Peptide binding to empty HLA-B27 molecules of viable human cells

التفاصيل البيبلوغرافية
العنوان: Peptide binding to empty HLA-B27 molecules of viable human cells
المؤلفون: Peter Parham, J A Madrigal, Richard J. Benjamin
المصدر: Nature. 351:74-77
بيانات النشر: Springer Science and Business Media LLC, 1991.
سنة النشر: 1991
مصطلحات موضوعية: T-Lymphocytes, Molecular Sequence Data, Peptide, Peptide binding, Plasma protein binding, Transfection, Major histocompatibility complex, Binding, Competitive, Cell Line, Antigen, Humans, Amino Acid Sequence, Binding site, Peptide sequence, Alleles, HLA-B27 Antigen, chemistry.chemical_classification, B-Lymphocytes, Multidisciplinary, biology, Antibodies, Monoclonal, Molecular biology, In vitro, Cell biology, Kinetics, chemistry, biology.protein, Peptides, Protein Binding
الوصف: Intracellular binding of antigenic peptides by polymorphic class I major histocompatibility complex molecules creates the ligands recognized by receptors of CD8+ T cells. Previously described in vitro assays of peptide binding to class I molecules have been limited by either the low proportion of accessible binding sites or the lack of allelic specificity. Here we describe a system in which the human class I molecule HLA-B27 binds considerable amounts of an influenza peptide with precise allelic discrimination. Binding requires viable cells, is stimulated by gamma-interferon and is inhibited by brefeldin A. Our results are consistent with the presence of fairly stable 'empty' HLA-B27 molecules at the cell surface. By contrast, analysis of the binding of a second influenza peptide indicates that empty HLA-Aw68 molecules are relatively short-lived. We speculate that HLA-B27 might bind extracellular peptides in vivo and that this property could underlie its association with autoimmune disease.
تدمد: 1476-4687
0028-0836
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42984679e8c40b1b606e7c63d3d91ad9
https://doi.org/10.1038/351074a0
حقوق: CLOSED
رقم الأكسشن: edsair.doi.dedup.....42984679e8c40b1b606e7c63d3d91ad9
قاعدة البيانات: OpenAIRE