Article: article from journal or magazin.
T-cell hybridoma specific for a cytochrome c peptide: specific antigen binding and interleukin 2 production.
Proceedings of the National Academy of Sciences of the United States of America
T-cell hybridomas were obtained after fusion of BW 5147 thymoma and long-term cultured T cells specific for cytochrome c peptide 66-80 derivatized with a 2,4-dinitroaminophenyl (DNAP) group. The resulting hybridomas were selected for their capacity to specifically bind to soluble radiolabeled peptide antigen. One T-cell hybrid was positive for antigen binding. This hybrid T cell exhibits surface phenotypic markers of the parent antigen-specific T cells. The binding could be inhibited either by an excess of unlabeled homologous antigen or by cytochrome c peptide 11-25 derivatized with a 2-nitrophenylsulfenyl group. Several other peptide antigens tested failed to inhibit binding of the radioactive peptide. This suggests that a specific amino acid sequence, modified by a DNAP group, is the antigenic structure recognized by the putative T-cell receptor. In addition, direct interaction of DNAP-66-80 peptide with the hybridoma cell line induced production of the T-cell growth factor interleukin 2. Furthermore, supernatants derived from syngeneic macrophages pulsed with the relevant peptide also induced the antigen-specific hybridoma to produce interleukin 2.
Amino Acid Sequence, Animals, Cells, Cultured, Cytochrome c Group/immunology, Epitopes/analysis, Female, Hybridomas/immunology, Interleukin-2/biosynthesis, Macrophages/immunology, Mice, Mice, Inbred AKR, Mice, Inbred Strains, Neoplasms, Experimental/immunology, Peptide Fragments/immunology, T-Lymphocytes/immunology, Thymoma/immunology, Thymus Neoplasms/immunology
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