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PVS: a web server for protein sequence variability analysis tuned to facilitate conserved epitope discovery
We have developed PVS (Protein Variability Server), a web-based tool that uses several variability metrics to compute the absolute site variability in multiple protein-sequence alignments (MSAs). The variability is then assigned to a user-selected reference sequence consisting of either the first se...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2008
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2447719/ https://www.ncbi.nlm.nih.gov/pubmed/18442995 http://dx.doi.org/10.1093/nar/gkn211 |
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author | Garcia-Boronat, Maria Diez-Rivero, Carmen M. Reinherz, Ellis L. Reche, Pedro A. |
author_facet | Garcia-Boronat, Maria Diez-Rivero, Carmen M. Reinherz, Ellis L. Reche, Pedro A. |
author_sort | Garcia-Boronat, Maria |
collection | PubMed |
description | We have developed PVS (Protein Variability Server), a web-based tool that uses several variability metrics to compute the absolute site variability in multiple protein-sequence alignments (MSAs). The variability is then assigned to a user-selected reference sequence consisting of either the first sequence in the alignment or a consensus sequence. Subsequently, PVS performs tasks that are relevant for structure-function studies, such as plotting and visualizing the variability in a relevant 3D-structure. Neatly, PVS also implements some other tasks that are thought to facilitate the design of epitope discovery-driven vaccines against pathogens where sequence variability largely contributes to immune evasion. Thus, PVS can return the conserved fragments in the MSA—as defined by a user-provided variability threshold—and locate them in a relevant 3D-structure. Furthermore, PVS can return a variability-masked sequence, which can be directly submitted to the RANKPEP server for the prediction of conserved T-cell epitopes. PVS is freely available at: http://imed.med.ucm.es/PVS/. |
format | Text |
id | pubmed-2447719 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-24477192008-07-09 PVS: a web server for protein sequence variability analysis tuned to facilitate conserved epitope discovery Garcia-Boronat, Maria Diez-Rivero, Carmen M. Reinherz, Ellis L. Reche, Pedro A. Nucleic Acids Res Articles We have developed PVS (Protein Variability Server), a web-based tool that uses several variability metrics to compute the absolute site variability in multiple protein-sequence alignments (MSAs). The variability is then assigned to a user-selected reference sequence consisting of either the first sequence in the alignment or a consensus sequence. Subsequently, PVS performs tasks that are relevant for structure-function studies, such as plotting and visualizing the variability in a relevant 3D-structure. Neatly, PVS also implements some other tasks that are thought to facilitate the design of epitope discovery-driven vaccines against pathogens where sequence variability largely contributes to immune evasion. Thus, PVS can return the conserved fragments in the MSA—as defined by a user-provided variability threshold—and locate them in a relevant 3D-structure. Furthermore, PVS can return a variability-masked sequence, which can be directly submitted to the RANKPEP server for the prediction of conserved T-cell epitopes. PVS is freely available at: http://imed.med.ucm.es/PVS/. Oxford University Press 2008-07-01 2008-04-27 /pmc/articles/PMC2447719/ /pubmed/18442995 http://dx.doi.org/10.1093/nar/gkn211 Text en © 2008 The Author(s) http://creativecommons.org/licenses/by-nc/2.0/uk/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Articles Garcia-Boronat, Maria Diez-Rivero, Carmen M. Reinherz, Ellis L. Reche, Pedro A. PVS: a web server for protein sequence variability analysis tuned to facilitate conserved epitope discovery |
title | PVS: a web server for protein sequence variability analysis tuned to facilitate conserved epitope discovery |
title_full | PVS: a web server for protein sequence variability analysis tuned to facilitate conserved epitope discovery |
title_fullStr | PVS: a web server for protein sequence variability analysis tuned to facilitate conserved epitope discovery |
title_full_unstemmed | PVS: a web server for protein sequence variability analysis tuned to facilitate conserved epitope discovery |
title_short | PVS: a web server for protein sequence variability analysis tuned to facilitate conserved epitope discovery |
title_sort | pvs: a web server for protein sequence variability analysis tuned to facilitate conserved epitope discovery |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2447719/ https://www.ncbi.nlm.nih.gov/pubmed/18442995 http://dx.doi.org/10.1093/nar/gkn211 |
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