Search anything and hit enter
  • Teams
  • Members
  • Projects
  • Events
  • Calls
  • Jobs
  • publications
  • Software
  • Tools
  • Network
  • Equipment

A little guide for advanced search:

  • Tip 1. You can use quotes "" to search for an exact expression.
    Example: "cell division"
  • Tip 2. You can use + symbol to restrict results containing all words.
    Example: +cell +stem
  • Tip 3. You can use + and - symbols to force inclusion or exclusion of specific words.
    Example: +cell -stem
e.g. searching for members in projects tagged cancer
Search for
Count
IN
OUT
Content 1
  • member
  • 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
  • Director of Center
  • Director of Department
  • Director of Institute
  • Director of National Reference Center
  • Group Leader
  • Head of Facility
  • Head of Structure
  • Honorary President of the Departement
  • Labex Coordinator
Content 2
  • member
  • 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
  • Director of Center
  • Director of Department
  • Director of Institute
  • Director of National Reference Center
  • Group Leader
  • Head of Facility
  • Head of Structure
  • Honorary President of the Departement
  • Labex Coordinator
Search
Go back
Scroll to top
Share
© Sandrine Etienne-Manneville
Photo prise à l'avant (dans la protrusion) d'astrocytes primaires de rat en migration. Marquage par immunofluorescence montrant en rouge, p150 Glued, une protéine associée aux extrémités 'plus' des microtubules et en vert la tubuline des microtubules. La photographie montre l'accumulation de p150 Glued à l'avant des cellules en migration, où la protéine pourrait participer à l'ancrage des microtubules à la membrane plasmique. Pour essayer de corriger, les dérèglements observés lors de la migration des cellules d'astrocytes tumuraux ou gliomes on cherche à connaitre les mécanismes moléculaires fondamentaux qui controlent la polarisation et la migration cellulaires.

About

Protein folding and membrane interactions

My research interests are mainly focused on protein folding, thermodynamics, hydrodynamics and protein translocation across membranes. In the BIM Unit, I am characterizing a bacterial toxin, the adenylate cyclase (CyaA) produced by Bordetella pertussis, the causative agent of whooping cough, which is currently in increasing incidence and represents a global public health concern. The study of CyaA offers a unique opportunity to explore various topics such as intrinsically disordered proteins (IDP), the effect of molecular crowding, protein-protein, protein-ligand and protein-membrane interactions. More about the CyaA project can be found on the page of the Group.

Secretion process of CyaA illustrating the intrinsically disordered nature of the apo-state inside cell and the calcium-loaded folded state in the extracellular milieu.Sans titre

 

Besides investigating the biophysics of CyaA, I have pursued several projects initiated during my previous post-doctoral positions or within new collaborations established with various groups inside or outside Institut Pasteur. The main goal is to improve the understanding of the behavior of amphitropic proteins, i.e., to describe how soluble proteins are able to partition from the solution to the membrane (and eventually translocate across the lipid bilayer) to regulate their functions. The methods used to characterize biophysics of amphitropic proteins are mainly biochemical and spectroscopic approaches. Inside Institut Pasteur, I am working with other Units from Institut Pasteur on these topics, like PimA with Pedro Alzari’ Unit and large clostridial toxins with Michel Popoff’ Unit. Outside IP, I am collaborating with several groups, such as WJ Tang, Chicago, USA, Marcelo Guerin, Bilbao, Spain, Scot Ouellette, South Dakota, USA, on protein membrane interactions; Abdel Aouacheria, Lyon and Vincent Forge, Grenoble on Bcl proteins; Allen Minton, Bethesda, USA, on molecular crowding; Daniel Isabey, Creteil Mondor, on multi-scale study of CyaA effects on the upper respiratory tract, …

Scheme of the pH-dependent membrane insertion process of the DT T domain. From left to right, membrane at pH 7 in the absence of T; membrane at the same pH in the presence of T; the membrane-bound state of T at pH 6; the membrane- inserted state of T at pH 4. Membrane layers, the T domain and water molecules are scaled. Red and blue cylinders represent the helical backbone of the N- and C-terminal regions of T, respectively. The depth of penetration and the orientation of helices are inferred from neutron scattering and solid-state NMR, respectively. The water molecules correspond to the contents determined for each layer from neutron experiments. The vertical bars are 1 nm scale. Picture from Chenal et al., 2009, JMB.

Illustration of the pH-dependent membrane insertion of the translocation domain of the diphtheria toxin, inferred from specular neutron reflectometry, solid state NMR and other biophysical methods (figure from Chenal et al., 2009, J. Mol. Biol.).

A: X-ray Structure of Anthrolysin O, a ALO PFOCholesterol-dependent Cytolysin Secreted by Bacillus anthracis. B: Structural comparison of ALO with other Cholesterol Dependent Cytolysins (CDC) such as PFO and ILY (figure from Bourdeau et al., 2009). 

Left, Scheme of Bcl-XL amyloidogenesis recapitulating our findings. We showed that Bcl-xL, an apoptotic protein, forms fibers in vitro. Their amyloid feature has an inverse relationship with the native protein stability. In vivo, Bcl-xL colocalizes with amyloid deposits within stressed neuroblastoma. Right, Electron microscopy of aggregates of Bcl-xL formed at 37 °C. The aggregates were negatively stained prior EM observation. Scale bar: 200 nm. Pictures from Chenal et al., 2012, JMB.

Schematic view of Bcl-XL amyloidogenesis and EM of fibrils (figure from Chenal et al., 2012, J. Mol. Biol.).

 

Projects

CV

2017: Research director at Institut Pasteur
2015: Team leader
2010: Habilitation to supervise research (HDR), Paris VII
2006: permanent position in BIM Unit, Institut Pasteur, Paris
2005-06: post-doc in Daniel Ladant Unit, Institut Pasteur, Paris
2004-05: post-doc in Daniel Gillet Unit, CEA
2002-03: post-doc in Florent Guillain group, CEA-CNRS, Grenoble
2001-1999 : PhD (CEA Saclay) ED 227, MNHN, Paris
1998 : M2 D.E.A. n° 950 103, MNHN, P. VII, ESPCI, Paris
1997 : M1 Maîtrise de Biologie Moléculaire et Cellulaire (UPMC, P. VI), Paris
1996 : Licence de Biologie Moléculaire et Cellulaire, UPMC (P. VI), Paris
1995 : D.E.U.G. de Biologie des Organismes, UPMC (P. VI), Paris

Publications

Download