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Updated: Mar 13, 2026
Label-Free Quantitative Proteomics Workflow for Discovery-Driven Host-Pathogen Interactions
Published on: October 20, 2020
Proteome data from a host-pathogen interaction study with Staphylococcus aureus and human lung epithelial cells.
Kristin Surmann1, Marjolaine Simon2, Petra Hildebrandt1
1Interfaculty Institute for Genetics and Functional Genomics, University Medicine Greifswald, Friedrich-Ludwig-Jahn-Str. 15a, 17475 Greifswald, Germany; ZIK-FunGene Junior Research Group Applied Proteomics, University Medicine Greifswald, Friedrich-Ludwig-Jahn-Str. 15a, 17475 Greifswald, Germany.
This study quantifies bacterial and host cell proteome changes during Staphylococcus aureus infection of human lung cells. It details time-resolved protein adaptations in both pathogen and host using advanced mass spectrometry techniques.
Area of Science:
- Microbiology
- Proteomics
- Cell Biology
Background:
- Investigating host-pathogen interactions is crucial for understanding infectious diseases.
- Simultaneous proteome analysis of host cells and invading pathogens provides comprehensive insights into infection dynamics.
Purpose of the Study:
- To simultaneously profile the proteomes of human alveolar epithelial cells (A549) and Staphylococcus aureus during infection.
- To characterize time-resolved protein abundance changes in both host and pathogen.
- To provide a resource for studying host-pathogen interplay at the proteome level.
Main Methods:
- Infection of A549 cells with GFP-expressing S. aureus HG001.
- Fluorescence-activated cell sorting for enrichment of infected cells and bacteria.
- Label-free quantification for bacterial proteome analysis.
- Stable Isotope Labeling by Amino acids in Cell culture (SILAC) for host proteome analysis.
- Nano liquid chromatography-tandem mass spectrometry (nanoLC-MS/MS) for protein identification and quantification.
Main Results:
- Quantitative proteome data for S. aureus and A549 cells were obtained at hourly intervals post-infection.
- Time-resolved changes in bacterial protein abundance were measured.
- Host cell proteome adaptations were monitored in response to infection.
- Separation techniques allowed for distinct analysis of host and pathogen proteomes.
Conclusions:
- This study provides a valuable dataset for understanding the dynamic proteome changes during S. aureus infection.
- The methodology enables simultaneous proteome analysis of host and pathogen, offering a powerful tool for infection research.
- The data contributes to a deeper understanding of the molecular mechanisms underlying host-pathogen interactions.
