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

JJ Priatel, D Chui, N Hiraoka, CJT Simmons… - Immunity, 2000 - cell.com
JJ Priatel, D Chui, N Hiraoka, CJT Simmons, KB Richardson, DM Page, M Fukuda, NM Varki…
Immunity, 2000cell.com
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-I 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-I substrate …
Abstract
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-I 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-I substrate CD43 recapitulates this phenotype by a caspase 3–independent mechanism. Control of core 1 O-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.
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