The ST3Gal-I Sialyltransferase Controls CD8+ T Lymphocyte Homeostasis by Modulating O-glycan Biosynthesis

Immunity. 2000 Mar;12(3):273-83. doi: 10.1016/s1074-7613(00)80180-6.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Antigens, CD*
  • Apoptosis
  • Base Sequence
  • CD8-Positive T-Lymphocytes / cytology
  • CD8-Positive T-Lymphocytes / metabolism*
  • Caspase 1 / metabolism
  • Caspase Inhibitors
  • Cytotoxicity, Immunologic
  • Enzyme Activation
  • Gene Expression Regulation
  • Glycoproteins / metabolism
  • Homeostasis
  • Leukosialin
  • Lymphocyte Activation
  • Mice
  • Molecular Sequence Data
  • Mutagenesis
  • Polysaccharides / biosynthesis*
  • Sialoglycoproteins / metabolism
  • Sialyltransferases / genetics
  • Sialyltransferases / metabolism*
  • Substrate Specificity

Substances

  • Antigens, CD
  • Caspase Inhibitors
  • Glycoproteins
  • Leukosialin
  • Polysaccharides
  • Sialoglycoproteins
  • Spn protein, mouse
  • Sialyltransferases
  • beta-galactoside alpha-2,3-sialyltransferase
  • Caspase 1

Associated data

  • GENBANK/AF214028
  • GENBANK/AF214029
  • GENBANK/AF214030