Interactions of HLA-B4801 with peptide and CD8
Functional properties of the B*4801 allotype were investigated using HLA class I‐deficient 221 cells transfected with B*4801 cDNA. From pool sequence analysis of endogenously bound peptides, B*4801 was shown to select for nonamer peptides having glutamine or lysine at position 2 and leucine at the c...
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| Published in: | Tissue antigens Vol. 50; no. 3; pp. 258 - 264 |
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| Main Authors: | , , , , , , , , , , |
| Format: | Journal Article |
| Language: | English |
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Blackwell Publishing Ltd
01-09-1997
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| Abstract | Functional properties of the B*4801 allotype were investigated using HLA class I‐deficient 221 cells transfected with B*4801 cDNA. From pool sequence analysis of endogenously bound peptides, B*4801 was shown to select for nonamer peptides having glutamine or lysine at position 2 and leucine at the carboxyl‐terminus. In an in vitro cell‐cell binding assay, B*4801 binds CD8α homodimers weakly due to the presence of a threonine residue at position 245 in the α3 domain. A mutant B*4801 molecule in which alanine replaces threonine 245, binds CD8α homodimers at levels comparable to those of other HLA class I allotypes. Despite the low affinity of B*4801 for CD8α, alloreactive T‐cells that recognize B*4801 molecules expressed by the 221 transfectant are inhibited by anti‐CD8 monoclonal antibodies. Analysis of 25 B*48‐expressing individuals from various populations showed threonine 245 was encoded by every B*48 allele. |
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| AbstractList | Functional properties of the B*4801 allotype were investigated using HLA class I‐deficient 221 cells transfected with B*4801 cDNA. From pool sequence analysis of endogenously bound peptides, B*4801 was shown to select for nonamer peptides having glutamine or lysine at position 2 and leucine at the carboxyl‐terminus. In an in vitro cell‐cell binding assay, B*4801 binds CD8α homodimers weakly due to the presence of a threonine residue at position 245 in the α3 domain. A mutant B*4801 molecule in which alanine replaces threonine 245, binds CD8α homodimers at levels comparable to those of other HLA class I allotypes. Despite the low affinity of B*4801 for CD8α, alloreactive T‐cells that recognize B*4801 molecules expressed by the 221 transfectant are inhibited by anti‐CD8 monoclonal antibodies. Analysis of 25 B*48‐expressing individuals from various populations showed threonine 245 was encoded by every B*48 allele. Functional properties of the B*4801 allotype were investigated using HLA class I-deficient 221 cells transfected with B*4801 cDNA. From pool sequence analysis of endogenously bound peptides, B*4801 was shown to select for nonamer peptides having glutamine or lysine at position 2 and leucine at the carboxyl-terminus. In an in vitro cell-cell binding assay, B*4801 binds CD8 alpha homodimers weakly due to the presence of a threonine residue at position 245 in the alpha sub(3) domain. A mutant B*4801 molecule in which alanine replaces threonine 245, binds CD8 alpha homodimers at levels comparable to those of other HLA class I allotypes. Despite the low affinity of B*4801 for CD8 alpha , alloreactive T-cells that recognize B*4801 molecules expressed by the 221 transfectant are inhibited by anti-CD8 monoclonal antibodies. Analysis of 25 B*48-expressing individuals from various populations showed threonine 245 was encoded by every B*48 allele. Functional properties of the B*4801 allotype were investigated using HLA class I-deficient 221 cells transfected with B*4801 cDNA. From pool sequence analysis of endogenously bound peptides, B*4801 was shown to select for nonamer peptides having glutamine or lysine at position 2 and leucine at the carboxyl-terminus. In an in vitro cell-cell binding assay, B*4801 binds CD8 alpha homodimers weakly due to the presence of a threonine residue at position 245 in the alpha 3 domain. A mutant B*4801 molecule in which alanine replaces threonine 245, binds CD8 alpha homodimers at levels comparable to those of other HLA class I allotypes. Despite the low affinity of B*4801 for CD8 alpha, alloreactive T-cells that recognize B*4801 molecules expressed by the 221 transfectant are inhibited by anti-CD8 monoclonal antibodies. Analysis of 25 B*48-expressing individuals from various populations showed threonine 245 was encoded by every B*48 allele. Functional properties of the B*4801 allotype were investigated using HLA class I‐deficient 221 cells transfected with B*4801 cDNA. From pool sequence analysis of endogenously bound peptides, B*4801 was shown to select for nonamer peptides having glutamine or lysine at position 2 and leucine at the carboxyl‐terminus. In an in vitro cell‐cell binding assay, B*4801 binds CD8α homodimers weakly due to the presence of a threonine residue at position 245 in the α 3 domain. A mutant B*4801 molecule in which alanine replaces threonine 245, binds CD8α homodimers at levels comparable to those of other HLA class I allotypes. Despite the low affinity of B*4801 for CD8α, alloreactive T‐cells that recognize B*4801 molecules expressed by the 221 transfectant are inhibited by anti‐CD8 monoclonal antibodies. Analysis of 25 B*48‐expressing individuals from various populations showed threonine 245 was encoded by every B*48 allele. |
