ArticleScientific reports2020
Visualizing the dynamics of exported bacterial proteins with the chemogenetic fluorescent reporter FAST.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed.
- Double-Labeling Method for Visualization and Quantification of Membrane-Associated Proteins inInternational journal of molecular sciences · 2023Article
- Click Triazole as a Linker for Pretargeting Strategies: Synthesis, Docking Investigations, Fluorescence Diagnosis, and Antibacterial Action Studies.Molecules (Basel, Switzerland) · 2023Article
- Recent Advancements in Tracking Bacterial Effector Protein Translocation.Microorganisms · 2022Review
- Engineering of a fluorescent chemogenetic reporter with tunable color for advanced live-cell imaging.Nature communications · 2021Article
- The C-Terminal Domain of Clostridioides difficile TcdC Is Exposed on the Bacterial Cell Surface.Journal of bacteriology · 2020Article
- Fluorescent secreted bacterial effectors reveal active intravacuolar proliferation of Listeria monocytogenes in epithelial cells.PLoS pathogens · 2020Article
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
Bacterial proteins exported to the cell surface play key cellular functions. However, despite the interest to study the localisation of surface proteins such as adhesins, transporters or hydrolases, monitoring their dynamics in live imaging remains challenging, due to the limited availability of fluorescent probes remaining functional after secretion. In this work, we used the Escherichia coli intimin and the Listeria monocytogenes InlB invasin as surface exposed scaffolds fused with the recently developed chemogenetic fluorescent reporter protein FAST. Using both membrane permeant (HBR-3,5DM) and non-permeant (HBRAA-3E) fluorogens that fluoresce upon binding to FAST, we demonstrated that fully functional FAST can be exposed at the cell surface and used to specifically tag the external side of the bacterial envelop in both diderm and monoderm bacteria. Our work opens new avenues to study the organization and dynamics of the bacterial cell surface proteins.
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Registered trials
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