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© J.M. Ghigo (Institut Pasteur) and Brigite Arbeille (LBC-ME. Faculté de Médecine de Tours)
Colorized scanning electron microscopy of an E. coli biofilm developing on a glass surface
Publication : Scientific Reports

Visualizing the dynamics of exported bacterial proteins with the chemogenetic fluorescent reporter FAST

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Scientific Reports - 25 Sep 2020

Y Chekli, C Perron-Cane, D Dell'Arcipret, JF Allemand, C Li, JM Ghigo, A Gauthier, A Lebreton, N Desprat*, C. Beloin*

Link to Pubmed [PMID] – 32978420

Link to DOI [DOI] – 10.1038/s41598-020-72498-2

Sci Rep. 2020 Sep 25;10(1):15791. doi: 10.1038/s41598-020-72498-2.

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.

https://pubmed.ncbi.nlm.nih.gov/32978420/