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Analysis of networks of host proteins in the early time points following HIV transduction
BACKGROUND: Utilization of quantitative proteomics data on the network level is still a challenge in proteomics data analysis. Currently existing models use sophisticated, sometimes hard to implement analysis techniques. Our aim was to generate a relatively simple strategy for quantitative proteomic...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6637640/ https://www.ncbi.nlm.nih.gov/pubmed/31315557 http://dx.doi.org/10.1186/s12859-019-2990-3 |
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author | Csősz, Éva Tóth, Ferenc Mahdi, Mohamed Tsaprailis, George Emri, Miklós Tőzsér, József |
author_facet | Csősz, Éva Tóth, Ferenc Mahdi, Mohamed Tsaprailis, George Emri, Miklós Tőzsér, József |
author_sort | Csősz, Éva |
collection | PubMed |
description | BACKGROUND: Utilization of quantitative proteomics data on the network level is still a challenge in proteomics data analysis. Currently existing models use sophisticated, sometimes hard to implement analysis techniques. Our aim was to generate a relatively simple strategy for quantitative proteomics data analysis in order to utilize as much of the data generated in a proteomics experiment as possible. RESULTS: In this study, we applied label-free proteomics, and generated a network model utilizing both qualitative, and quantitative data, in order to examine the early host response to Human Immunodeficiency Virus type 1 (HIV-1). A weighted network model was generated based on the amount of proteins measured by mass spectrometry, and analysis of weighted networks and functional sub-networks revealed upregulation of proteins involved in translation, transcription, and DNA condensation in the early phase of the viral life-cycle. CONCLUSION: A relatively simple strategy for network analysis was created and applied to examine the effect of HIV-1 on host cellular proteome. We believe that our model may prove beneficial in creating algorithms, allowing for both quantitative and qualitative studies of proteome change in various biological and pathological processes by quantitative mass spectrometry. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12859-019-2990-3) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-6637640 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-66376402019-07-29 Analysis of networks of host proteins in the early time points following HIV transduction Csősz, Éva Tóth, Ferenc Mahdi, Mohamed Tsaprailis, George Emri, Miklós Tőzsér, József BMC Bioinformatics Research Article BACKGROUND: Utilization of quantitative proteomics data on the network level is still a challenge in proteomics data analysis. Currently existing models use sophisticated, sometimes hard to implement analysis techniques. Our aim was to generate a relatively simple strategy for quantitative proteomics data analysis in order to utilize as much of the data generated in a proteomics experiment as possible. RESULTS: In this study, we applied label-free proteomics, and generated a network model utilizing both qualitative, and quantitative data, in order to examine the early host response to Human Immunodeficiency Virus type 1 (HIV-1). A weighted network model was generated based on the amount of proteins measured by mass spectrometry, and analysis of weighted networks and functional sub-networks revealed upregulation of proteins involved in translation, transcription, and DNA condensation in the early phase of the viral life-cycle. CONCLUSION: A relatively simple strategy for network analysis was created and applied to examine the effect of HIV-1 on host cellular proteome. We believe that our model may prove beneficial in creating algorithms, allowing for both quantitative and qualitative studies of proteome change in various biological and pathological processes by quantitative mass spectrometry. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12859-019-2990-3) contains supplementary material, which is available to authorized users. BioMed Central 2019-07-17 /pmc/articles/PMC6637640/ /pubmed/31315557 http://dx.doi.org/10.1186/s12859-019-2990-3 Text en © The Author(s). 2019 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Csősz, Éva Tóth, Ferenc Mahdi, Mohamed Tsaprailis, George Emri, Miklós Tőzsér, József Analysis of networks of host proteins in the early time points following HIV transduction |
title | Analysis of networks of host proteins in the early time points following HIV transduction |
title_full | Analysis of networks of host proteins in the early time points following HIV transduction |
title_fullStr | Analysis of networks of host proteins in the early time points following HIV transduction |
title_full_unstemmed | Analysis of networks of host proteins in the early time points following HIV transduction |
title_short | Analysis of networks of host proteins in the early time points following HIV transduction |
title_sort | analysis of networks of host proteins in the early time points following hiv transduction |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6637640/ https://www.ncbi.nlm.nih.gov/pubmed/31315557 http://dx.doi.org/10.1186/s12859-019-2990-3 |
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