Interleukin 1 and Its Synthetic Peptide 163–171 as Vaccine Adjuvants
Interleukin 1 (IL-1) is a family of cytokines of key importance in the mechanisms of host defense, being involved in the onset and development of both immune and inflammatory reactions (Dinarello, 1991; Boraschi and Tagliabue, 1989). The IL-1 family includes IL-1α and IL-1γ, which have similar structures and overlapping biological activities, and IL-1ra, which is a pure receptor antagonist, able to occupy the activating IL-1 receptor (IL-1RI) without exerting any agonistic effect. IL-1 binds to two types of receptors on the cell surface. IL-1RI (CDw121a) is an 80 kDa monomeric transmembrane glycoprotein of the immunoglobulin superfamily which is responsible for initiating the cell activation mechanism upon IL-1 binding. Both agonist IL-1α and IL-1β and antagonist IL-1ra bind equally well to IL-1RI. Conversely, IL-1RII (CDw121b) is a 68 kDa receptor very similar to IL-1RI in its extracellular domain, but apparently unable to initiate cell activation. The extracellular IL-1 binding domain of IL-1RII can be naturally released from the cell surface and can capture IL-1β (Fig. 1).
KeywordsVaccine Adjuvant Muramyl Dipeptide Active Specific Immunotherapy Specific Antibody Titer Human Ferritin
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