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Monoclonal antibodies which differentiate high‐ and low‐affinity binding sites of interleukin‐2
Author(s) -
Takemoto Hiroshi,
Murai Yasuo,
Ide Misao
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80983-9
Subject(s) - monoclonal antibody , receptor , recombinant dna , microbiology and biotechnology , chemistry , interleukin 2 , antibody , interleukin , interleukin 1 receptor , biology , biochemistry , cytokine , immunology , gene
Five monoclonal antibodies (L15, L20, L23, L34, and L61) against human recombinant interleukin‐2 were tested for their effects on the interleukin‐2 bioactivity and binding. Four of these monoclonal antibodies, L15, L20, L34, and L61, which had neutralizing activity, completely blocked interleukin‐2 binding to the high‐affinity receptor. On the other hand, L23, which had a very weak neutralizing activity, blocked interleukin‐2 binding to the low‐affinity receptor. These results suggest that there are at least two distinct binding sites on the interleukin‐2 molecule; those for the high‐affinity receptor and those for the low‐affinity receptor. These monoclonal antibodies should be useful tools in the study of the interaction between interleukin‐2 and interleukin‐2 receptor.