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Developmentally regulated glycosylation of the CD8alphabeta coreceptor stalk modulates ligand binding.

Moody, A M and Chui, D and Reche, Pedro A and Priatel, J J and Marth, J D and Reinherz, Ellis L (2001) Developmentally regulated glycosylation of the CD8alphabeta coreceptor stalk modulates ligand binding. Cell, 107 (4). pp. 501-12. ISSN 0092-8674

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Abstract

The functional consequences of glycan structural changes associated with cellular differentiation are ill defined. Herein, we investigate the role of glycan adducts to the O-glycosylated polypeptide stalk tethering the CD8alphabeta coreceptor to the thymocyte surface. We show that immature CD4(+)CD8(+) double-positive thymocytes bind MHCI tetramers more avidly than mature CD8 single-positive thymocytes, and that this differential binding is governed by developmentally programmed O-glycan modification controlled by the ST3Gal-I sialyltransferase. ST3Gal-I induction and attendant core 1 sialic acid addition to CD8beta on mature thymocytes decreases CD8alphabeta-MHCI avidity by altering CD8alphabeta domain-domain association and/or orientation. Hence, glycans on the CD8beta stalk appear to modulate the ability of the distal binding surface of the dimeric CD8 globular head domains to clamp MHCI.


Item Type:Article
Subjects:Medical sciences > Medicine > Immunology
Medical sciences > Biology > Molecular biology
ID Code:9344
Deposited On:14 Aug 2009 10:06
Last Modified:25 Aug 2010 08:24

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