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Critical role of glycosylation in determining the length and structure of T cell epitopes

Tamás G Szabó1, Robin Palotai2, Péter Antal3, Itay Tokatly1, László Tóthfalusi4, Ole Lund5, György Nagy16, András Falus17 and Edit I Buzás1*

Author Affiliations

1 Department of Genetics, Cell- and Immunobiology, Semmelweis University, Nagyvárad tér 4, Budapest, Hungary

2 Department of Medical Chemistry, Molecular Biology and Pathobiochemistry, Semmelweis University, Budapest, 1094 Budapest, Tűzoltó u 37-47, Hungary

3 Department of Measurement and Information Systems, Budapest University of Technology and Economics, Budapest, Pf 91, 1521 Budapest, Hungary

4 Department of Pharmacodynamics, Semmelweis University, Nagyvárad tér 4, 1089 Budapest, Hungary

5 Center for Biological Sequence Analysis, Department of Systems Biology, Technical University of Denmark, Building 208, DK-2800 Kongens Lyngby, Denmark

6 Department of Rheumatology, Semmelweis University, Árpád fejedelem u 7, 1022 Budapest, Hungary

7 Research Group for Inflammation Biology and Immunogenomics, Hungarian Academy of Sciences, Nagyvárad tér 4, 1089 Budapest, Hungary

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Immunome Research 2009, 5:4  doi:10.1186/1745-7580-5-4

Published: 24 September 2009



Using a combined in silico approach, we investigated the glycosylation of T cell epitopes and autoantigens. The present systems biology analysis was made possible by currently available databases (representing full proteomes, known human T cell epitopes and autoantigens) as well as glycosylation prediction tools.


We analyzed the probable glycosylation of human T cell epitope sequences extracted from the ImmuneEpitope Database. Our analysis suggests that in contrast to full length SwissProt entries, only a minimal portion of experimentally verified T cell epitopes is potentially N- or O-glycosylated (2.26% and 1.22%, respectively). Bayesian analysis of entries extracted from the Autoantigen Database suggests a correlation between N-glycosylation and autoantigenicity. The analysis of random generated sequences shows that glycosylation probability is also affected by peptide length. Our data suggest that the lack of peptide glycosylation, a feature that probably favors effective recognition by T cells, might have resulted in a selective advantage for short peptides to become T cell epitopes. The length of T cell epitopes is at the intersection of curves determining specificity and glycosylation probability. Thus, the range of length of naturally occurring T cell epitopes may ensure the maximum specificity with the minimal glycosylation probability.


The findings of this bioinformatical approach shed light on fundamental factors that might have shaped adaptive immunity during evolution. Our data suggest that amino acid sequence-based hypo/non-glycosylation of certain segments of proteins might be substantial for determining T cell immunity/autoimmunity.