Differential Glycosylation Of T Helper Cell Subsets Selectively Regulates Susceptibility To Cell Death

MARTA A. TOSCANO; GERMÁN A. BIANCO; JUAN M. ILARREGUI; DIEGO O. CROCI; JORGE CORREALE; JOSEPH HERNANDEZ; NORBERTO W. ZWIRNER; FRANCOISE POIRIER; ELEANOR RILEY; LINDA G. BAUM; GABRIEL A. RABINOVICH

NATURE IMMUNOLOGY (PRINT)

Nature America Inc

Año: 2007 vol. 8 p. 825 - 834

1529-2908

Regulated glycosylation controls T cell processes, including activation, differentiation and homing by creating or masking ligands for endogenous lectins. Here we show that stimuli promoting T helper type 1 (TH1), TH2 or interleukin 17-producing T helper (TH-17) differentiation can differentially regulate the glycosylation pattern of T helper cells and modulate their susceptibility to galectin-1, a glycan-binding protein with anti-inflammatory activity. Although TH1- and TH-17-differentiated cells expressed the repertoire of cell surface glycans critical for galectin-1-induced cell death, TH2 cells were protected from galectin-1 through differential sialylation of cell surface glycoproteins. Consistent with those findings, galectin-1-deficient mice developed greater TH1 and TH-17 responses and enhanced susceptibility to autoimmune neuroinflammation. Our findings identify a molecular link among differential glycosylation of T helper cells, susceptibility to cell death and termination of the inflammatory response.