Unknown

Dataset Information

0

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.

SUBMITTER: Chekli Y 

PROVIDER: S-EPMC7519654 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Chekli Yankel Y   Peron-Cane Caroline C   Dell'Arciprete Dario D   Allemand Jean-François JF   Li Chenge C   Ghigo Jean-Marc JM   Gautier Arnaud A   Lebreton Alice A   Desprat Nicolas N   Beloin Christophe C  

Scientific reports 20200925 1


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 recentl  ...[more]

Similar Datasets

| S-EPMC6037777 | biostudies-literature
| S-EPMC8633346 | biostudies-literature
| S-EPMC4836418 | biostudies-literature
| S-EPMC2752587 | biostudies-literature
| S-EPMC154567 | biostudies-literature
| S-EPMC7610487 | biostudies-literature
| S-EPMC5788022 | biostudies-literature
| S-EPMC2935039 | biostudies-literature
| S-EPMC4518229 | biostudies-literature
| S-EPMC3035939 | biostudies-literature