Faculty Opinions recommendation of New insights into the metal specificity of the Pseudomonas aeruginosa pyoverdine-iron uptake pathway.

2017 ◽  
Author(s):  
John Coates
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Iron Uptake ◽  
Metal Specificity ◽  
Uptake Pathway

scholarly journals Pyoverdine-Mediated Iron Uptake in Pseudomonas aeruginosa: the Tat System Is Required for PvdN but Not for FpvA Transport

2006 ◽  
Vol 188 (9) ◽  
pp. 3317-3323 ◽  
Author(s):  
Romé Voulhoux ◽  
Alain Filloux ◽  
Isabelle J. Schalk
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Outer Membrane ◽  
Iron Uptake ◽  
Cytoplasmic Membrane ◽  
Signal Sequence ◽  
Iron Release ◽  
Outer Membrane Receptor ◽  
Uptake Pathway ◽  
Uptake Process ◽  
Tat System

ABSTRACT Under iron-limiting conditions, Pseudomonas aeruginosa PAO1 secretes a fluorescent siderophore called pyoverdine (Pvd). After chelating iron, this ferric siderophore is transported back into the cells via the outer membrane receptor FpvA. The Pvd-dependent iron uptake pathway requires several essential genes involved in both the synthesis of Pvd and the uptake of ferric Pvd inside the cell. A previous study describing the global phenotype of a tat-deficient P. aeruginosa strain showed that the defect in Pvd-mediated iron uptake was due to the Tat-dependent export of proteins involved in Pvd biogenesis and ferric Pvd uptake (U. Ochsner, A. Snyder, A. I. Vasil, and M. L. Vasil, Proc. Natl. Acad. Sci. USA 99:8312-8317, 2002). Using biochemical and biophysical tools, we showed that despite its predicted Tat signal sequence, FpvA is correctly located in the outer membrane of a tat mutant and is fully functional for all steps of the iron uptake process (ferric Pvd uptake and recycling of Pvd on FpvA after iron release). However, in the tat mutant, no Pvd was produced. This suggested that a key element in the Pvd biogenesis pathway must be exported to the periplasm by the Tat pathway. We located PvdN, a still unknown but essential component in Pvd biogenesis, at the periplasmic side of the cytoplasmic membrane and showed that its export is Tat dependent. Our results further support the idea that a critical step of the Pvd biogenesis pathway involving PvdN occurs at the periplasmic side of the cytoplasmic membrane.

The PvdRT-OpmQ efflux pump controls the metal selectivity of the iron uptake pathway mediated by the siderophore pyoverdine in Pseudomonas aeruginosa

2011 ◽  
Vol 14 (7) ◽  
pp. 1696-1708 ◽  
Author(s):  
Mélissa Hannauer ◽  
Armelle Braud ◽  
Françoise Hoegy ◽  
Pascale Ronot ◽  
Anne Boos ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Iron Uptake ◽  
Efflux Pump ◽  
Uptake Pathway ◽  
Metal Selectivity

scholarly journals Phenotypic Adaptation of Pseudomonas aeruginosa in the Presence of Siderophore-Antibiotic Conjugates during Epithelial Cell Infection

2020 ◽  
Vol 8 (11) ◽  
pp. 1820
Author(s):  
Quentin Perraud ◽  
Paola Cantero ◽  
Mathilde Munier ◽  
Françoise Hoegy ◽  
Nicolas Zill ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Phenotypic Plasticity ◽  
Epithelial Cell ◽  
Iron Uptake ◽  
Iron Acquisition ◽  
Trojan Horse ◽  
Cell Infection ◽  
Uptake Pathway ◽  
Pathway Expression ◽  
Uptake Process

Iron acquisition pathways have often been considered to be gateways for the uptake of antibiotics into bacteria. Bacteria excrete chelators, called siderophores, to access iron. Antibiotic molecules can be covalently attached to siderophores for their transport into pathogens during the iron-uptake process. P. aeruginosa produces two siderophores and is also able to use many siderophores produced by other bacteria. We investigated the phenotypic plasticity of iron-uptake pathway expression in an epithelial cell infection assay in the presence of two different siderophore–antibiotic conjugates, one with a hydroxamate siderophore and the second with a tris-catechol. Proteomic and RT-qPCR approaches showed that P. aeruginosa was able to sense the presence of both compounds in its environment and adapt the expression of its iron uptake pathways to access iron via them. Moreover, the catechol-type siderophore–antibiotic was clearly more efficient in inducing the expression of its corresponding transporter than the hydroxamate compound when both were simultaneously present. In parallel, the expression of the proteins of the two iron uptake pathways using siderophores produced by P. aeruginosa was significantly repressed in the presence of both conjugates. Altogether, the data indicate that catechol-type siderophores are more promising vectors for antibiotic vectorization using a Trojan-horse strategy.

scholarly journals Phenotypic Adaption of Pseudomonas aeruginosa by Hacking Siderophores Produced by Other Microorganisms

2020 ◽  
Vol 19 (4) ◽  
pp. 589-607 ◽  
Author(s):  
Quentin Perraud ◽  
Paola Cantero ◽  
Béatrice Roche ◽  
Véronique Gasser ◽  
Vincent P. Normant ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Phenotypic Plasticity ◽  
Iron Uptake ◽  
Opportunistic Pathogen ◽  
Growth Conditions ◽  
Growth Media ◽  
Cell Infection ◽  
Uptake Pathway ◽  
Pathway Expression ◽  
Strong Competition

