The ST3Gal-I sialyltransferase controls CD8+ T lymphocyte homeostasis by modulating O-glycan biosynthesis

T lymphocyte activation evokes distinct changes in cell surface O-glycans. CD8(+) T cells undergo an elimination of sialic acid on core 10-glycans and an induction of core 2 O-glycans until either apoptotic death or differentiation into memory cells, We find that the ST3Gal-I sialyltransferase is required for core 10-glycan sialylation and its deficiency induces core 2 O-glycan biosynthesis. Apoptosis ensues with the loss of peripheral CD8(+) T cells in the absence of immune stimulation. Cell surface ligation of the ST3Gal-I substrate CD43 recapitulates this phenotype by a caspase 3-independent mechanism. Control of core 10-glycan sialylation in T lymphocytes by ST3Gal-I comprises a homeostatic mechanism that eliminates CD8(+) T cells by apoptosis while facilitating the production of viable CD8(+) memory T cells.