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A role for PchHI as the ABC transporter in iron acquisition by the siderophore pyochelin in Pseudomonas aeruginosa

Summary Iron is an essential nutrient for bacterial growth but poorly bioavailable. Bacteria scavenge ferric iron by synthesizing and secreting siderophores, small compounds with a high affinity for iron. Pyochelin (PCH) is one of the two siderophores produced by the opportunistic pathogen Pseudomon...

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Published in:Environmental microbiology 2022-02, Vol.24 (2), p.866-877
Main Authors: Roche, Béatrice, Garcia‐Rivera, Mariel A., Normant, Vincent, Kuhn, Lauriane, Hammann, Philippe, Brönstrup, Mark, Mislin, Gaëtan L. A., Schalk, Isabelle J.
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creator Roche, Béatrice
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Mislin, Gaëtan L. A.
Schalk, Isabelle J.
description Summary Iron is an essential nutrient for bacterial growth but poorly bioavailable. Bacteria scavenge ferric iron by synthesizing and secreting siderophores, small compounds with a high affinity for iron. Pyochelin (PCH) is one of the two siderophores produced by the opportunistic pathogen Pseudomonas aeruginosa. After capturing a ferric iron molecule, PCH‐Fe is imported back into bacteria first by the outer membrane transporter FptA and then by the inner membrane permease FptX. Here, using molecular biology, 55Fe uptake assays, and LC–MS/MS quantification, we first find a role for PchHI as the heterodimeric ABC transporter involved in the siderophore‐free iron uptake into the bacterial cytoplasm. We also provide the first evidence that PCH is able to reach the bacterial periplasm and cytoplasm when both FptA and FptX are expressed. Finally, we detected an interaction between PchH and FptX, linking the ABC transporter PchHI with the inner permease FptX in the PCH‐Fe uptake pathway. These results pave the way for a better understanding of the PCH siderophore pathway, giving future directions to tackle P. aeruginosa infections.
doi_str_mv 10.1111/1462-2920.15811
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We also provide the first evidence that PCH is able to reach the bacterial periplasm and cytoplasm when both FptA and FptX are expressed. Finally, we detected an interaction between PchH and FptX, linking the ABC transporter PchHI with the inner permease FptX in the PCH‐Fe uptake pathway. 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A.</creatorcontrib><creatorcontrib>Schalk, Isabelle J.</creatorcontrib><title>A role for PchHI as the ABC transporter in iron acquisition by the siderophore pyochelin in Pseudomonas aeruginosa</title><title>Environmental microbiology</title><addtitle>Environ Microbiol</addtitle><description>Summary Iron is an essential nutrient for bacterial growth but poorly bioavailable. Bacteria scavenge ferric iron by synthesizing and secreting siderophores, small compounds with a high affinity for iron. Pyochelin (PCH) is one of the two siderophores produced by the opportunistic pathogen Pseudomonas aeruginosa. After capturing a ferric iron molecule, PCH‐Fe is imported back into bacteria first by the outer membrane transporter FptA and then by the inner membrane permease FptX. Here, using molecular biology, 55Fe uptake assays, and LC–MS/MS quantification, we first find a role for PchHI as the heterodimeric ABC transporter involved in the siderophore‐free iron uptake into the bacterial cytoplasm. 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A.</au><au>Schalk, Isabelle J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A role for PchHI as the ABC transporter in iron acquisition by the siderophore pyochelin in Pseudomonas aeruginosa</atitle><jtitle>Environmental microbiology</jtitle><addtitle>Environ Microbiol</addtitle><date>2022-02</date><risdate>2022</risdate><volume>24</volume><issue>2</issue><spage>866</spage><epage>877</epage><pages>866-877</pages><issn>1462-2912</issn><eissn>1462-2920</eissn><abstract>Summary Iron is an essential nutrient for bacterial growth but poorly bioavailable. Bacteria scavenge ferric iron by synthesizing and secreting siderophores, small compounds with a high affinity for iron. Pyochelin (PCH) is one of the two siderophores produced by the opportunistic pathogen Pseudomonas aeruginosa. After capturing a ferric iron molecule, PCH‐Fe is imported back into bacteria first by the outer membrane transporter FptA and then by the inner membrane permease FptX. Here, using molecular biology, 55Fe uptake assays, and LC–MS/MS quantification, we first find a role for PchHI as the heterodimeric ABC transporter involved in the siderophore‐free iron uptake into the bacterial cytoplasm. We also provide the first evidence that PCH is able to reach the bacterial periplasm and cytoplasm when both FptA and FptX are expressed. Finally, we detected an interaction between PchH and FptX, linking the ABC transporter PchHI with the inner permease FptX in the PCH‐Fe uptake pathway. 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ispartof Environmental microbiology, 2022-02, Vol.24 (2), p.866-877
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language eng
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source Wiley-Blackwell Read & Publish Collection
subjects ABC transporter
ABC transporters
ATP-Binding Cassette Transporters - genetics
ATP-Binding Cassette Transporters - metabolism
Bacteria
Bacterial Outer Membrane Proteins - genetics
Bacterial Outer Membrane Proteins - metabolism
Bacteriology
Bioavailability
Biochemistry
Biochemistry, Molecular Biology
Biology
Chromatography, Liquid
Cytoplasm
Iron
Iron - metabolism
Life Sciences
Membranes
Microbiology and Parasitology
Molecular biology
Opportunist infection
Pathogens
Periplasm
Permease
Phenols
Pseudomonas aeruginosa
Pseudomonas aeruginosa - genetics
Pseudomonas aeruginosa - metabolism
Receptors, Cell Surface - metabolism
Siderophores
Siderophores - metabolism
Tandem Mass Spectrometry
Thiazoles
Uptake
title A role for PchHI as the ABC transporter in iron acquisition by the siderophore pyochelin in Pseudomonas aeruginosa
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