Human inhibitory receptors Ig-like transcript 2 (ILT2) and ILT4 compete with CD8 for MHC class I binding and bind preferentially to HLA-G
| العنوان: | Human inhibitory receptors Ig-like transcript 2 (ILT2) and ILT4 compete with CD8 for MHC class I binding and bind preferentially to HLA-G |
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| المؤلفون: | Benjamin E. Willcox, Kouhei Tsumoto, Mitsunori Shiroishi, Marco Colonna, Veronique M. Braud, Katsumi Maenaka, Izumi Kumagai, P. Anton van der Merwe, E. Yvonne Jones, Azure T Makadzange, Yasuo Shirakihara, David S.J. Allan, Sarah Rowland-Jones, Kimie Amano |
| المساهمون: | Division of Structural Biology, Kyushu University [Fukuoka]-Medical Institute of Bioregulation, Department of Biomolecular Engineering, Graduate School of Engineering-Tohoku University [Sendai], Structural Biology Center, National Institute of Genetics (NIG), Department of Pathology and Immunology, Washington University School of Medicine, Nuffield Department of Clinical Medicine [Oxford], University of Oxford [Oxford], Institut de pharmacologie moléculaire et cellulaire (IPMC), Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Centre National de la Recherche Scientifique (CNRS), Cancer Research UK Receptor Structure Group, Wellcome Trust Centre for Human Genetics, Sir William Dunn School of Pathology [Oxford], Ministry of Education, Sports, Culture, and Technology of Japan, the 2000th year Joint Research Project of Sokendai, Nakajima Foundation, Cancer Research UK, Medical Research Council |
| المصدر: | Proceedings of the National Academy of Sciences of the United States of America Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2003, 100 (15), pp.8856-61. ⟨10.1073/pnas.1431057100⟩ |
| سنة النشر: | 2016 |
| مصطلحات موضوعية: | Models, Molecular, Protein Conformation, MESH: Sequence Homology, Amino Acid, MESH: Membrane Glycoproteins, Leukocyte Immunoglobulin-like Receptor B1, MESH: Amino Acid Sequence, Protein tyrosine phosphatase, CD8-Positive T-Lymphocytes, MESH: Base Sequence, Leukocyte immunoglobulin-like receptors, MESH: Histocompatibility Antigens Class I, MESH: Recombinant Proteins, MESH: Protein Conformation, 0302 clinical medicine, HLA Antigens, HLA-G, Immunoreceptor tyrosine-based activation motif, Receptors, Immunologic, MESH: Antigens, CD, MESH: HLA Antigens, 0303 health sciences, Membrane Glycoproteins, Multidisciplinary, MESH: Kinetics, biology, Biological Sciences, MESH: CD8-Positive T-Lymphocytes, Recombinant Proteins, MESH: Surface Plasmon Resonance, Cell biology, Killer Cells, Natural, [SDV.IMM]Life Sciences [q-bio]/Immunology, Immunoreceptor tyrosine-based inhibitory motif, MESH: Models, Molecular, MESH: Killer Cells, Natural, DNA, Complementary, CD8 Antigens, Molecular Sequence Data, MESH: Binding, Competitive, In Vitro Techniques, Binding, Competitive, 03 medical and health sciences, Antigens, CD, Cell surface receptor, MHC class I, Humans, Amino Acid Sequence, MESH: Receptors, Immunologic, 030304 developmental biology, HLA-G Antigens, Binding Sites, MESH: Humans, MESH: Molecular Sequence Data, Base Sequence, Sequence Homology, Amino Acid, Histocompatibility Antigens Class I, MESH: DNA, Complementary, Surface Plasmon Resonance, Molecular biology, Kinetics, MESH: Binding Sites, biology.protein, MESH: Antigens, CD8, 030215 immunology |
| الوصف: | Ig-like transcript 4 (ILT4) (also known as leukocyte Ig-like receptor 2, CD85d, and LILRB2) is a cell surface receptor expressed mainly on myelomonocytic cells, whereas ILT2 (also known as leukocyte Ig-like receptor 1, CD85j, and LILRB1) is expressed on a wider range of immune cells including subsets of natural killer and T cells. Both ILTs contain immunoreceptor tyrosine-based inhibitory receptor motifs in their cytoplasmic tails that inhibit cellular responses by recruiting phosphatases such as SHP-1 (Src homology 2 domain containing tyrosine phosphatase 1). Although these ILTs have been shown to recognize a broad range of classical and nonclassical human MHC class I molecules (MHCIs), their precise binding properties remain controversial. We have used surface plasmon resonance to analyze the interaction of soluble forms of ILT4 and ILT2 with several MHCIs. Although the range of affinities measured was quite broad (Kd= 2–45 μM), some interesting differences were observed. ILT2 generally bound with a 2- to 3-fold higher affinity than ILT4 to the same MHCI. Furthermore, ILT2 and ILT4 bound to HLA-G with a 3- to 4-fold higher affinity than to classical MHCIs, suggesting that ILT/HLA-G recognition may play a dominant role in the regulation of natural killer, T, and myelomonocytic cell activation. Finally, we show that ILT2 and ILT4 effectively compete with CD8 for MHCI binding, raising the possibility that ILT2 modulates CD8+T cell activation by blocking the CD8 binding as well as by recruiting inhibitory molecules through its immunoreceptor tyrosine-based inhibitory receptor motif. |
| اللغة: | English |
| تدمد: | 0027-8424 1091-6490 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::edd83b1c2e0672d9e9d31bd829f7c7b9 https://ora.ox.ac.uk/objects/uuid:5a73b58d-9e21-4563-ad6c-6263c2c5469e |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....edd83b1c2e0672d9e9d31bd829f7c7b9 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 00278424 10916490 |
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