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T lymphocyte activation evokes distinct changes in cell surface O-glycans. CD8 + T cells undergo an elimination of sialic acid on core 1 O-glycans and an induction of core 2 O-glycans until either apoptotic death or differentiation into memory cells. We find that the ST3Gal-l sialyltransferase is required for core 1 O-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-l substrate CD43 recapitulates this phenotype by a caspase 3-independent mechanism. Control of core 1 O-glycan sialylation in T lymphocytes by ST3Gal-l comprises a homeostatic mechanism that eliminates CD8 + T cells by apoptosis while facilitating the production of viable CD8 + memory T cells.
Howard Hughes Medical Institute, the Glycobiology Research and Training Center, and Department of Cellular and Molecular Medicine University of California, San Diego La Jolla, California 92093 USA
Howard Hughes Medical Institute, the Glycobiology Research and Training Center, and Department of Cellular and Molecular Medicine University of California, San Diego La Jolla, California 92093 USA
Howard Hughes Medical Institute, the Glycobiology Research and Training Center, and Department of Cellular and Molecular Medicine University of California, San Diego La Jolla, California 92093 USA