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Institut Pasteur de Lille
Université Lille Nord de France
00 33 3 20 33 72 41 / 00 33 3 20 87 73 07

2007 | 2008 | 2009 | 2010
Group members
BONACHERA Fanny | FRITZINGER Bernd | HANOUILLE Xavier | LANDRIEU Isabelle | LEROY Arnaud | LIPPENS Guy |SIBILLE Nathalie | SMET Caroline | TRIVELLI Xavier | WIERUSZESKI Jean-Michel
Students : AMNIAI Laziza | DACCACHE Anthony


1] Mission of the facility
Give acces to Nuclear Magnetic Resonance for the analysis of molecules coming from organic synthesis, and for biomolecules.

2] Description of the facility
The facility is composed of two spectrometers, one at 300MHz and one at 600MHz. Small organic molecules coming from the organic chemistry groups from the campus are analysed with the 300MHz. The operator, Mme E. Boll (Technicienne CNRS) will acquire the spectra, process them and give a paper trace from the resulting spectra The 600MHz spectrometer is mainly used for applications in the field of structural and analytical biochemistry and biology. Equiped with a cryogenic probe head, whereby noise in the probe head is limited to obtain a superior sensitivity, the spectrometer can analyse biomolecules at concentrations down to the low micromolar range. For the 600MHz, with Dr. J.-M. Wieruszeski (IR1 CNRS) as person in charge, not only the data acquisition but equally the interpretation of the biomolecular spectra is itself quite specialized. The majority of the projects hence involve a collaboration with the interested biochemists. After defining the problem in terms of spectroscopy and an agreement on sample preparation (that often involves the incorporation of stable isotopes in the biomolecule), the facility will record the NMR spectra and interpret them in order to obtain the tridimensional structure of the biomolécule.
The NMR facility of the Campus equally has access to the 800MHz spectrometer at the University of Lille I, and also to the recently installed 900MHz installed in November 209 at the Haute Borne Campus in Villeneuve d’Ascq. The former spectrometer is equipped for a dual use in liquid and solid state NMR, and has two different High Resolution Magic Angle Spinning probe heads. It is therefore particularly well suited for the study of heterogeneous samples such as intact bacteria. The latter has a cryogenic probe head installed, and thus gives the supreme resolution and sensitivity.

3] Projects
The 300MHz spectrometer performs mainly the analysis of small organic molecules coming from the chemistry groups on campus. The field of study of the 600MHz spectrometer ranges from the structural analysis of proteins in solution, the identification of complex sugar motifs, the elucidation of posttranscriptional modifications such as phosphorylation, … The detection and quantification of biomolecular interactions is a well established and important application of the NMR facility.
Projets in collaboration with other groups of the campus Calmette involve the study of the natively unfolded tail of the Mycobacterial heparin binding hemaglutinin, with its possible post-translational modifications (PTMs) (collaboration with Dr D Raze and Dr C Locht), the study of the inhibitor of the PP1 phosphatase of Plasmodium falciparum (collaboration with Dr J Khalife) and a novel prolyl cis/trans isomerase from B pertussis (collaboration with Dr F Jacob-Dubuisson). He group itself is centered on the neuronal protein Tau and its PTMs, and equally on the study of the natively unfolded NS5A protein of Hepatitis C.




B, Wieruszeski JM, Lippens G.
Spectroscopic studies of GSK3{beta} phosphorylation of the neuronal tau protein and its interaction with the N-terminal domain of apolipoprotein E. Leroy A, Landrieu I, Huvent I, Legrand D, Codeville
J Biol Chem. 2010 Aug 2. [Epub ahead of print]

Landrieu I, Leroy A, Smet-Nocca C, Huvent I, Amniai L, Hamdane M, Sibille N, Buée L, Wieruszeski JM, Lippens G.
2.NMR spectroscopy of the neuronal tau protein : normal function and implication in Alzheimer's disease.
Biochem Soc Trans. 2010 Aug;38(4):1006-11.

Landrieu I, Hanoulle X, Bonachera F, Hamel A, Sibille N, Yin Y, Wieruszeski JM, Horvath D, Wei Q, Vuagniaux G, Lippens G.
Structural basis for the non-immunosuppressive character of the cyclosporin A analogue Debio 025.
Biochemistry. 2010 Jun 8;49(22):4679-86.


Amniai L, Barbier P, Sillen A, Wieruszeski JM, Peyrot V, Lippens G, Landrieu I.
Alzheimer disease specific phosphoepitopes of Tau interfere with assembly of tubulin but not binding to microtubules.
FASEB J, 2009, 23:1146-1152.

Hanoulle X, Badillo A, Wieruszeski JM, Verdegem D, Landrieu I, Bartenschlager R, Penin F, Lippens G.
Hepatitis C virus NS5A protein is a substrate for the Peptidyl-Prolyl cis/trans isomerase activity of Cyclophilins A and B.
J Biol Chem, 2009, 284:13589-13601.


Bodart JF, Wieruszeski JM, Amniai L, Leroy A, Landrieu I, Rousseau- Lescuyer A, Vilain JP, Lippens G.
NMR observation of Tau in Xenopus oocytes.
J Magn Reson, 2008, 192:252-257.

Hodak H, Wohlkönig A, Smet-Nocca C, Drobecq H, Wieruszeski JM, Sénéchal M, Landrieu I, Locht C, Jamin M, Jacob-Dubuisson F.
The peptidyl-prolyl isomerase and chaperone Par27 of Bordetella pertussis as the prototype for a new group of parvulins.
J Mol Biol, 2008, 376:414-426.

Rodius S, Chaloin O, Moes M, Schaffner-Reckinger E, Landrieu I, Lippens G, Lin M, Zhang J, Kieffer N.
The Talin Rod IBS2 {alpha}-Helix Interacts with the {beta}3 Integrin Cytoplasmic Tail Membrane-proximal Helix by Establishing Charge Complementary Salt Bridges.
J Biol Chem, 2008, 283:24212-24223.

Wieruszeski JM, Fritzinger B, Hanoulle X, Martins JC, Lippens G.
Sandwich-ELISE NMR: Reducing the sample volume of NMR samples.
J Magn Reson, 2008, 193:37-40.


Sillen A, Barbier P, Landrieu I, Lefebvre S, Wieruszeski JM, Leroy A, Peyrot V, Lippens G.
NMR investigation of the interaction between the neuronal protein tau and the microtubules.
Biochemistry, 2007, 46:3055-64.



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