Bacteria secrete siderophores to access iron, a key nutrient poorly bioavailable and the source of strong competition between microorganisms in most biotopes. Many bacteria also use siderophores produced by other microorganisms (exosiderophores) in a piracy strategy. Pseudomonas aeruginosa, an opportunistic pathogen, produces two siderophores, pyoverdine and pyochelin, and is also able to use a panel of exosiderophores. We first investigated expression of the various iron-uptake pathways of P. aeruginosa in three different growth media using proteomic and RT-qPCR approaches and observed three different phenotypic patterns, indicating complex phenotypic plasticity in the expression of the various iron-uptake pathways. We then investigated the phenotypic plasticity of iron-uptake pathway expression in the presence of various exosiderophores (present individually or as a mixture) under planktonic growth conditions, as well as in an epithelial cell infection assay. In all growth conditions tested, catechol-type exosiderophores were clearly more efficient in inducing the expression of their corresponding transporters than the others, showing that bacteria opt for the use of catechol siderophores to access iron when they are present in the environment. In parallel, expression of the proteins of the pyochelin pathway was significantly repressed under most conditions tested, as well as that of proteins of the pyoverdine pathway, but to a lesser extent. There was no effect on the expression of the heme and ferrous uptake pathways. Overall, these data provide precise insights on how P. aeruginosa adjusts the expression of its various iron-uptake pathways (phenotypic plasticity and switching) to match varying levels of iron and competition.

scholarly journals The Pseudomonas aeruginosa Pyochelin-Iron Uptake Pathway and Its Metal Specificity

2009 ◽  
Vol 191 (11) ◽  
pp. 3517-3525 ◽  
Author(s):  
Armelle Braud ◽  
Mélissa Hannauer ◽  
Gaëtan L. A. Mislin ◽  
Isabelle J. Schalk
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Inductively Coupled Plasma ◽  
Metal Uptake ◽  
Emission Spectrometry ◽  
Fluorescent Properties ◽  
Plasma Atomic Emission Spectrometry ◽  
Extracellular Medium ◽  
Metal Specificity ◽  
Uptake Pathway

ABSTRACT Pyochelin (Pch) is one of the two major siderophores produced and secreted by Pseudomonas aeruginosa PAO1 to assimilate iron. It chelates iron in the extracellular medium and transports it into the cell via a specific outer membrane transporter, FptA. We used the fluorescent properties of Pch to show that this siderophore chelates, in addition to Fe3+ albeit with substantially lower affinities, Ag+, Al3+, Cd2+, Co2+, Cr2+, Cu2+, Eu3+, Ga3+, Hg2+, Mn2+, Ni2+, Pb2+, Sn2+, Tb3+, Tl+, and Zn2+. Surprisingly, the Pch complexes with all these metals bound to FptA with affinities in the range of 10 nM to 4.8 μM (the affinity of Pch-Fe is 10 nM) and were able to inhibit, with various efficiencies, Pch-55Fe uptake in vivo. We used inductively coupled plasma atomic emission spectrometry to follow metal uptake by P. aeruginosa. Energy-dependent metal uptake, in the presence of Pch, was efficient only for Fe3+. Co2+, Ga3+, and Ni2+ were also transported, but the uptake rates were 23- to 35-fold lower than that for Fe3+. No uptake was seen for all the other metals. Thus, cell surface FptA has broad metal specificity at the binding stage but is much more selective for the metal uptake process. This uptake pathway does not appear to efficiently assimilate any metal other than Fe3+.

New insights into the metal specificity of thePseudomonas aeruginosapyoverdine-iron uptake pathway

2009 ◽  
Vol 11 (5) ◽  
pp. 1079-1091 ◽  
Author(s):  
Armelle Braud ◽  
Françoise Hoegy ◽  
Karine Jezequel ◽  
Thierry Lebeau ◽  
Isabelle J. Schalk
Keyword(s):  
Iron Uptake ◽  
Metal Specificity ◽  
Uptake Pathway

A new mechanism for membrane iron transport in Pseudomonas aeruginosa

2002 ◽  
Vol 30 (4) ◽  
pp. 702-705 ◽  
Author(s):  
I.J. Schalk ◽  
M. A. Abdallah ◽  
F. Pattus
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Outer Membrane ◽  
Iron Uptake ◽  
Iron Transport ◽  
Membrane Receptor ◽  
Gram Negative Bacteria ◽  
Outer Membrane Receptor ◽  
Uptake Mechanism ◽  
Atp Binding Cassette Transporter ◽  
Biophysical Studies

Various biochemical and biophysical studies have demonstrated the existence of a novel iron-uptake mechanism in Pseudomonas aeruginosa, different from that generally described for ferrichrome and ferric-enterobactin in Escherichia coli. This new iron-uptake mechanism involves all the proteins generally reported to be involved in the uptake of ferric-siderophore complexes in Gram-negative bacteria (i.e. the outer membrane receptor, periplasmic binding protein and ATP-binding-cassette transporter), but differs in the behaviour of the siderophore. One of the key features of this process is the binding of iron-free pyoverdin to the outer membrane receptor FpvA in conditions of iron deficiency.

A cell biological view of the siderophore pyochelin iron uptake pathway inPseudomonas aeruginosa

2014 ◽  
Vol 17 (1) ◽  
pp. 171-185 ◽  
Author(s):  
Olivier Cunrath ◽  
Véronique Gasser ◽  
Françoise Hoegy ◽  
Cornelia Reimmann ◽  
Laurent Guillon ◽  
...  
Keyword(s):  
Iron Uptake ◽  
Uptake Pathway ◽  
A Cell
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