Imperial College London
Dr Satomi Inoue

DrSatomiInoue

Faculty of Natural Sciences, Department of Life Sciences

Visiting Researcher
 
 
 
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Contact

 

+44 (0)1235 567 809s.inoue

 
 
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Location

 

1.11Diamond Light Source LtdHarwell Science and Innovation Campus

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Summary

 

Publications

Citation

BibTex format

@article{Travin:2022:10.1101/2022.04.27.489825,
author = {Travin, DY and Vigouroux, A and Inaba-Inoue, S and Qu, F and Jouan, R and Lachat, J and Sutormin, D and Dubiley, S and Beis, K and Moréra, S and Severinov, K and Mergaert, P},
doi = {10.1101/2022.04.27.489825},
title = {The antibiotic phazolicin displays a dual mode of uptake in Gram-negative bacteria},
url = {http://dx.doi.org/10.1101/2022.04.27.489825},
year = {2022}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - <jats:title>ABSTRACT</jats:title><jats:p>Phazolicin (PHZ) is a peptide antibiotic exhibiting narrow-spectrum activity against rhizobia closely related to its producer <jats:italic>Rhizobium</jats:italic> sp. Pop5. Using genetic and biochemical techniques, we here identified BacA and YejABEF as two importers of PHZ in a sensitive model strain <jats:italic>Sinorhizobium meliloti</jats:italic> Sm1021. BacA and YejABEF are members of SLiPT and ABC transporter families of non-specific peptide importers, respectively. The uptake of PHZ by two distinct families of transporters dramatically decreases the naturally occurring rate of resistance. Moreover, since both BacA and YejABEF are essential for the development of functional symbiosis of rhizobia with leguminous plants, the acquisition of PHZ resistance via the inactivation of transporters is further disfavoured since single <jats:italic>bacA</jats:italic> or <jats:italic>yejABEF</jats:italic> mutants are unable to propagate in root nodules. Crystal structures of the periplasmic subunit YejA from <jats:italic>S. meliloti</jats:italic> and <jats:italic>Escherichia coli</jats:italic> revealed fortuitous bound peptides, suggesting a non-specific peptide-binding mechanism that facilitates the uptake of PHZ and other antimicrobial peptides.</jats:p><jats:sec><jats:title>SIGNIFICANCE</jats:title><jats:p>Many bacteria produce antimicrobial peptides to eliminate competitors and create an exclusive niche. These peptides kill bacteria by either membrane disruption or inhibiting essential intracellular processes. The Achilles heel of the latter type of antimicrobials is their dependence on transporters to enter the susceptible bacteria since mutations in such transporters result in resistance. We describe here how the ribosome-targeting peptide phazolicin, produced by <jats:italic>Rhizobium</jats:italic&g
AU  - Travin,DY
AU  - Vigouroux,A
AU  - Inaba-Inoue,S
AU  - Qu,F
AU  - Jouan,R
AU  - Lachat,J
AU  - Sutormin,D
AU  - Dubiley,S
AU  - Beis,K
AU  - Moréra,S
AU  - Severinov,K
AU  - Mergaert,P
DO  - 10.1101/2022.04.27.489825
PY  - 2022///
TI  - The antibiotic phazolicin displays a dual mode of uptake in Gram-negative bacteria
UR  - http://dx.doi.org/10.1101/2022.04.27.489825
ER  -
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