Proteomics and Mass Spectrometry of Biomolecules

Picture of Odile Schiltz
Odile Schiltz

Group Leader

The objective of the group is to develop efficient strategies in mass spectrometry (MS)-based proteomics and structural MS, associated to dedicated bioinformatics tools, to obtain new insights into protein function, regulation and dynamics. Our main projects focus on studying the role of proteasome, characterizing mycobacterial proteins, and deciphering signaling pathways in immune cells.

We are expert in large-scale quantitative proteomics, structural mass spectrometry, and bioinformatics for the in depth study of proteomes and signaling pathways, and for the characterization of pivotal proteins and protein complexes, like the proteasome.

Proteomics and structural MS represent complementary and powerful approaches for the understanding of complex biological systems. MS is a key technology in proteomic strategies offering various platforms with specific capabilities continuously improving in terms of sensitivity, mass resolution and acquisition speed. Major advances in proteomics and structural MS can also be attributed to the optimization of biochemical protocols and analytical methods for sample preparation before data acquisition, and to the development of sophisticated bioinformatics software for efficient data analysis. Based on our expertise in MS and proteomics, research projects are pursued to characterize several biological systems.

Role of human proteasome complexes

We are interested in understanding the structure/activity relationships of human proteasome, a large multi-catalytic complex in charge of intracellular protein degradation and a therapeutic target for some cancers. We developed integrated strategies using in-vivo crosslinking, affinity-purification and quantitative proteomics to characterize the diversity of proteasome complexes and their dynamics in various cells, physiological and pathological contexts. We also designed an MS-based quantitative method to measure the quantities of several proteasome subtypes in patient samples. We then optimized structural MS approaches to determine the structural features that govern protein-protein interactions and allosteric changes during proteasome association to its regulatory protein complexes.


We developed efficient large-scale quantitative proteomic analyses (interactomics, phosphoproteomics) to obtain a detailed characterization of different cells from the adaptative and innate immune systems. This further permits us to get new insights into the molecular mechanisms of the inflammatory and immune responses. Major efforts have been invested to decipher, at the cellular and molecular levels, the functional mechanisms of T lymphocytes. We analysed in mouse primary T cells the signalosome of several key components of the TCR pathway using optimized interactomics and phosphoproteomics strategies.

Characterization of mycobacterial proteins

We are interested in the characterization of proteins and protein complexes that play a role in the formation of the mycomembrane and in the targeting of proteins to the plasma membrane, mycomembrane and extracellular medium. We also developed an expertise in the analysis of O-mannosylated proteins in mycobacteria to study their implication in the virulence of Mycobacterium tuberculosis.

Team members

Research Scientists

François Amalric (Emeritus)
Marie-Pierre Bousquet (University)
Manuelle Ducoux (University)
Anne Gonzalez de Peredo (CNRS)
Christel Lutz (University)
Julien Marcoux (CNRS)
Odile Schiltz (CNRS)

Research Engineers

Renaud Albigot (CNRS)
David Bouyssié (CNRS)
Marie Locard-Paulet (CNRS)
Emmanuelle Mouton (University)

Postdoctoral Fellows

Angelique Dafun
Paulo Espirito-Santo

PhD Students

Rim Abderrahim
Pinar Altiner
Amélie Bosc-Rosati
Maurine Marteau
Ronald Siaden-Ortega
Zoltán Udvardy

Our research projects

Role of human proteasome complexes


Characterization of mycobacterial proteins

Lesne et al. (2020) Conformational maps of human 20S proteasomes reveal PA28- and immuno-dependent inter-ring crosstalks. Nat Commun

Bouyssié et al. (2020) Proline: an efficient and user-friendly software suite for large-scale proteomics. Bioinformatics

Locard-Paulet et al. (2020) LymphoAtlas: a dynamic and integrated phosphoproteomic resource of TCR signaling in primary T cells reveals ITSN2 as a regulator of effector functions. Mol Syst Biol

Tonini et al. (2020) Potential plasticity of the mannoprotein repertoire associated to Mycobacterium tuberculosis virulence unveiled by mass spectrometry-based glycoproteomics. Molecules

Zivkovic et al. (2022) Proteasome complexes experience profound structural and functional rearrangements throughout mammalian spermatogenesis. Proc Natl Acad Sci USA

Voisinne et al. (2022) Kinetic proofreading through the multi-step activation of the ZAP70 kinase underlies early T cell ligand discrimination. Nat Immunol

Using high-throughput phosphoproteomic methods, we can monitor the phosphorylation kinetics of thousands of phosphosites during the first 10min following TCR engagement in primary T lymphocytes. (Illustration by SciStories-