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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...

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Autores principales: Szabó, Tamás G, Palotai, Robin, Antal, Péter, Tokatly, Itay, Tóthfalusi, László, Lund, Ole, Nagy, György, Falus, András, Buzás, Edit I
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2009
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.
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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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