Binding of the two polypeptide chains of dengue virus-induced suppressor cytokine to its receptor isolated from macrophages.

Dengue type 2 virus (DV)-induced suppressor cytokine (SF) is composed of two polypeptide chains (alpha and beta) and has a receptor on macrophages (M phi), which has been purified. The present study was undertaken to study the binding of the two polypeptide chains of SF to M phi and its purified receptor (SF-R) protein. It was observed that both alpha and beta-chains of SF, purified by high performance liquid chromatography (HPLC), bound to M phi cell, but only alpha-chain bound to SF-R protein. Only H-2A positive M phi bound SF. Anti-H-2Ak mAb blocked the binding of SF to M phi but had no effect on binding of SF to SF-R. Both anti-SF-antiserum and anti-SF-R-antiserum blocked the binding of SF to M phi. The binding of the beta-chain of SF to M phi was blocked by anti-H-2Ak mAb while the anti-SF-R-antiserum blocked the binding of alpha-chain on M phi. Thus, the alpha-chain of SF binds to SF-R and the beta-chain binds to H-2A determinants on M phi.