Binding of labelled influenza matrix peptide to HLA DR in living B lymphoid cells

• Published in: Nature (London) 1989-06, Vol.339 (6223), p.392-394
• Main Authors: Ceppellini, Ruggero, Frumento, Guido, Ferrara, Giovanni B, Tosi, Roberto, Chersi, Alberto, Pernis, Benvenuto
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Antigen-antibody reactions, antigen-antibody complexes, antibody-complement and others. Study of affinity. Antigen presentation; B-Lymphocytes - immunology; Biological and medical sciences; Fundamental and applied biological sciences. Psychology; Fundamental immunology; Genetics; HLA-DR Antigens - immunology; Humanities and Social Sciences; Humans; In Vitro Techniques; Influenza; Influenza A virus - immunology; influenza virus; Kinetics; letter; Major Histocompatibility Complex; Medical research; Molecular immunology; Molecular Sequence Data; multidisciplinary; Peptides; Protein Binding; Proteins; Science; Science (multidisciplinary); T-Lymphocytes - immunology; Viral Matrix Proteins - immunology
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/339392a0

T CELLS recognize protein antigens as fragments (peptides) held in a defined binding site 1 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 2–6 . 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 7–9 . 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.