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J Gen Virol 67 (1986), 1205-1209; DOI 10.1099/0022-1317-67-6-1205
© 1986 Society for General Microbiology
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Binding of Murine 125I-labelled Natural Interferon-{gamma} to Murine Cell Receptors

F. Cofano, A. Fassio, G. Cavallo and S. Landolfo

Department of Microbiology, Medical School, University of Torino, Via Santena 9, 10126-Torino, Italy

Natural murine interferon-{gamma} (naMuIFN-{gamma}) produced by T-lymphoma cells (L12-R4) stimulated with phorbol myristic acetate was purified by use of an anti-MuIFN-{gamma} immunoadsorbent and was labelled with 125I to study its binding to murine cell receptors. All the cell lines examined bound naMuIFN-{gamma}, although the binding affinity varied considerably. By adding increasing concentrations of unlabelled naMuIFN-{gamma} in competition binding assays we determined dissociation constants (KD) of 8.2 x 10-10 and 7.4 x 10-10 M for L1210 and TS/A cells, respectively, and of 6.5 x 10-9 M for L-929 cells. The numbers of receptors present per cell of these lines were 3000, 1000 and 2000 respectively. Highly purified naMuIFN-{gamma} as well as recombinant MuIFN-{gamma} competed for binding sites with 125I-labelled IFN-{gamma} on L1210 cells, although the latter displayed a KD greater than the former (5.8 x 10-9 M compared to 8.2 x 10-10 M). Moreover, protease, but not endoglycosidase, treatment of target cells prevented the subsequent binding of 125I-labelled IFN-{gamma}, suggesting that a protein moiety is involved in the binding of the ligand. These studies demonstrate that naMuIFN-{gamma} binds in a specific manner and with high affinity to murine cell receptors.

Keywords: interferon (MuIFN-{gamma}), receptors, murine cells

Received 2 December 1985; accepted 26 February 1986.




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Copyright © 1986 by the Society for General Microbiology.