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

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.

journal_name

Sci Rep

journal_title

Scientific reports

authors

Chekli Y,Peron-Cane C,Dell'Arciprete D,Allemand JF,Li C,Ghigo JM,Gautier A,Lebreton A,Desprat N,Beloin C

doi

10.1038/s41598-020-72498-2

subject

Has Abstract

pub_date

2020-09-25 00:00:00

pages

15791

issue

1

issn

2045-2322

pii

10.1038/s41598-020-72498-2

journal_volume

10

pub_type

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