Directrice de Recherche, CNRS

+33 4 91 16 45 49

Equipe / Group: BIP 02

We are interested in the proteins that regulate CO2 assimilation in microalgae and diatoms, and more specifically in Intrinsically disordered proteins (IDPs). These proteins are fascinating because they fulfill essential biological functions while lacking a stable ordered structure, whereas it was long thought that a well folded structure was an absolute prerequesite for the proper activity of proteins. Instead, they are highly dynamics and adopt a myriad of conformations in the cell. We now know that no less than 30% of the proteins encoded by eukaryotic genomes contain long disordered regions. They are often involved in multiple interactions fostered by their structural plasticity. Encounter with their partners is often accompanied by dramatic changes in the structure and dynamics of these IDPs.
We have developed an expertise in the study of these original proteins and of their mechanisms of action by combining a series of complementary biophysical techniques. We are in particular expert in Small Angle X-ray Scattering (SAXS) and Small Angle Neutron Scattering (SANS), two very powerful techniques that provide crucial information on the structural properties of flexible polypeptide chains and on their distribution of conformations. We use SAXS, in combination with data from X-ray crystallography, NMR, circular dichroism and molecular modelling, to assess the structure and dynamics of IDPs, when free in various solution conditions, and when they undergo large conformational changes upon interaction with their partner(s).

ORCID id: 0000-0002-7464-6192


Hui Shao, Wenmin Huang, Luisana Avilan, Véronique Receveur-Bréchot, Carine Puppo, Rémy Puppo, Régine Lebrun, Brigitte Gontero, Hélène Launay.
A new type of flexible CP12 protein in the marine diatom Thalassiosira pseudonana.
Cell Commun Signal, 2021, 19 (1). DOI: 10.1186/s12964-021-00718-x HAL: hal-03194815

Helene Launay, Hui Shao, Olivier Bornet, Francois-Xavier Cantrelle, Regine Lebrun, Veronique Receveur-Brechot, Brigitte Gontero.
Flexibility of Oxidized and Reduced States of the Chloroplast Regulatory Protein CP12 in Isolation and in Cell Extracts.
Biomolecules, 2021, 11 (5), 701 -. DOI: 10.3390/biom11050701 HAL: hal-03194824


Hélène Launay, Véronique Receveur-Bréchot, Frédéric Carrière, Brigitte Gontero.
Orchestration of algal metabolism by protein disorder.
Archives of Biochemistry and Biophysics, 2019, 672, 108070 -. DOI: 10.1016/j.abb.2019.108070 HAL: hal-02266032v1


Hélène Launay, Patrick Barré, Carine Puppo, Yizhi Zhang, Stéphanie Maneville, Brigitte Gontero, Véronique Receveur-Bréchot.
Cryptic Disorder Out of Disorder: Encounter between Conditionally Disordered CP12 and Glyceraldehyde-3-Phosphate Dehydrogenase.
Journal of Molecular Biology, 2018, 430 (8), 1218 - 1234. DOI: 10.1016/j.jmb.2018.02.020 HAL: hal-01794097v1


Aurelie Badillo, Véronique Receveur-Brechot, Stéphane Sarrazin, François-Xavier Cantrelle, Frédéric Delolme, Marie-Laure Fogeron, Jennifer Molle, Roland Montserret, Anja Bockmann, Ralf Bartenschlager, Volker Lohmann, Guy Lippens, Sylvie Ricard-Blum, Xavier Hanoulle, François Penin.
Overall Structural Model of NS5A Protein from Hepatitis C Virus and Modulation by Mutations Confering Resistance of Virus Replication to Cyclosporin A.
Biochemistry, 2017, 56 (24), 3029 - 3048. DOI: 10.1021/acs.biochem.7b00212 HAL: hal-01785410v1


Hélène Launay, Patrick Barré, Carine Puppo, Stéphanie Manneville, Brigitte Gontero, Véronique Receveur-Bréchot.
Absence of residual structure in the intrinsically disordered regulatory protein CP12 in its reduced state.
Biochemical and Biophysical Research Communications, 2016, 477 (1), 20 - 26. DOI: 10.1016/j.bbrc.2016.06.014 HAL: hal-01430932v1

Rodrigo Arias-Cartin, Pierre Ceccaldi, Barbara Schoepp-Cothenet, Klaudia Frick, Jean-Michel Blanc, Bruno Guigliarelli, Anne Walburger, Stéphane Grimaldi, Thorsten Friedrich, Véronique Receveur-Brechot, Axel Magalon.
Redox cofactors insertion in prokaryotic molybdoenzymes occurs via a conserved folding mechanism.
Sci Rep, 2016, 12 (1), 543 -. DOI: 10.1038/srep37743 HAL: hal-01415067v1

Shishir P. S. Chundawat, Chad D. Paavola, Babu Raman, Matthieu Nouailler, Suzanne L. Chan, Jonathan R. Mielenz, Veronique Receveur-Brechot, Jonathan D. Trent, Bruce E. Dale.
Saccharification of thermochemically pretreated cellulosic biomass using native and engineered cellulosomal enzyme systems.
React. Chem. Eng., 2016, 16 (5), 577 - 628. DOI: 10.1039/c6re00172f


