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Proteome data from a host-pathogen interaction study with Staphylococcus aureus and human lung epithelial cells
To simultaneously obtain proteome data of host and pathogen from an internalization experiment, human alveolar epithelial A549 cells were infected with Staphylococcus aureus HG001 which carried a plasmid (pMV158GFP) encoding a continuously expressed green fluorescent protein (GFP). Samples were take...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5063755/ https://www.ncbi.nlm.nih.gov/pubmed/27761493 http://dx.doi.org/10.1016/j.dib.2016.03.027 |
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author | Surmann, Kristin Simon, Marjolaine Hildebrandt, Petra Pförtner, Henrike Michalik, Stephan Dhople, Vishnu M. Bröker, Barbara M. Schmidt, Frank Völker, Uwe |
author_facet | Surmann, Kristin Simon, Marjolaine Hildebrandt, Petra Pförtner, Henrike Michalik, Stephan Dhople, Vishnu M. Bröker, Barbara M. Schmidt, Frank Völker, Uwe |
author_sort | Surmann, Kristin |
collection | PubMed |
description | To simultaneously obtain proteome data of host and pathogen from an internalization experiment, human alveolar epithelial A549 cells were infected with Staphylococcus aureus HG001 which carried a plasmid (pMV158GFP) encoding a continuously expressed green fluorescent protein (GFP). Samples were taken hourly between 1.5 h and 6.5 h post infection. By fluorescence activated cell sorting GFP-expressing bacteria could be enriched from host cell debris, but also infected host cells could be separated from those which did not carry bacteria after contact (exposed). Additionally, proteome data of A549 cells which were not exposed to S. aureus but underwent the same sample processing steps are provided as a control. Time-resolved changes in bacterial protein abundance were quantified in a label-free approach. Proteome adaptations of host cells were monitored by comparative analysis to a stable isotope labeled cell culture (SILAC) standard. Proteins were extracted from the cells, digested proteolytically, measured by nanoLC–MS/MS, and subsequently identified by database search and then quantified. The data presented here are related to a previously published research article describing the interplay of S. aureus HG001 and human epithelial cells (Surmann et al., 2015 [1]). They have been deposited to the ProteomeXchange platform with the identifiers PRIDE: http://www.ebi.ac.uk/pride/archive/projects/PXD002384 for the S. aureus HG001 proteome dataset and PRIDE: http://www.ebi.ac.uk/pride/archive/projects/PXD002388 for the A549 proteome dataset. |
format | Online Article Text |
id | pubmed-5063755 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-50637552016-10-19 Proteome data from a host-pathogen interaction study with Staphylococcus aureus and human lung epithelial cells Surmann, Kristin Simon, Marjolaine Hildebrandt, Petra Pförtner, Henrike Michalik, Stephan Dhople, Vishnu M. Bröker, Barbara M. Schmidt, Frank Völker, Uwe Data Brief Data Article To simultaneously obtain proteome data of host and pathogen from an internalization experiment, human alveolar epithelial A549 cells were infected with Staphylococcus aureus HG001 which carried a plasmid (pMV158GFP) encoding a continuously expressed green fluorescent protein (GFP). Samples were taken hourly between 1.5 h and 6.5 h post infection. By fluorescence activated cell sorting GFP-expressing bacteria could be enriched from host cell debris, but also infected host cells could be separated from those which did not carry bacteria after contact (exposed). Additionally, proteome data of A549 cells which were not exposed to S. aureus but underwent the same sample processing steps are provided as a control. Time-resolved changes in bacterial protein abundance were quantified in a label-free approach. Proteome adaptations of host cells were monitored by comparative analysis to a stable isotope labeled cell culture (SILAC) standard. Proteins were extracted from the cells, digested proteolytically, measured by nanoLC–MS/MS, and subsequently identified by database search and then quantified. The data presented here are related to a previously published research article describing the interplay of S. aureus HG001 and human epithelial cells (Surmann et al., 2015 [1]). They have been deposited to the ProteomeXchange platform with the identifiers PRIDE: http://www.ebi.ac.uk/pride/archive/projects/PXD002384 for the S. aureus HG001 proteome dataset and PRIDE: http://www.ebi.ac.uk/pride/archive/projects/PXD002388 for the A549 proteome dataset. Elsevier 2016-03-19 /pmc/articles/PMC5063755/ /pubmed/27761493 http://dx.doi.org/10.1016/j.dib.2016.03.027 Text en © 2016 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Data Article Surmann, Kristin Simon, Marjolaine Hildebrandt, Petra Pförtner, Henrike Michalik, Stephan Dhople, Vishnu M. Bröker, Barbara M. Schmidt, Frank Völker, Uwe Proteome data from a host-pathogen interaction study with Staphylococcus aureus and human lung epithelial cells |
title | Proteome data from a host-pathogen interaction study with Staphylococcus aureus and human lung epithelial cells |
title_full | Proteome data from a host-pathogen interaction study with Staphylococcus aureus and human lung epithelial cells |
title_fullStr | Proteome data from a host-pathogen interaction study with Staphylococcus aureus and human lung epithelial cells |
title_full_unstemmed | Proteome data from a host-pathogen interaction study with Staphylococcus aureus and human lung epithelial cells |
title_short | Proteome data from a host-pathogen interaction study with Staphylococcus aureus and human lung epithelial cells |
title_sort | proteome data from a host-pathogen interaction study with staphylococcus aureus and human lung epithelial cells |
topic | Data Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5063755/ https://www.ncbi.nlm.nih.gov/pubmed/27761493 http://dx.doi.org/10.1016/j.dib.2016.03.027 |
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