Binding of labelled influenza matrix peptide to HLA DR in living B lymphoid cells
| Autor: | Giovanni Battista Ferrara, Ruggero Ceppellini, Roberto Tosi, Guido Frumento, Alberto Chersi, Benvenuto Pernis |
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| Rok vydání: | 1989 |
| Předmět: |
T-Lymphocytes
Antigen presentation Molecular Sequence Data Peptide In Vitro Techniques Major histocompatibility complex Major Histocompatibility Complex Viral Matrix Proteins Antigen HLA-DR Humans Amino Acid Sequence Binding site Peptide sequence HLA-DR Antigen chemistry.chemical_classification B-Lymphocytes Multidisciplinary biology HLA-DR Antigens Virology Molecular biology Kinetics chemistry Influenza A virus biology.protein Protein Binding |
| Zdroj: | Nature. 339(6223) |
| ISSN: | 0028-0836 |
| Popis: | T cells recognize protein antigens as fragments (peptides) held in a defined binding site of class I or class II major histocompatibility (MHC) molecules. The formation of complexes between various immunologically active peptides and different MHC molecules has been demonstrated directly in binding studies between the peptides and solubilized, purified molecules of class II MHC. Studies with intact cells, living or fixed, have not directly demonstrated the binding of the peptides to MHC molecules on antigen-presenting cells, but the formation of such complexes has been shown indirectly through the capacity of antigen-presenting cells to stimulate specific T cells. Here we report evidence that supports directly the binding of radiolabelled influenza matrix peptide 17-29 to products of the human class II MHC locus HLA-DR, on living homozygous B-cell lines, and we show that the kinetics of such binding is much faster with living cells than with fixed cells. Furthermore, whereas the peptide reacts with HLA-DR molecules of all alleles, it binds preferentially to DR1, the restricting element in antigen presentation. |
| Databáze: | OpenAIRE |
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