You hold a PhD (or are completing one) in biological mass spectrometry, proteomics, or structural biology, with demonstrated expertise in LC–MS/MS sample preparation and data analysis. While hands-on experience in cross-linking mass spectrometry (XL–MS) or structural proteomics is a strong advantage, it is not mandatory—we provide extensive, tailored training. You are collaborative, independent, and eager to push methodological boundaries. Strong English communication skills are required; French lessons are offered to support your integration.
Cross-linking mass spectrometry has emerged as an innovative and powerful technique for investigating protein–protein interactions. A small chemical linker serves to covalently link two interacting protein sites, preserving critical information about their spatial interaction. Advanced mass spectrometric analysis serves to detect and interpret cross-linked peptides, providing detailed insights into the specific domains and regions involved in protein interactions. In recent years, the field has moved from the analysis of purified complexes to proteome-wide studies thanks to fundamental instrumental and bioinformatic advancements. In this project, we aim to develop cutting-edge XL–MS methods to elucidate the structural organization of protein complexes critical to microbial virulence. We focus on studying the type VI secretion system of enteroaggregative E. coli, the type IV piliation machinery of Neisseria meningitidis, and rhoptry exocytosis signaling in Toxoplasma gondii. These protein complexes represent major targets for understanding bacterial competition, host cell adhesion, and protozoan invasion mechanisms.