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Proposing Low-Similarity Peptide Vaccines against Mycobacterium tuberculosis
Using the currently available proteome databases and based on the concept that a rare sequence is a potential epitope, epitopic sequences derived from Mycobacterium tuberculosis were examined for similarity score to the proteins of the host in which the epitopes were defined. We found that: (i) most...
Autores principales: | , , |
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Formato: | Texto |
Lenguaje: | English |
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Hindawi Publishing Corporation
2010
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2896900/ https://www.ncbi.nlm.nih.gov/pubmed/20625421 http://dx.doi.org/10.1155/2010/832341 |
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author | Lucchese, Guglielmo Stufano, Angela Kanduc, Darja |
author_facet | Lucchese, Guglielmo Stufano, Angela Kanduc, Darja |
author_sort | Lucchese, Guglielmo |
collection | PubMed |
description | Using the currently available proteome databases and based on the concept that a rare sequence is a potential epitope, epitopic sequences derived from Mycobacterium tuberculosis were examined for similarity score to the proteins of the host in which the epitopes were defined. We found that: (i) most of the bacterial linear determinants had peptide fragment(s) that were rarely found in the host proteins and (ii) the relationship between low similarity and epitope definition appears potentially applicable to T-cell determinants. The data confirmed the hypothesis that low-sequence similarity shapes or determines the epitope definition at the molecular level and provides a potential tool for designing new approaches to prevent, diagnose, and treat tuberculosis and other infectious diseases. |
format | Text |
id | pubmed-2896900 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-28969002010-07-12 Proposing Low-Similarity Peptide Vaccines against Mycobacterium tuberculosis Lucchese, Guglielmo Stufano, Angela Kanduc, Darja J Biomed Biotechnol Methodology Report Using the currently available proteome databases and based on the concept that a rare sequence is a potential epitope, epitopic sequences derived from Mycobacterium tuberculosis were examined for similarity score to the proteins of the host in which the epitopes were defined. We found that: (i) most of the bacterial linear determinants had peptide fragment(s) that were rarely found in the host proteins and (ii) the relationship between low similarity and epitope definition appears potentially applicable to T-cell determinants. The data confirmed the hypothesis that low-sequence similarity shapes or determines the epitope definition at the molecular level and provides a potential tool for designing new approaches to prevent, diagnose, and treat tuberculosis and other infectious diseases. Hindawi Publishing Corporation 2010 2010-06-03 /pmc/articles/PMC2896900/ /pubmed/20625421 http://dx.doi.org/10.1155/2010/832341 Text en Copyright © 2010 Guglielmo Lucchese et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Methodology Report Lucchese, Guglielmo Stufano, Angela Kanduc, Darja Proposing Low-Similarity Peptide Vaccines against Mycobacterium tuberculosis |
title | Proposing Low-Similarity Peptide Vaccines against Mycobacterium tuberculosis |
title_full | Proposing Low-Similarity Peptide Vaccines against Mycobacterium tuberculosis |
title_fullStr | Proposing Low-Similarity Peptide Vaccines against Mycobacterium tuberculosis |
title_full_unstemmed | Proposing Low-Similarity Peptide Vaccines against Mycobacterium tuberculosis |
title_short | Proposing Low-Similarity Peptide Vaccines against Mycobacterium tuberculosis |
title_sort | proposing low-similarity peptide vaccines against mycobacterium tuberculosis |
topic | Methodology Report |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2896900/ https://www.ncbi.nlm.nih.gov/pubmed/20625421 http://dx.doi.org/10.1155/2010/832341 |
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