Publications
2021
Gasser Véronique, Kuhn Lauriane, Hubert Thibaut, Aussel Laurent, Hammann Philippe, Schalk Isabelle J.
The Esterase PfeE, the Achilles' Heel in the Battle for Iron between Pseudomonas aeruginosa and Escherichia coli Article de journal
Dans: International Journal of Molecular Sciences, vol. 22, no. 6, p. 2814, 2021, ISSN: 1422-0067.
Résumé | Liens | BibTeX | Étiquettes: Carrier Proteins, co-cultures, enterobactin, Escherichia coli, Escherichia coli Proteins, Esterases, Iron, iron homeostasis, iron uptake, outer membrane transporters, PPSE, Pseudomonas aeruginosa, siderophore, TonB
@article{gasser_esterase_2021,
title = {The Esterase PfeE, the Achilles' Heel in the Battle for Iron between Pseudomonas aeruginosa and Escherichia coli},
author = {Véronique Gasser and Lauriane Kuhn and Thibaut Hubert and Laurent Aussel and Philippe Hammann and Isabelle J. Schalk},
doi = {10.3390/ijms22062814},
issn = {1422-0067},
year = {2021},
date = {2021-03-01},
urldate = {2021-03-01},
journal = {International Journal of Molecular Sciences},
volume = {22},
number = {6},
pages = {2814},
abstract = {Bacteria access iron, a key nutrient, by producing siderophores or using siderophores produced by other microorganisms. The pathogen Pseudomonas aeruginosa produces two siderophores but is also able to pirate enterobactin (ENT), the siderophore produced by Escherichia coli. ENT-Fe complexes are imported across the outer membrane of P. aeruginosa by the two outer membrane transporters PfeA and PirA. Iron is released from ENT in the P. aeruginosa periplasm by hydrolysis of ENT by the esterase PfeE. We show here that pfeE gene deletion renders P. aeruginosa unable to grow in the presence of ENT because it is unable to access iron via this siderophore. Two-species co-cultures under iron-restricted conditions show that P. aeruginosa strongly represses the growth of E. coli as long it is able to produce its own siderophores. Both strains are present in similar proportions in the culture as long as the siderophore-deficient P. aeruginosa strain is able to use ENT produced by E. coli to access iron. If pfeE is deleted, E. coli has the upper hand in the culture and P. aeruginosa growth is repressed. Overall, these data show that PfeE is the Achilles' heel of P. aeruginosa in communities with bacteria producing ENT.},
keywords = {Carrier Proteins, co-cultures, enterobactin, Escherichia coli, Escherichia coli Proteins, Esterases, Iron, iron homeostasis, iron uptake, outer membrane transporters, PPSE, Pseudomonas aeruginosa, siderophore, TonB},
pubstate = {published},
tppubtype = {article}
}
2004
Marco Valeria De, Stier Gunter, Blandin Stephanie A, de Marco Ario
The solubility and stability of recombinant proteins are increased by their fusion to NusA Article de journal
Dans: Biochem. Biophys. Res. Commun., vol. 322, no. 3, p. 766–771, 2004, ISSN: 0006-291X.
Résumé | Liens | BibTeX | Étiquettes: blandin, Drug Stability, Escherichia coli Proteins, Genetic Vectors, Glutathione Transferase, Kinetics, M3i, Oxidation-Reduction, Peptide Elongation Factors, Recombinant Fusion Proteins, Recombinant Proteins, Solubility, Transcription Factors, Transcriptional Elongation Factors
@article{de_marco_solubility_2004,
title = {The solubility and stability of recombinant proteins are increased by their fusion to NusA},
author = {Valeria De Marco and Gunter Stier and Stephanie A Blandin and Ario de Marco},
doi = {10.1016/j.bbrc.2004.07.189},
issn = {0006-291X},
year = {2004},
date = {2004-01-01},
journal = {Biochem. Biophys. Res. Commun.},
volume = {322},
number = {3},
pages = {766--771},
abstract = {The new bacterial vector pETM60 enables the expression of His-tagged recombinant proteins fused to the C-terminus of NusA through a TEV protease recognition sequence. Three sequences coding for two protein domains (Xklp3A and Tep3Ag) and one membrane-bound viral protein (E8R) could not be expressed in a soluble form in bacteria. Their GST-fusions were mostly soluble but quickly degraded during purification. The same sequences cloned in pETM60 were efficiently purified by metal affinity and recovered soluble after the removal of the fusion partner. The NusA-fused constructs enabled to yield 13-20mg of fusion protein per litre of culture and 2.5-5mg of pure protein per litre of culture. Structural analysis indicated that the purified proteins were monodispersed and correctly folded. NusA has been used to raise antibodies that have been successfully used for Western blot and immunoprecipitation of NusA fusion proteins.},
keywords = {blandin, Drug Stability, Escherichia coli Proteins, Genetic Vectors, Glutathione Transferase, Kinetics, M3i, Oxidation-Reduction, Peptide Elongation Factors, Recombinant Fusion Proteins, Recombinant Proteins, Solubility, Transcription Factors, Transcriptional Elongation Factors},
pubstate = {published},
tppubtype = {article}
}