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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...

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Autores principales: Surmann, Kristin, Simon, Marjolaine, Hildebrandt, Petra, Pförtner, Henrike, Michalik, Stephan, Dhople, Vishnu M., Bröker, Barbara M., Schmidt, Frank, Völker, Uwe
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2016
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.
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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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