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P2P proteomics -- data sharing for enhanced protein identification

BACKGROUND: In order to tackle the important and challenging problem in proteomics of identifying known and new protein sequences using high-throughput methods, we propose a data-sharing platform that uses fully distributed P2P technologies to share specifications of peer-interaction protocols and s...

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Autores principales: Schorlemmer, Marco, Abián, Joaquín, Sierra, Carles, de la Cruz, David, Bernacchioni, Lorenzo, Jaén, Enric, Perreau de Pinninck, Adrian, Atencia, Manuel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3298698/
https://www.ncbi.nlm.nih.gov/pubmed/22293032
http://dx.doi.org/10.1186/1759-4499-4-1
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author Schorlemmer, Marco
Abián, Joaquín
Sierra, Carles
de la Cruz, David
Bernacchioni, Lorenzo
Jaén, Enric
Perreau de Pinninck, Adrian
Atencia, Manuel
author_facet Schorlemmer, Marco
Abián, Joaquín
Sierra, Carles
de la Cruz, David
Bernacchioni, Lorenzo
Jaén, Enric
Perreau de Pinninck, Adrian
Atencia, Manuel
author_sort Schorlemmer, Marco
collection PubMed
description BACKGROUND: In order to tackle the important and challenging problem in proteomics of identifying known and new protein sequences using high-throughput methods, we propose a data-sharing platform that uses fully distributed P2P technologies to share specifications of peer-interaction protocols and service components. By using such a platform, information to be searched is no longer centralised in a few repositories but gathered from experiments in peer proteomics laboratories, which can subsequently be searched by fellow researchers. METHODS: The system distributively runs a data-sharing protocol specified in the Lightweight Communication Calculus underlying the system through which researchers interact via message passing. For this, researchers interact with the system through particular components that link to database querying systems based on BLAST and/or OMSSA and GUI-based visualisation environments. We have tested the proposed platform with data drawn from preexisting MS/MS data reservoirs from the 2006 ABRF (Association of Biomolecular Resource Facilities) test sample, which was extensively tested during the ABRF Proteomics Standards Research Group 2006 worldwide survey. In particular we have taken the data available from a subset of proteomics laboratories of Spain's National Institute for Proteomics, ProteoRed, a network for the coordination, integration and development of the Spanish proteomics facilities. RESULTS AND DISCUSSION: We performed queries against nine databases including seven ProteoRed proteomics laboratories, the NCBI Swiss-Prot database and the local database of the CSIC/UAB Proteomics Laboratory. A detailed analysis of the results indicated the presence of a protein that was supported by other NCBI matches and highly scored matches in several proteomics labs. The analysis clearly indicated that the protein was a relatively high concentrated contaminant that could be present in the ABRF sample. This fact is evident from the information that could be derived from the proposed P2P proteomics system, however it is not straightforward to arrive to the same conclusion by conventional means as it is difficult to discard organic contamination of samples. The actual presence of this contaminant was only stated after the ABRF study of all the identifications reported by the laboratories.
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spelling pubmed-32986982012-03-12 P2P proteomics -- data sharing for enhanced protein identification Schorlemmer, Marco Abián, Joaquín Sierra, Carles de la Cruz, David Bernacchioni, Lorenzo Jaén, Enric Perreau de Pinninck, Adrian Atencia, Manuel Autom Exp Research BACKGROUND: In order to tackle the important and challenging problem in proteomics of identifying known and new protein sequences using high-throughput methods, we propose a data-sharing platform that uses fully distributed P2P technologies to share specifications of peer-interaction protocols and service components. By using such a platform, information to be searched is no longer centralised in a few repositories but gathered from experiments in peer proteomics laboratories, which can subsequently be searched by fellow researchers. METHODS: The system distributively runs a data-sharing protocol specified in the Lightweight Communication Calculus underlying the system through which researchers interact via message passing. For this, researchers interact with the system through particular components that link to database querying systems based on BLAST and/or OMSSA and GUI-based visualisation environments. We have tested the proposed platform with data drawn from preexisting MS/MS data reservoirs from the 2006 ABRF (Association of Biomolecular Resource Facilities) test sample, which was extensively tested during the ABRF Proteomics Standards Research Group 2006 worldwide survey. In particular we have taken the data available from a subset of proteomics laboratories of Spain's National Institute for Proteomics, ProteoRed, a network for the coordination, integration and development of the Spanish proteomics facilities. RESULTS AND DISCUSSION: We performed queries against nine databases including seven ProteoRed proteomics laboratories, the NCBI Swiss-Prot database and the local database of the CSIC/UAB Proteomics Laboratory. A detailed analysis of the results indicated the presence of a protein that was supported by other NCBI matches and highly scored matches in several proteomics labs. The analysis clearly indicated that the protein was a relatively high concentrated contaminant that could be present in the ABRF sample. This fact is evident from the information that could be derived from the proposed P2P proteomics system, however it is not straightforward to arrive to the same conclusion by conventional means as it is difficult to discard organic contamination of samples. The actual presence of this contaminant was only stated after the ABRF study of all the identifications reported by the laboratories. BioMed Central 2012-01-31 /pmc/articles/PMC3298698/ /pubmed/22293032 http://dx.doi.org/10.1186/1759-4499-4-1 Text en Copyright ©2012 Schorlemmer 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
Schorlemmer, Marco
Abián, Joaquín
Sierra, Carles
de la Cruz, David
Bernacchioni, Lorenzo
Jaén, Enric
Perreau de Pinninck, Adrian
Atencia, Manuel
P2P proteomics -- data sharing for enhanced protein identification
title P2P proteomics -- data sharing for enhanced protein identification
title_full P2P proteomics -- data sharing for enhanced protein identification
title_fullStr P2P proteomics -- data sharing for enhanced protein identification
title_full_unstemmed P2P proteomics -- data sharing for enhanced protein identification
title_short P2P proteomics -- data sharing for enhanced protein identification
title_sort p2p proteomics -- data sharing for enhanced protein identification
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3298698/
https://www.ncbi.nlm.nih.gov/pubmed/22293032
http://dx.doi.org/10.1186/1759-4499-4-1
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