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Impact of glycans on T‐cell tolerance to glycosylated self‐antigens
Author(s) -
Purcell Anthony W,
Driel Ian R,
Gleeson Paul A
Publication year - 2008
Publication title -
immunology and cell biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.999
H-Index - 104
eISSN - 1440-1711
pISSN - 0818-9641
DOI - 10.1038/icb.2008.48
Subject(s) - glycan , antigen , glycosylation , immunology , virology , chemistry , biology , glycoprotein , microbiology and biotechnology , genetics
There is now substantial evidence that antigen post‐translational modifications are recognized by T cells, and alterations in epitope modification has been linked to a number of autoimmune diseases. An estimated one third of the MHC ligands contain post‐translational modification of epitopes. A common post‐translational modification of proteins is glycosylation and it is predicted on theoretical grounds that ∼1–5% of MHC ligands may bear a glycan. From numerous studies over the past 15 years it is clear that glycans can influence T cell responses either by contribution to the structure of the epitope or by influencing the profile of peptide epitopes presented by APCs. The influence of glycans on antigen processing and T cell recognition has particular relevance to the induction of tolerance to self‐antigens. Here we discuss the potential impact of glycans on the profile of self‐epitopes presented by APCs and the consequence of changes in glycosylation to generate neo self‐epitopes resulting in the loss of tolerance and the development of autoimmune diseases. With the recent developments in profiling T cell epitopes, and with strategies for modulating glycosylation in vivo , it is now feasible to directly examine the global influence of glycans on self‐tolerance and autoimmunity.