunology · 2025Review
- The Biological Significance of Trogocytosis.Results and problems in cell differentiation · 2024Article
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- Conventional and non-conventional antigen presentation by mast cells.Discovery immunology · 2023Review
- Variation of Complement Protein Levels in Maternal Plasma and Umbilical Cord Blood during Normal Pregnancy: An Observational Study.Journal of clinical medicine · 2022Article
- The HLA-G immune checkpoint: a new immuno-stimulatory role for the α1-domain-deleted isoform.Cellular and molecular life sciences : CMLS · 2022Article
- Review
- Biological Characteristics of HLA-G and Its Role in Solid Organ Transplantation.Frontiers in immunology · 2022Review
- Sequence Variations WithinFrontiers in immunology · 2022Article
- Primary Trophoblast Cultures: Characterization of HLA Profiles and Immune Cell Interactions.Frontiers in immunology · 2022Article
- Review
- Maternal natural killer cells at the intersection between reproduction and mucosal immunity.Mucosal immunology · 2021Review
- Selective deletion of human leukocyte antigens protects stem cell-derived islets from immune rejection.Cell reports · 2021Article
- Role and expression of non-classical human leukocyte antigen-G in renal transplanted allografts.Clinical and experimental nephrology · 2021Article
- Review
- HLA Class I Molecules as Immune Checkpoints for NK Cell Alloreactivity and Anti-Viral Immunity in Kidney Transplantation.Frontiers in immunology · 2021Review
- Fit-For-All iPSC-Derived Cell Therapies and Their Evaluation in Humanized Mice With NK Cell Immunity.Frontiers in immunology · 2021Review
- Abrogation of HLA surface expression using CRISPR/Cas9 genome editing: a step toward universal T cell therapy.Scientific reports · 2020Article
- Maternal Obesity and the Uterine Immune Cell Landscape: The Shaping Role of Inflammation.International journal of molecular sciences · 2020Review
29 more citing papers are in PubMed but not listed here.
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5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have investigated the protective role of the membrane-bound HLA-G1 and HLA-G2 isoforms against natural killer (NK) cell cytotoxicity. For this purpose, HLA-G1 and HLA-G2 cDNAs were transfected into the HLA class I-negative human K562 cell line, a known reference target for NK lysis. The HLA-G1 protein, encoded by a full-length mRNA, presents a structure similar to that of classical HLA class I antigens. The HLA-G2 protein, deduced from an alternatively spliced transcript, consists of the alpha1 domain linked to the alpha3 domain. In this study we demonstrate that (i) HLA-G2 is present at the cell surface as a truncated class I molecule associated with beta2-microglobulin; (ii) NK cytolysis, observed in peripheral blood mononuclear cells and in polyclonal CD3(-) CD16(+) CD56(+) NK cells obtained from 20 donors, is inhibited by both HLA-G1 and HLA-G2; this HLA-G-mediated inhibition is reversed by blocking HLA-G with a specific mAb; this led us to the conjecture that HLA-G is the public ligand for NK inhibitory receptors (NKIR) present in all individuals; (iii) the alpha1 domain common to HLA-G1 and HLA-G2 could mediate this protection from NK lysis; and (iv) when transfected into the K562 cell line, both HLA-G1 and HLA-G2 abolish lysis by the T cell leukemia NK-like YT2C2 clone due to interaction between the HLA-G isoform on the target cell surface and a membrane receptor on YT2C2. Because NKIR1 and NKIR2, known to interact with HLA-G, were undetectable on YT2C2, we conclude that a yet-unknown specific receptor for HLA-G1 and HLA-G2 is present on these cells.
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