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Quasi-prime peptides: identification of the shortest peptide sequences unique to a species
Determining the organisms present in a biosample has many important applications in agriculture, wildlife conservation, and healthcare. Here, we develop a universal fingerprint based on the identification of short peptides that are unique to a specific organism. We define quasi-prime peptides as seq...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10124967/ https://www.ncbi.nlm.nih.gov/pubmed/37101657 http://dx.doi.org/10.1093/nargab/lqad039 |
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author | Mouratidis, Ioannis Chan, Candace S Y Chantzi, Nikol Tsiatsianis, Georgios Christos Hemberg, Martin Ahituv, Nadav Georgakopoulos-Soares, Ilias |
author_facet | Mouratidis, Ioannis Chan, Candace S Y Chantzi, Nikol Tsiatsianis, Georgios Christos Hemberg, Martin Ahituv, Nadav Georgakopoulos-Soares, Ilias |
author_sort | Mouratidis, Ioannis |
collection | PubMed |
description | Determining the organisms present in a biosample has many important applications in agriculture, wildlife conservation, and healthcare. Here, we develop a universal fingerprint based on the identification of short peptides that are unique to a specific organism. We define quasi-prime peptides as sequences that are found in only one species, and we analyzed proteomes from 21 875 species, from viruses to humans, and annotated the smallest peptide kmer sequences that are unique to a species and absent from all other proteomes. We also perform simulations across all reference proteomes and observe a lower than expected number of peptide kmers across species and taxonomies, indicating an enrichment for nullpeptides, sequences absent from a proteome. For humans, we find that quasi-primes are found in genes enriched for specific gene ontology terms, including proteasome and ATP and GTP catalysis. We also provide a set of quasi-prime peptides for a number of human pathogens and model organisms and further showcase its utility via two case studies for Mycobacterium tuberculosis and Vibrio cholerae, where we identify quasi-prime peptides in two transmembrane and extracellular proteins with relevance for pathogen detection. Our catalog of quasi-prime peptides provides the smallest unit of information that is specific to a single organism at the protein level, providing a versatile tool for species identification. |
format | Online Article Text |
id | pubmed-10124967 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-101249672023-04-25 Quasi-prime peptides: identification of the shortest peptide sequences unique to a species Mouratidis, Ioannis Chan, Candace S Y Chantzi, Nikol Tsiatsianis, Georgios Christos Hemberg, Martin Ahituv, Nadav Georgakopoulos-Soares, Ilias NAR Genom Bioinform Standard Article Determining the organisms present in a biosample has many important applications in agriculture, wildlife conservation, and healthcare. Here, we develop a universal fingerprint based on the identification of short peptides that are unique to a specific organism. We define quasi-prime peptides as sequences that are found in only one species, and we analyzed proteomes from 21 875 species, from viruses to humans, and annotated the smallest peptide kmer sequences that are unique to a species and absent from all other proteomes. We also perform simulations across all reference proteomes and observe a lower than expected number of peptide kmers across species and taxonomies, indicating an enrichment for nullpeptides, sequences absent from a proteome. For humans, we find that quasi-primes are found in genes enriched for specific gene ontology terms, including proteasome and ATP and GTP catalysis. We also provide a set of quasi-prime peptides for a number of human pathogens and model organisms and further showcase its utility via two case studies for Mycobacterium tuberculosis and Vibrio cholerae, where we identify quasi-prime peptides in two transmembrane and extracellular proteins with relevance for pathogen detection. Our catalog of quasi-prime peptides provides the smallest unit of information that is specific to a single organism at the protein level, providing a versatile tool for species identification. Oxford University Press 2023-04-24 /pmc/articles/PMC10124967/ /pubmed/37101657 http://dx.doi.org/10.1093/nargab/lqad039 Text en © The Author(s) 2023. Published by Oxford University Press on behalf of NAR Genomics and Bioinformatics. https://creativecommons.org/licenses/by-nc/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (https://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Standard Article Mouratidis, Ioannis Chan, Candace S Y Chantzi, Nikol Tsiatsianis, Georgios Christos Hemberg, Martin Ahituv, Nadav Georgakopoulos-Soares, Ilias Quasi-prime peptides: identification of the shortest peptide sequences unique to a species |
title | Quasi-prime peptides: identification of the shortest peptide sequences unique to a species |
title_full | Quasi-prime peptides: identification of the shortest peptide sequences unique to a species |
title_fullStr | Quasi-prime peptides: identification of the shortest peptide sequences unique to a species |
title_full_unstemmed | Quasi-prime peptides: identification of the shortest peptide sequences unique to a species |
title_short | Quasi-prime peptides: identification of the shortest peptide sequences unique to a species |
title_sort | quasi-prime peptides: identification of the shortest peptide sequences unique to a species |
topic | Standard Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10124967/ https://www.ncbi.nlm.nih.gov/pubmed/37101657 http://dx.doi.org/10.1093/nargab/lqad039 |
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