Nuclear Magnetic Resonance of Biomolecules - CNRS URA2185  


  HEADProf. DELEPIERRE Muriel / murield@pasteur.fr
  MEMBERSCAILLET-SAGUY Célia / Dr CHAFFOTTE Alain / Dr CORDIER Florence / Dr GUIJARRO Inaki
GUILLIÈRE Florence / Dr IZADI-PRUNEYRE Nadia / Dr LECROISEY Anne
LEFÈVRE Julien / Dr PROCHNICKA-CHALUFOUR Ada / SIMENEL Catherine
THEILLLET François-Xavier / Dr WECKER Karine / Dr WOLFF Nicolas


  Annual Report

Our research area is mainly dedicated to the structure determination of proteins, peptides, nucleic acids and oligosaccharides, in relation to their function but also to molecular interactions studies. The driving force is to adapt NMR techniques to biological problems. How can NMR be used to answer a peculiar biological question and is NMR the only tool to answer it? Thus, not only modern NMR techniques are employed but also different biophysical approaches are used.

Structural and functional studies of bacterial proteins involved in heme acquisition

Several pathogenic gram-negative bacteria use a heme uptake system involving an extracellular heme-binding protein called hemophore that acquires free or hemoprotein-bound heme and transfers it to its specific outer membrane receptor, via protein-protein interaction. Over the years we have been involved in the molecular characterization of all steps of the mechanism at both structural and functional levels, from the hemophore secretion, to heme delivery to the cell via the heme uptake and release to the receptor. In particular the hemophore’s structures in the holo and apo forms have been solved as well that of its dimeric form.

genic determinants recognized by a protective monoclonal antibody in view of developing a vaccine against shigellosis

A possible strategy for human vaccination against shigellosis is to develop synthetic chemically defined vaccines with simple molecules able to mimic the O-SP that would induce the synthesis of protective antibodies. The conformations and the epitopes of oligosaccharides from O-SP of two different serotypes, 5a and 2a, free and bound to protective monoclonal have been characterized.

Structure and function of transcription regulators from hyperthermophile-Archaea viruses

Hyperthermophile-archaea viruses show an exceptional diversity and are very different from viruses that infect bacteria and eukaryotes. Study of the structure and function of proteins that could be involved in transcription regulation has been initiated. The first protein studied, D56, belongs to the virus Sulfolobus islandicus rudivirus and is expressed throughout the infection cycle of the virus. It interacts specifically with the regions of its own promoter and of the promoter of a neighboring gene. The protein forms a dimer.

Structural and functional study of NEMO, a regulatory protein of the NF-κB pathway

NEMO is a central regulatory protein of the NF-κB signaling pathway, involved in early inflammatory and immune responses and in regulation of apoptosis. In order to understand the molecular mechanism by which NEMO participates in NF-κB activation and to facilitate the elaboration of anti-inflammatory and anti-cancer drugs, we are studying the biophysical, structural and functional characteristics of the C-terminal regulatory domains of NEMO and their interactions with biological partners and with small inhibitory molecules.



  Web Site

More informations on our web site


  Publications

Publications 2006 of the unit on Pasteur's references database




Activity Reports 2006 - Institut Pasteur
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