Understanding the structural basis of protein assemblies that are functionally important for various aspects of cell contacts with its microenvironment.

Cell contacts with the microenvironment orchestrate the development of organisms, homeostasis, and the functions of individual cells. When cells do not interact correctly or decode external molecular messages incorrectly, cellular responses are disturbed, and diseases can develop.

Therefore, understanding the structural basis of protein assemblies involved in the sophisticated mechanisms of action developed by cells to interact/communicate with their microenvironment is of main importance.

Our research is focused on the study of these membrane-associated protein complexes. The primary focus of our research is on how human Galectins interactions are regulated at the cell surface during cell-cell interactions.

This study involves protein-protein as well as protein-carbohydrates interactions. We also seek to understand the mechanisms regulating bacterial cell motility from structural studies of focal adhesion protein complexes in M. xanthus.

Exemple of structural investigations performed in the group on cell-cell interactions involving Galectin-1 during B cell development in the bone marrow
(Elantak et al. 2012, Bonzi et al. 2015).

To pursue our goals, we use Nuclear Magnetic resonance (NMR) spectroscopy combined with biochemical and biophysical techniques in an integrated structural biology approach. NMR can provide an atomic-level view of the structure and dynamics of macromolecular systems in solution. A particular strength of NMR is its ability to reveal the structural details of specific interactions between biological macromolecules, even in the case of transient complexes between proteins and their targets in solution.

Overall, our aim is to decipher at atomic level the assembly of multi-protein complexes, determine their structures, gain insight into their activities and regulation, and identify roles for proteins or domains of unknown function.

Publications

2022
1H, 13C and 15N chemical shift assignments of the ZnR and GYF cytoplasmic domains of the GltJ protein from Myxococcus xanthus

Bouchra Attia, Bastien Serrano, Olivier Bornet, Françoise Guerlesquin, Laetitia My, Jean-Philippe Castaing, Tâm Mignot, Latifa Elantak

Biomolecular NMR Assignments 16:219-223 (2022)10.1007/s12104-022-10083-6

2022
FrzS acts as a polar beacon to recruit SgmX , a central activator of type IV pili during Myxococcus xanthus motility

Sarah Bautista, Victoria Schmidt, Annick Guiseppi, Emillia M F Mauriello, Bouchra Attia, Latifa Elantak, Tâm Mignot, Romain Mercier

EMBO Journal e111661 (2022)10.15252/embj.2022111661

2022
Identification of the three zinc-binding sites on tau protein

Romain Rocca, Philipp O Tsvetkov, Andrey Golovin, Diane Allegro, Pascale Barbier, Soazig Malesinski, Françoise Guerlesquin, François Devred

International Journal of Biological Macromolecules 209:779-784 (2022)10.1016/j.ijbiomac.2022.04.058

2021
Glutamate optimizes enzymatic activity under high hydrostatic pressure in Desulfovibrio species: effects on the ubiquitous thioredoxin system

Hélène Gaussier, M. Nouailler, Edouard Champaud, Edwige Garcin, Sebban -Kreuzer, Olivier Bornet, Marc Garel, Christian Tamburini, Laetitia Pieulle, Alain Dolla, Nathalie Pradel

Extremophiles 25:385-392 (2021)10.1007/s00792-021-01236-x

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2020
The unusual structure of Ruminococcin C1 antimicrobial peptide confers clinical properties

Clarisse Roblin, Steve Chiumento, Olivier Bornet, Matthieu Nouailler, Christina S. Müller, Katy Jeannot, Christian Basset, Sylvie Kieffer-Jaquinod, Yohann Couté, Stéphane Torelli, Laurent Le pape, Volker Schünemann, Hamza Olleik, Bruno de La Villeon, Philippe Sockeel, Eric Di Pasquale, Cendrine Nicoletti, Nicolas Vidal, Leonora Poljak, Olga Iranzo, Thierry Giardina, Michel Fons, Estelle Devillard, Patrice Polard, Marc Maresca, Josette Perrier, Mohamed Atta, Francoise Guerlesquin, Mickaël Lafond, Victor Duarte

Proceedings of the National Academy of Sciences of the United States of America 120:e2302405120 (2020)10.1073/pnas.2302405120

2019
Deciphering the specific interaction between the acyl carrier protein IacP and the T3SS‐major hydrophobic translocator SipB from Salmonella

Mickaël J Canestrari, Bastien Serrano, Julia Bartoli, Valerie Prima, Olivier Bornet, Rémy Puppo, Emmanuelle Bouveret, Francoise Guerlesquin, Julie Viala

