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Critical role of glycosylation in determining the length and structure of T cell epitopes
BACKGROUND: 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 glyco...
Autores principales: | , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2009
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2760507/ https://www.ncbi.nlm.nih.gov/pubmed/19778434 http://dx.doi.org/10.1186/1745-7580-5-4 |
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author | Szabó, Tamás G Palotai, Robin Antal, Péter Tokatly, Itay Tóthfalusi, László Lund, Ole Nagy, György Falus, András Buzás, Edit I |
author_facet | Szabó, Tamás G Palotai, Robin Antal, Péter Tokatly, Itay Tóthfalusi, László Lund, Ole Nagy, György Falus, András Buzás, Edit I |
author_sort | Szabó, Tamás G |
collection | PubMed |
description | BACKGROUND: 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. RESULTS: 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. CONCLUSION: 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. |
format | Text |
id | pubmed-2760507 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-27605072009-10-13 Critical role of glycosylation in determining the length and structure of T cell epitopes Szabó, Tamás G Palotai, Robin Antal, Péter Tokatly, Itay Tóthfalusi, László Lund, Ole Nagy, György Falus, András Buzás, Edit I Immunome Res Research BACKGROUND: 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. RESULTS: 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. CONCLUSION: 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. BioMed Central 2009-09-24 /pmc/articles/PMC2760507/ /pubmed/19778434 http://dx.doi.org/10.1186/1745-7580-5-4 Text en Copyright ©2009 Szabó et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Szabó, Tamás G Palotai, Robin Antal, Péter Tokatly, Itay Tóthfalusi, László Lund, Ole Nagy, György Falus, András Buzás, Edit I Critical role of glycosylation in determining the length and structure of T cell epitopes |
title | Critical role of glycosylation in determining the length and structure of T cell epitopes |
title_full | Critical role of glycosylation in determining the length and structure of T cell epitopes |
title_fullStr | Critical role of glycosylation in determining the length and structure of T cell epitopes |
title_full_unstemmed | Critical role of glycosylation in determining the length and structure of T cell epitopes |
title_short | Critical role of glycosylation in determining the length and structure of T cell epitopes |
title_sort | critical role of glycosylation in determining the length and structure of t cell epitopes |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2760507/ https://www.ncbi.nlm.nih.gov/pubmed/19778434 http://dx.doi.org/10.1186/1745-7580-5-4 |
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