Cécile Jourlin-Castelli

Dr. Cécile Jourlin-Castelli

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Research Focus & Metrics

Academic Career Length

14Years (2013-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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18 April 2014 in Environmental Microbiology Reports
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Journal Article
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JAJoshua Armitano
Joshua Armitano
VMVincent Méjean
Vincent Méjean
CJCécile Jourlin-Castelli
Cécile Jourlin-Castelli
Summary: There is a growing interest in the bacterial pellicle, a biofilm floating at the air–liquid interface. Pellicles have been well studied in the G ram‐positive bacterium B acillus subtilis, but far less in G ram‐negative bacteria, where pellicle studies have mostly focused on matrix components rather than on the regulatory cascades involved. Several G ram‐negative bacteria, including pathogenic bacteria, have been shown to be able to form a pellicle under static conditions. Here, we summarize the growing body of knowledge about pellicle formation in G ram‐negative bacteria, especially about the components of the pellicle matrix. We also propose that the pellicle is a specific biofilm, and that its formation involves particular processes. Since this lifestyle concerns a growing number of bacteria, its properties undoubtedly deserve further investigation.

22 November 2017 in PLOS ONE
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Journal Article
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HBHiba Baaziz
Hiba Baaziz
CGCyril Gambari
Cyril Gambari
ABAnne Boyeldieu
Anne Boyeldieu
ACAmine Ali Chaouche
Amine Ali Chaouche
RARadia Alatou
Radia Alatou
MFMichel Fons
Michel Fons
The chromate efflux pump encoding gene chrASO was identified on the chromosome of Shewanella oneidensis MR1. Although chrASO is expressed without chromate, its expression level increases when Cr(VI) is added. When deleted, the resulting mutant ΔchrASO exhibits a chromate sensitive phenotype compared to that of the wild-type strain. Interestingly, heterologous expression of chrASO in E. coli confers resistance to high chromate concentration. Moreover, expression of chrASO in S. oneidensis and E. coli significantly improves Cr(VI) reduction. This effect could result either from extracytoplasmic chromate reduction or from a better cell survival leading to enhanced Cr(VI) reduction.

21 May 2013 in Environmental Microbiology
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JAJoshua Armitano
Joshua Armitano
VMVincent Méjean
Vincent Méjean
CJCécile Jourlin-Castelli
Cécile Jourlin-Castelli

19 February 2018 in Environmental Microbiology Reports
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Journal Article
Open access
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SBSophie Bouillet
Sophie Bouillet
DADallel Arabet
Dallel Arabet
CJCécile Jourlin-Castelli
Cécile Jourlin-Castelli
VMVincent Méjean
Vincent Méjean
CIChantal Iobbi-Nivol
Chantal Iobbi-Nivol
Summary: Partner‐Switching Systems (PSS) are widespread regulatory systems, each comprising a kinase‐anti‐σ, a phosphorylatable anti‐σ antagonist and a phosphatase module. The anti‐σ domain quickly sequesters or delivers the target σ factor according to the phosphorylation state of the anti‐σ antagonist induced by environmental signals. The PSS components are proteins alone or merged to other domains probably to adapt to the input signals. PSS are involved in major cellular processes including stress response, sporulation, biofilm formation and pathogenesis. Surprisingly, the target σ factors are often unknown and the sensing modules acting upstream from the PSS diverge according to the bacterial species. Indeed, they belong to either two‐component systems or complex pathways as the stressosome or Chemosensory Systems (CS). Based on a phylogenetic analysis, we propose that the sensing module in Gram‐negative bacteria is often a CS.

25 September 2018 in Environmental Microbiology
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Journal Article
Closed access
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CGCyril Gambari
Cyril Gambari
ABAnne Boyeldieu
Anne Boyeldieu
JAJoshua Armitano
Joshua Armitano
VMVincent Méjean
Vincent Méjean
CJCécile Jourlin-Castelli
Cécile Jourlin-Castelli

1 December 2016 in Journal of Biological Chemistry
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Journal Article
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SBSophie Bouillet
Sophie Bouillet
OGOlivier Genest
Olivier Genest
CJCécile Jourlin-Castelli
Cécile Jourlin-Castelli
MFMichel Fons
Michel Fons
VMVincent Méjean
Vincent Méjean
CIChantal Iobbi-Nivol
Chantal Iobbi-Nivol
Here, we show that a partner-switching system of the aquatic Proteobacterium Shewanella oneidensis regulates post-translationally σS (also called RpoS), the general stress response sigma factor. Genes SO2118 and SO2119 encode CrsA and CrsR, respectively. CrsR is a three-domain protein comprising a receiver, a phosphatase, and a kinase/anti-sigma domains, and CrsA is an anti-sigma antagonist. In vitro, CrsR sequesters σS and possesses kinase and phosphatase activities toward CrsA. In turn, dephosphorylated CrsA binds the anti-sigma domain of CrsR to allow the release of σS. This study reveals a novel pathway that post-translationally regulates the general stress response sigma factor differently than what was described for other proteobacteria like Escherichia coli. We argue that this pathway allows probably a rapid bacterial adaptation.