Pierre Roblin, Pierre Lebrun, Prakash Rucktooa, Frederique Dewitte, Zoe Lens, Véronique Receveur-Brechot, Vincent Raussens, Vincent Villeret, Coralie Bompard.
The structural organization of the N-terminus domain of SopB, a virulence factor of Salmonella, depends on the nature of its protein partners.
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2013, 1834 (12), 2564 - 2572. DOI: 10.1016/j.bbapap.2013.09.014


Mirjam Czjzek, Henri-Pierre Fierobe, Véronique Receveur-Bréchot.
Chapter ten - Small-Angle X-ray Scattering and Crystallography: A Winning Combination for Exploring the Multimodular Organization of Cellulolytic Macromolecular Complexes.
Methods in Enzymology, 2012, 510, 183 - 210. DOI: 10.1016/B978-0-12-415931-0.00010-0

Veronique Receveur-Brechot, Dominique Durand.
How Random are Intrinsically Disordered Proteins? A Small Angle Scattering Perspective.
CPPS, 2012, 13 (1), 55 - 75. DOI: 10.2174/138920312799277901

Gary W. Daughdrill, Stepan Kashtanov, Amber Stancik, Shannon E. Hill, Gregory Helms, Martin Muschol, Véronique Receveur-Bréchot, F. Marty Ytreberg.
Understanding the structural ensembles of a highly extended disordered protein.
Mol. BioSyst., 2012, 19 (S3), 109 - 319. DOI: 10.1039/c1mb05243h


Virginie Moucadel, Renaud Prudent, Céline F. Sautel, Florence Teillet, Caroline Barette, Laurence Lafanechere, Veronique Receveur-Brechot, Claude Cochet.
Antitumoral activity of allosteric inhibitors of Protein kinase CK2.
Oncotarget, 2011, 2 (12). DOI: 10.18632/oncotarget.361

Eric Durand, Gabriel Waksman, Veronique Receveur-Brechot.
Structural insights into the membrane-extracted dimeric form of the ATPase TraB from the Escherichia coli pKM101 conjugation system.
BMC Structural Biology, 2011, 11 (1), 4 -. DOI: 10.1186/1472-6807-11-4

Anne-Laure Molinier, Matthieu Nouailler, Odile Valette, Chantal Tardif, Véronique Receveur-Bréchot, Henri-Pierre Fierobe.
Synergy, Structure and Conformational Flexibility of Hybrid Cellulosomes Displaying Various Inter-cohesins Linkers.
Journal of Molecular Biology, 2011, 405 (1), 143 - 157. DOI: 10.1016/j.jmb.2010.10.013


Marine Foucault, Katia Mayol, Véronique Receveur-Bréchot, Marie-Claire Bussat, Christine Klinguer-Hamour, Bernard Verrier, Alain Beck, Richard Haser, Patrice Gouet, Christophe Guillon.
UV and X-ray structural studies of a 101-residue long Tat protein from a HIV-1 primary isolate and of its mutated, detoxified, vaccine candidate.
Proteins, 2009, 293, 321 - NA. DOI: 10.1002/prot.22661 HAL: hal-02121744v1


Guillaume K. Sonan, Véronique Receveur-Brechot, Colette Duez, Nushin Aghajari, Mirjam Czjzek, Richard Haser, Charles Gerday.
The linker region plays a key role in the adaptation to cold of the cellulase from an Antarctic bacterium.
2007, 22 (2), 4673 - 302. DOI: 10.1042/BJ20070640 HAL: hal-00478802v1


Guy Schoehn, Frédéric M. D. Vellieux, M. Asunción Durá, Véronique Receveur-Bréchot, Céline M. S. Fabry, Rob W. H. Ruigrok, Christine Ebel, Alain Roussel, Bruno Franzetti.
An Archaeal Peptidase Assembles into Two Different Quaternary Structures.
J. Biol. Chem., 2006, 40 (47), 7035 - 36337. DOI: 10.1074/jbc.M604417200 HAL: hal-00475651v1

Véronique Receveur-Bréchot, Mirjam Czjzek, Annick Barre, Alain Roussel, Willy J. Peumans, Els J.M. Van Damme, Pierre Rougé.
Crystal structure at 1.45-Å resolution of the major allergen endo-β-1,3-glucanase of banana as a molecular basis for the latex-fruit syndrome.
Proteins, 2006, 20 (1), 513 - 242. DOI: 10.1002/prot.20876 HAL: hal-00475655v1

Gross M, Receveur-Bréchot V.
Les protéines humaines.
La Recherche, Hors-Série « La biologie en 18 mots clés », 2006.


Véronique Receveur-Bréchot, Jean-Marie Bourhis, Vladimir N. Uversky, Bruno Canard, Sonia Longhi.
Assessing protein disorder and induced folding.
Proteins, 2005, 415 (Pt 12), 549 - 45. DOI: 10.1002/prot.20750

Receveur-Bréchot V, Karlin D.
Le désordre, clé de voûte des protéines.
La Recherche, 2005.


Receveur-Bréchot V, Gross M.
Protéines de stress au front contre le cancer..
Biofutur, 2004, 244 (13).


Gross M, Receveur V.
Les protéines humaines.
La Recherche, 2000.


Gross M, Receveur V.
Le repliement raté des protéines.
La Recherche, 1999.