Binding to IL1a and not to IL1 nor IL1Ra, Neutralizing biological effects of natural and recombinant IL1a, Inhibition of IL1a binding to IL1 receptors
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Description
Interleukin-1 (IL-1) defines two polypeptides, IL-1α and IL-1β, that possess a wide spectrum of biological effects. Two natural antagonists of IL-1 action have been characterized: the IL-1 receptor antagonist (IL-1Ra) and a soluble form of the type II IL-1 receptor. Neutralizing autoantibodies to IL-1α have also been detected in sera of healthy individuals and patients with autoimmune or inflammatory diseases. By combining CD40-activation and Epstein-Barr virus-immortalization of B lymphocytes from individuals with circulating anti-IL-1α, a natural anti-IL-1α monoclonal autoantibody was developed that bound specifically to human IL-1α, but not to IL-1β and IL-1Ra, with a high affinity (Kd = 1.2 x 10-10 M). HuMAb X3 inhibited IL-1α binding to IL-1 receptors and neutralized biological activities of both recombinant and natural forms of IL-1α. This high affinity neutralizing anti-IL-1α human autoantibody can function as a third type of IL-1 antagonist. (Garrone P et al, Mol Immunol 1996, 33 (7-8), 649-58 ; Guillot-Chene P, Lebecque S, Rigal D, Annales Pharmaceutiques Francaises, 06/2009, 67 (3) 182-6).