Monoclonal antibodies which differentiate high- and low-affinity binding sites of interleukin-2.
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.
Takemoto
H
H
Shionogi Research Laboratories, Shionogi & Co., Ltd., Osaka, Japan.
Murai
Y
Y
Ide
M
M
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D001665:Binding Sites; D002460:Cell Line; D006825:Hybridomas / Q000276:immunology; D007376:Interleukin-2 / Q000276:immunology / Q000378:metabolism*; D051379:Mice; D015375:Receptors, Interleukin-2 / Q000378:metabolism*
D000911:Antibodies, Monoclonal; D007376:Interleukin-2; D015375:Receptors, Interleukin-2