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Identification of receptor-binding sites of human interferon-gamma by competition studies with series of synthetic peptides corresponding to different fragments of human interferon-gamma molecules


Identification of receptor-binding sites of human interferon-gamma by competition studies with series of synthetic peptides corresponding to different fragments of human interferon-gamma molecules



Immunologiya 1998(3): 24-27



ISSN/ISBN: 0206-4952

Competitive receptor-binding experiments with synthetic peptides derived from the structure of human interferon-gamma (HuIFN-g) were performed to determine receptor-binding sites of HuIFN-g. ELISA was made to study the effects of synthetic peptides 1-17, 33-43, 64-75 on binding HuIFN-g and anti-idiotypic antibodies (AITA) to the recombinant soluble extracellular HuIFN-g receptor. Two N-terminal peptides 1-17 and 33-43 exhibited a modest but reproducible competition with HuIFN-g and AITA. The competition between HuIFN-g and N-terminal peptides 1-17 and 5-14 for receptor binding was shown also by radioimmunoassay in contrast to the C-terminal peptide 120-131. It was demonstrated by competition studies that N-terminal peptides 1-17 and 33-43 competed with neutralizing monoclonal antibody D9D10 for binding to HuIFN-g. These results show the importance of the HuIFN-g N-terminus for receptor binding.

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Accession: 008809932

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