Abstract
BackgroundUsing 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.ResultsWe 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.ConclusionThe 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.
Highlights
Using a combined in silico approach, we investigated the glycosylation of T cell epitopes and autoantigens
Our data suggest that amino acid sequencebased hypo/non-glycosylation of certain segments of proteins might be substantial for determining T cell immunity/autoimmunity
Glycosylation of the human proteome In order to generate a basis for comparison with antigens and antigen-derived T cell epitopes, we set to assess the glycosylation of the human proteome based on sequence analysis of entries extracted from SwissProt/UniProtKB
Summary
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. Antigen recognition by the immune system is decisive in the fight against pathogens and tumors. T lymphocytes recognize short, linear peptide fragments (epitopes) of antigenic proteins in context with self MHC. The significance of the posttranslationally modified antigenic determinants in shaping the receptor repertoire and determining the outcome of an immune response, is poorly understood. Despite the extensive work, fundamental questions (such as the role of epitope glycosylation in T cell recognition) remain to be answered
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