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Glycobiology Advance Access published online on April 5, 2006
Glycobiology, doi:10.1093/glycob/cwj111
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© The Author 2006. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org
Received March 3, 2006
Revised March 27, 2006
Accepted March 27, 2006

Review Article

T cell recognition of glycolipids presented by CD1 proteins

David C. Young 1 * and D. Branch Moody 1 *

1 Division of Rheumatology, Immunology and Allergy Brigham and Women’s Hospital and Harvard Medical School Smith Building Rm 514 1 Jimmy Fund Way Boston, MA 02115, USA

* To whom correspondence should be addressed.
David C. Young, E-mail: dyoung{at}rics.bwh.harvard.edu
D. Branch Moody, E-mail: bmoody{at}rics.bwh.harvard.edu


  Abstract

The most well known molecular paradigm of antigen recognition by T cells involves partial digestion of proteins to generate small peptides, which bind to major histocompatibility complex (MHC) proteins. Recent studies of CD1, an MHC class I homolog encoded outside the MHC, have revealed that it presents diverse glycolipids to T cells. The molecular mechanism for lipid antigen recognition involves insertion of the lipid portion of antigens into a hydrophobic groove to form CD1-lipid complexes, which contact T cell receptors. Here we examine the known antigen structures presented by CD1, the majority of which have sugar moieties that are capable of interacting with T cell receptors. Recognition of carbohydrate epitopes is precise, and lipid-reactive T cells alter systemic immune responses in models of infectious and autoimmune disease. These findings provide a previously unrecognized mechanism by which cellular immunity can include recognition and response to alterations in many types of carbohydrate structures.

Keywords: glycolipid antigens/lipid antigens/T cells/NK T cells/alpha galactosyl ceramide.
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