Sialic acid capping of CD8β core 1-O-glycans controls thymocyte-major histocompatibility complex class I interaction

Anne Marie Moody, Simon J. North, Bruce Reinhold, Steven J. Van Dyken, Mark E. Rogers, Maria Panico, Anne Dell, Howard R. Morris, Jamey D. Marth, Ellis L. Reinherz

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66 Scopus citations

Abstract

Bidentate interaction of a T-cell receptor and CD8αβ heterodimer with a peptide-MHCI complex is required for the generation of cytotoxic T-lymphocytes. During thymic development, the modification of CD813 glycans influences major histocompatibility complex class I binding to T-cell precursors called thymocytes. ES mass spectrometry (MS) and tandem MS/MS analysis were used to identify the changes occurring in the CD8β-glycopeptides during T-cell development. Several threonine residues proximal to the CD8β Ig headpiece are glycosylated with core-type 1 O-glycans. Non-sialylated glycoforms are present in immature thymocytes but are virtually absent in mature thymocytes. These results suggest how sialylation in a discrete segment of the CD8β stalk by ST3Gal-1 sialyltransferase creates a molecular developmental switch that affects ligand binding.

Original languageEnglish
Pages (from-to)7240-7246
Number of pages7
JournalJournal of Biological Chemistry
Volume278
Issue number9
DOIs
StatePublished - Feb 28 2003
Externally publishedYes

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    Moody, A. M., North, S. J., Reinhold, B., Van Dyken, S. J., Rogers, M. E., Panico, M., Dell, A., Morris, H. R., Marth, J. D., & Reinherz, E. L. (2003). Sialic acid capping of CD8β core 1-O-glycans controls thymocyte-major histocompatibility complex class I interaction. Journal of Biological Chemistry, 278(9), 7240-7246. https://doi.org/10.1074/jbc.M210468200