| Author | Clayberger, C. Markow, T. Lyu, S.-C. Petzl-Erler, M.L. Williams, R.C. Gorodezky, C. Martinez-Naves, E. Madrigal, J.A. Vullo, C.M. Barber, L.D. Parham, P. |
| Author_xml | – sequence: 1 givenname: E. surname: Martinez-Naves fullname: Martinez-Naves, E. organization: Departments of Structural Biology and Microbiology & Immunology, Stanford University School of Medicine, Stanford, California, USA – sequence: 2 givenname: L.D. surname: Barber fullname: Barber, L.D. organization: Departments of Structural Biology and Microbiology & Immunology, Stanford University School of Medicine, Stanford, California, USA – sequence: 3 givenname: J.A. surname: Madrigal fullname: Madrigal, J.A. organization: Departments of Structural Biology and Microbiology & Immunology, Stanford University School of Medicine, Stanford, California, USA – sequence: 4 givenname: C.M. surname: Vullo fullname: Vullo, C.M. organization: Laboratorio de Histocompatibilidad, Hospital Nacional de Clínicas, Córdoba National University, Córdoba, Argentina – sequence: 5 givenname: C. surname: Clayberger fullname: Clayberger, C. organization: Departments of Cardiothoracic Surgery, Stanford University School of Medicine, Stanford, California, USA – sequence: 6 givenname: S.-C. surname: Lyu fullname: Lyu, S.-C. organization: Departments of Cardiothoracic Surgery, Stanford University School of Medicine, Stanford, California, USA – sequence: 7 givenname: R.C. surname: Williams fullname: Williams, R.C. organization: Department of Immunogenetics, INORE, SSA, Mexico D.F., Mexico – sequence: 8 givenname: C. surname: Gorodezky fullname: Gorodezky, C. organization: Departments of Anthropology, Arizona State University, Tempe, USA – sequence: 9 givenname: T. surname: Markow fullname: Markow, T. organization: Departments of Zoology, Arizona State University, Tempe, USA – sequence: 10 givenname: M.L. surname: Petzl-Erler fullname: Petzl-Erler, M.L. organization: Department of Genetics, Federal University of Paraná, Brazil – sequence: 11 givenname: P. surname: Parham fullname: Parham, P. organization: Departments of Structural Biology and Microbiology & Immunology, Stanford University School of Medicine, Stanford, California, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/9331948$$D View this record in MEDLINE/PubMed |
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| Copyright | Copyright © 1997 Munksgaard |
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| References_xml | – volume: 1 start-page: 1065 year: 1992 end-page: 1220 – volume: 41 start-page: 162 year: 1995 end-page: 164 article-title: Peptide motifs of HLA‐B38 and B39 molecules publication-title: Immunogenetics – volume: 166 start-page: 956 year: 1987 end-page: 966 article-title: A single amino acid substitution in the α3 domain of an H‐2 class I molecule abrogates reactivity with CTL publication-title: J Exp Med – volume: 345 start-page: 41 year: 1990 end-page: 46 article-title: A binding site for the T‐cell co‐receptor CD8 on the α3 domain of HLA‐A2 publication-title: Nature – volume: 64 start-page: 403 year: 1992 end-page: 416 article-title: American Indian prehistory as written in the mitochondrial DNA: a review publication-title: Hum Biol – volume: 244 start-page: 169 year: 1991 end-page: 177 article-title: CD8 independence and specificity of cytotoxic T lymphocytes restricted by HLA‐Aw68.1 publication-title: Proc R Soc Land B – volume: 357 start-page: 326 year: 1992 end-page: 329 article-title: Unusual HLA‐B alleles in two tribes of Brazilian Indians publication-title: Nature (Lond) – volume: 14 start-page: 9 year: 1978 end-page: 20 article-title: Production of monoclonal antibodies to group A erythrocytes. HLA and other human cell surface antigens. 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| Snippet | Functional properties of the B*4801 allotype were investigated using HLA class I‐deficient 221 cells transfected with B*4801 cDNA. From pool sequence analysis... Functional properties of the B*4801 allotype were investigated using HLA class I-deficient 221 cells transfected with B*4801 cDNA. From pool sequence analysis... |
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| SubjectTerms | Alleles Amerindian B4801 CD8 CD8 Antigens - metabolism Cell Line HLA class I HLA-B Antigens - metabolism Humans Mutagenesis, Site-Directed peptide-binding Polymerase Chain Reaction Polymorphism, Genetic Protein Binding T-Lymphocytes, Cytotoxic - immunology Transfection |
| Title | Interactions of HLA-B4801 with peptide and CD8 |
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