A predictive model for vertebrate bone identification from collagen using proteomic mass spectrometry

Abstract Proteogenomics is an increasingly common method for species identification as it allows for rapid and inexpensive interrogation of an unknown organism’s proteome—even when the proteome is partially degraded. The proteomic method typically uses tandem mass spectrometry to survey all peptides...

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Autores principales:	Heyi Yang, Erin R. Butler, Samantha A. Monier, Jennifer Teubl, David Fenyö, Beatrix Ueberheide, Donald Siegel
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/f72890fc2a914052b3c97c1744bba3b2
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spelling	oai:doaj.org-article:f72890fc2a914052b3c97c1744bba3b22021-12-02T15:00:25ZA predictive model for vertebrate bone identification from collagen using proteomic mass spectrometry10.1038/s41598-021-90231-52045-2322https://doaj.org/article/f72890fc2a914052b3c97c1744bba3b22021-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-90231-5https://doaj.org/toc/2045-2322Abstract Proteogenomics is an increasingly common method for species identification as it allows for rapid and inexpensive interrogation of an unknown organism’s proteome—even when the proteome is partially degraded. The proteomic method typically uses tandem mass spectrometry to survey all peptides detectable in a sample that frequently contains hundreds or thousands of proteins. Species identification is based on detection of a small numbers of species-specific peptides. Genetic analysis of proteins by mass spectrometry, however, is a developing field, and the bone proteome, typically consisting of only two proteins, pushes the limits of this technology. Nearly 20% of highly confident spectra from modern human bone samples identify non-human species when searched against a vertebrate database—as would be necessary with a fragment of unknown bone. These non-human peptides are often the result of current limitations in mass spectrometry or algorithm interpretation errors. Consequently, it is difficult to know if a “species-specific” peptide used to identify a sample is actually present in that sample. Here we evaluate the causes of peptide sequence errors and propose an unbiased, probabilistic approach to determine the likelihood that a species is correctly identified from bone without relying on species-specific peptides.Heyi YangErin R. ButlerSamantha A. MonierJennifer TeublDavid FenyöBeatrix UeberheideDonald SiegelNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Heyi Yang Erin R. Butler Samantha A. Monier Jennifer Teubl David Fenyö Beatrix Ueberheide Donald Siegel A predictive model for vertebrate bone identification from collagen using proteomic mass spectrometry
description	Abstract Proteogenomics is an increasingly common method for species identification as it allows for rapid and inexpensive interrogation of an unknown organism’s proteome—even when the proteome is partially degraded. The proteomic method typically uses tandem mass spectrometry to survey all peptides detectable in a sample that frequently contains hundreds or thousands of proteins. Species identification is based on detection of a small numbers of species-specific peptides. Genetic analysis of proteins by mass spectrometry, however, is a developing field, and the bone proteome, typically consisting of only two proteins, pushes the limits of this technology. Nearly 20% of highly confident spectra from modern human bone samples identify non-human species when searched against a vertebrate database—as would be necessary with a fragment of unknown bone. These non-human peptides are often the result of current limitations in mass spectrometry or algorithm interpretation errors. Consequently, it is difficult to know if a “species-specific” peptide used to identify a sample is actually present in that sample. Here we evaluate the causes of peptide sequence errors and propose an unbiased, probabilistic approach to determine the likelihood that a species is correctly identified from bone without relying on species-specific peptides.
format	article
author	Heyi Yang Erin R. Butler Samantha A. Monier Jennifer Teubl David Fenyö Beatrix Ueberheide Donald Siegel
author_facet	Heyi Yang Erin R. Butler Samantha A. Monier Jennifer Teubl David Fenyö Beatrix Ueberheide Donald Siegel
author_sort	Heyi Yang
title	A predictive model for vertebrate bone identification from collagen using proteomic mass spectrometry
title_short	A predictive model for vertebrate bone identification from collagen using proteomic mass spectrometry
title_full	A predictive model for vertebrate bone identification from collagen using proteomic mass spectrometry
title_fullStr	A predictive model for vertebrate bone identification from collagen using proteomic mass spectrometry
title_full_unstemmed	A predictive model for vertebrate bone identification from collagen using proteomic mass spectrometry
title_sort	predictive model for vertebrate bone identification from collagen using proteomic mass spectrometry
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/f72890fc2a914052b3c97c1744bba3b2
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A predictive model for vertebrate bone identification from collagen using proteomic mass spectrometry

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