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  • team
  • department
  • center
  • program_project
  • nrc
  • whocc
  • project
  • software
  • tool
  • patent
  • Administrative Staff
  • Assistant Professor
  • Associate Professor
  • Clinical Research Assistant
  • Full Professor
  • Graduate Student
  • Lab assistant
  • Non-permanent Researcher
  • Permanent Researcher
  • Pharmacist
  • PhD Student
  • Physician
  • Post-doc
  • Project Manager
  • Research Associate
  • Research Engineer
  • Retired scientist
  • Technician
  • Undergraduate Student
  • Veterinary
  • Visiting Scientist
  • Deputy Director of Center
  • Deputy Director of Department
  • Deputy Director of National Reference Center
  • Deputy Head of Facility
  • Director of Center
  • Director of Department
  • Director of Institute
  • Director of National Reference Center
  • Group Leader
  • Head of Facility
  • Head of Operations
  • Head of Structure
  • Honorary President of the Departement
  • Labex Coordinator
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Starting Date
01
Jan 2016
Ending Date
01
Jan 2018
Status
Ongoing
Members
2
Structures
2

About

cover.tif

Many Gram-negative bacteria secrete stably folded or even multimeric proteins across the outer membrane. The secreted substrates are often virulence factors like hydolases or toxins that contribute to the ability of bacteria to adapt and shape their environment. Our aim is to elucidate the molecular mechanism of folded protein transport, which implicates a complex machinery called the type 2 secretion system (T2SS) spanning the bacterial envelope. Our model to study this system in the pullulanase secretion machinery from Klebsiella oxytoca, functionally reconstituted in Escherichia coli.

We are currenty focusing on several aspects of T2SS function using structural, biochemical, genetic and modeling analysis to decipher how, at the molecular level, the T2S systems specifically recognize and take up folded substrates. In the Klebsiella T2SS, so far only one substrate has been identified – the 116 kDa lipoprotein pullulanase (PulA). We have recently identified two structural motifs required for PulA secretion, in collaboration with Pedro Alzari (Institut Pasteur) and Peter J. Bond (A-STAR Institute, Singapore). The Ig-like domain N1 and the domain Ins of PulA are both highly mobile stabilized by disulfide bridges at their base and each seems to play a distinct role in secretion,  possibly via binding to  different components of the secretion machinery. The aim of our current studies  is to characterize these interactions and to identify their molecular function.

N1 and Ins domains are required for PulA recognition by the type 2 secretion apparatus
N1 and Ins domains of PulA are required for secretion

Fundings