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Updated: Jun 13, 2026
07:33
Bacterial Cell Culture at the Single-cell Level Inside Giant Vesicles
Published on: April 30, 2019
Transcriptomic and proteomic responses to gas vesicle collapse in native and engineered bacterial systems
Biorxiv : the Preprint Server for Biology
|June 12, 2026
Summary
Cellular responses to gas vesicle (GV) collapse were investigated. The cyanobacterium Dolichospermum flos-aquae showed stress responses, unlike E. coli, and no specific protein binders for collapsed GVs were found.
Area of Science:
- Microbiology
- Biophysics
- Biotechnology
Background:
- Gas vesicles (GVs) are microbial protein nanostructures for buoyancy control.
- GV collapse under pressure is key to applications like acoustic imaging but its cellular impact is unknown.
- Understanding cellular responses to collapsed GVs is crucial for their biomedical applications.
Purpose of the Study:
- To investigate cellular responses to gas vesicle (GV) collapse using omics approaches.
- To identify potential protein binders that recognize collapsed GVs within cells.
- To compare cellular stress reactions in native and heterologous GV-producing systems.
Main Methods:
- Transcriptomic (RNA sequencing) and proteomic (LC-MS/MS pull-down assays) analyses were performed.
- Cellular responses were studied in the native cyanobacterium Dolichospermum flos-aquae and heterologously in E. coli.
- Bioluminescence reporter assays were used to assess stress promoter activation.
Main Results:
- RNA sequencing in D. flos-aquae revealed upregulation of heat shock proteins, indicating a stress response to collapsed GVs.
- E. coli expressing GVs did not show comparable heat shock promoter activation.
- No strong candidate protein binders for collapsed GVs were identified in either system.
Conclusions:
- Cellular responses to gas vesicle collapse appear complex and differ between native and heterologous systems.
- The mechanism by which cells detect and manage collapsed GVs remains elusive.
- Further research with enhanced sensitivity is needed to fully understand cellular management of protein aggregates like collapsed GVs.
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