FEBS Letters (2019)10.1002/1873-3468.13593

2019
Ruminococcin C, a promising antibiotic produced by a human gut symbiont

Steve Chiumento, Clarisse Roblin, Sylvie Kieffer-Jaquinod, Sybille Tachon, Chloé Leprêtre, Christian Basset, Dwi Aditiyarini, Hamza Olleik, Cendrine Nicoletti, Olivier Bornet, Olga Iranzo, Marc Maresca, Renaud Hardré, Michel Fons, Thierry Giardina, Estelle Devillard, Françoise Guerlesquin, Yohann Couté, Mohamed Atta, Josette Perrier, Mickael Lafond, Victor Duarte

Science Advances 5:eaaw9969 (2019)10.1126/sciadv.aaw9969

2017
Electrostatic interactions between the CTX phage minor coat protein and the bacterial host receptor TolA drive the pathogenic conversion of Vibrio cholerae

Laetitia Houot, Romain Navarro, Matthieu Nouailler, Denis Duché, Francoise Guerlesquin, Roland Lloubès

Journal of Biological Chemistry 292:13584-13598 (2017)10.1074/jbc.M117.786061

2017
1H, 13C and 15N assignments of the C-terminal intrinsically disordered cytosolic fragment of the receptor tyrosine kinase ErbB2

Yinghui Wang, Louise Pinet, Nadine Assrir, Latifa Elantak, Francoise Guerlesquin, Ali Badache, Ewen Lescop, Carine van Heijenoort

Biomolecular NMR Assignments 12:23-26 (2017)10.1007/s12104-017-9773-4

2016
(1)H, (15)N and (13)C resonance assignments of the C-terminal domain of Vibrio cholerae TolA protein.

Romain Navarro, Olivier Bornet, Laetitia Houot, Roland Lloubes, Francoise Guerlesquin, Matthieu Nouailler

Biomol NMR Assign (2016)10.1007/s12104-016-9690-y

2015
Pre-B cell receptor binding to galectin-1 modifies galectin-1/carbohydrate affinity to modulate specific galectin-1/glycan lattice interactions

Jeremy Bonzi, Olivier Bornet, Stéphane Betzi, Brian T Kasper, Lara K Mahal, Stéphane Mancini, Claudine Schiff, Corinne Sebban-Kreuzer, Francoise Guerlesquin, Latifa Elantak

Nature Communications 6:6194 (2015)10.1038/ncomms7194

2015
Examination of galectin-induced lattice formation on early B-cell development.

Stephane J C Mancini, Latifa El Antak, Annie Boned, Marion Espeli, Francoise Guerlesquin, Claudine Schiff

Methods in Molecular Biology 1207:169-84 (2015)10.1007/978-1-4939-1396-1_11

2014
Identification of a Src kinase SH3 binding site in the C-terminal domain of the human ErbB2 receptor tyrosine kinase.

Olivier Bornet, Matthieu Nouailler, Michaël Feracci, Corinne Sebban-Kreuzer, Deborah Byrne, Hubert Halimi, Xavier Morelli, Ali Badache, Francoise Guerlesquin

FEBS Letters 588:2031-6 (2014)10.1016/j.febslet.2014.04.029

2014
1H, 13C and 15N backbone and side-chain chemical shift assignments for reduced unusual thioredoxin Patrx2 of Pseudomonas aeruginosa.

Edwige B Garcin, Olivier Bornet, Latifa El Antak, Matthieu Nouailler, Francoise Guerlesquin, Corinne Sebban-Kreuzer

Biomol NMR Assign 8:247-50 (2014)10.1007/s12104-013-9493-3

2014
Glycan Dependence of Galectin-3 Self-Association Properties

Hubert Halimi, Annafrancesca Rigato, Deborah Byrne, Géraldine Ferracci, Corinne Sebban-Kreuzer, Latifa Elantak, Francoise Guerlesquin

PLoS ONE 9:e111836 (2014)10.1371/journal.pone.0111836

2012
Structural Basis for Galectin-1-dependent Pre-B Cell Receptor (Pre-BCR) Activation

Latifa Elantak, Marion Espeli, Annie Boned, Olivier Bornet, Jeremy Bonzi, Laurent Gauthier, Mikael Feracci, Philippe Roche, Francoise Guerlesquin, Claudine Schiff

Journal of Biological Chemistry 287:44703-44713 (2012)10.1074/jbc.m112.395152

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Collaborations

  • National
    • Tâm Mignot, LCB UMR7283, Marseille
    • Romain Mercier, LCB UMR7283, Marseille
    • Stephane Mancini, Rennes
    • Guido Pintacuda, Lyon
  • International
    • Victor Thijssen, Amsterdam
    • Daniel Abankwa, Luxembourg
    • Lincoln Scott, San Diego

Funding

© 2024 LISM - Laboratoire d'Ingénierie des Systèmes Macromoléculaires - CNRS UMR7255

31 Chemin Joseph Aiguier, 13402 Marseille cedex 20, France