HLA Class I Allelic Sequence and Conformation Regulate Leukocyte Ig-Like Receptor Binding
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- Des C Jones
- Immunology Division, Department of Pathology, University of Cambridge , Cambridge CB2 1QP ,
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- Vasilis Kosmoliaptsis
- Tissue Typing Laboratories, Addenbrookes Hospital , Cambridge, CB2 0QQ
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- Richard Apps
- Immunology Division, Department of Pathology, University of Cambridge , Cambridge CB2 1QP ,
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- Nicolas Lapaque
- Institut National de la Recherche Agronomique, Unité Mixte de Recherche, 1319 Micalis , Domaine de Vilvert, F-78352 Jouy-en-Josas ,
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- Isobel Smith
- Immunology Division, Department of Pathology, University of Cambridge , Cambridge CB2 1QP ,
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- Azumi Kono
- Department of Basic Medical Science and Molecular Medicine, Tokai University School of Medicine , Isehara, Kanagawa 259-1143 ,
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- Chiwen Chang
- Immunology Division, Department of Pathology, University of Cambridge , Cambridge CB2 1QP ,
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- Louise H Boyle
- Immunology Division, Department of Pathology, University of Cambridge , Cambridge CB2 1QP ,
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- Craig J Taylor
- Tissue Typing Laboratories, Addenbrookes Hospital , Cambridge, CB2 0QQ
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- John Trowsdale
- Immunology Division, Department of Pathology, University of Cambridge , Cambridge CB2 1QP ,
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- Rachel L Allen
- Centre for Infection, St. George’s Hospital, University of London , London SW17 0RE ,
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説明
<jats:title>Abstract</jats:title> <jats:p>Leukocyte Ig-like receptors (LILRs) are a family of innate immune receptors predominantly expressed by myeloid cells that can alter the Ag presentation properties of macrophages and dendritic cells. Several LILRs bind HLA class I. Altered LILR recognition due to HLA allelic variation could be a contributing factor in disease. We comprehensively assessed LILR binding to >90 HLA class I alleles. The inhibitory receptors LILRB1 and LILRB2 varied in their level of binding to different HLA alleles, correlating in some cases with specific amino acid motifs. LILRB2 displayed the weakest binding to HLA-B*2705, an allele genetically associated with several autoimmune conditions and delayed progression of HIV infection. We also assessed the effect of HLA class I conformation on LILR binding. LILRB1 exclusively bound folded β2-microglobulin–associated class I, whereas LILRB2 bound both folded and free H chain forms. In contrast, the activating receptor LILRA1 and the soluble LILRA3 protein displayed a preference for binding to HLA-C free H chain. To our knowledge, this is the first study to identify the ligand of LILRA3. These findings support the hypothesis that LILR-mediated detection of unfolded versus folded MHC modulates immune responses during infection or inflammation.</jats:p>
収録刊行物
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- The Journal of Immunology
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The Journal of Immunology 186 (5), 2990-2997, 2011-03-01
Oxford University Press (OUP)
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キーワード
- Protein Folding
- MYELOMONOCYTIC CELLS
- Protein Conformation
- [SDV]Life Sciences [q-bio]
- Amino Acid Motifs
- Genes, MHC Class I
- ACTIVATED T-CELLS
- SURFACE EXPRESSION
- HLA-C Antigens
- IMMUNOGLOBULIN-LIKE RECEPTORS
- HLA Antigens
- INHIBITORY RECEPTOR
- Humans
- C HEAVY-CHAINS
- Myeloid Cells
- Amino Acid Sequence
- Receptors, Immunologic
- Alleles
- HLA-B27 Antigen
- CUTTING EDGE
- Membrane Glycoproteins
- MULTIPLE-SCLEROSIS
- MHC CLASS-I
- HEK293 Cells
- HUMAN DENDRITIC CELLS
- beta 2-Microglobulin
- Protein Binding
詳細情報 詳細情報について
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- CRID
- 1361699993637756416
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- ISSN
- 15506606
- 00221767
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- PubMed
- 21270408
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- データソース種別
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- Crossref
- OpenAIRE
