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Soluble human lymphocyte sugar binding proteins with immunosuppressive activity
C Grillon1, M Monsigny, C Kieda
1Département de Biochimie des Glycoconjugués et Lectines Endogènes, Centre de Biophysique Moléculaire, CNRS, Orléans, France.
Suppression of the immune response, which involves suppressor factors released from specialized T cells, is inhibited by alpha-L-rhamnose. In this paper, we show the presence of rhamnose-specific receptors on a human CD8+ T cell-rich population and describe a novel method to isolate cells which express a given sugar-binding protein on their surface. We describe the isolation of alpha-L-rhamnose-specific molecules (rhamnose-binding fractions: RBF) from a water-soluble extract from lymphocytes, their purification by affinity chromatography on immobilized neoglycoproteins containing rhamnose residues. RBF kept their ability to bind rhamnose, as shown by the binding of fluorescein-labeled RBF to rhamnosylated BSA-substituted beads. RBF efficiently suppresses DNA synthesis of mitogen-stimulated human lymphocytes as well as B cell immunoglobulin production. Therefore, these rhamnose-binding molecules appear to be antigen-independent suppressor factors.
Suppression of the immune response, which involves suppressor factors released from specialized T cells, is inhibited by alpha-L-rhamnose. In this paper, we show the presence of rhamnose-specific receptors on a human CD8+ T cell-rich population and describe a novel method to isolate cells which express a given sugar-binding protein on their surface. We describe the isolation of alpha-L-rhamnose-specific molecules (rhamnose-binding fractions: RBF) from a water-soluble extract from lymphocytes, their purification by affinity chromatography on immobilized neoglycoproteins containing rhamnose residues. RBF kept their ability to bind rhamnose, as shown by the binding of fluorescein-labeled RBF to rhamnosylated BSA-substituted beads. RBF efficiently suppresses DNA synthesis of mitogen-stimulated human lymphocytes as well as B cell immunoglobulin production. Therefore, these rhamnose-binding molecules appear to be antigen-independent suppressor factors.