Our research projects focus on the structural and functional characterization of bacterial tyrosine-kinases (BYK) and serine/threonine-kinases (STKP).
My group has pioneered the studies of protein phosphorylation in bacteria on hydroxyl amino acids. More precisely, we were the first to biochemically and genetically characterize a tyrosine-kinase activity in a bacterium and we also strongly contributed to the description of their cellular roles and to the understanding of their structural features (in E. coli and S. aureus). Recently, we have also initiated studies devoted to another type of bacterial-kinases that share resemblance with eukaryotic-kinases (STPK) and we have shown that they play a crucial role in cytokinesis and morphogenesis of the human pathogen S. pneumoniae.
Recently, global analysis of bacterial phosphoproteomes led to the publication of long lists of bacterial proteins phosphorylated on serine, threonine and tyrosine suggesting crosstalk between BYK and STPK signaling pathways. Therefore, major challenges are now to tackle the bacterial kinase interaction networks (substrates and partners possibly regulating the kinase activity), to integrate all functional components into signaling pathways and to determine their biological functions. Our long-term interest is in reconstruction of bacterial dynamic phosphorylation networks involving S/T/Y phosphorylation to better understand the inner workings of the bacterial cell and the global bacterial response and adaptation to its environment.

In applied terms, our study is expected to open new avenues towards specific inhibition of these bacterial protein kinases and thus pave the way towards the search for efficient inhibitors that could constitute promising leads for future antibiotics.

Key words: Molecular Microbiology, Streptococcus pneumoniae, S/T/Y-protein-kinases, Protein phosphorylation, Cell division, Morphogenesis, Peptidoglycan and cell wall, Kinases inhibitors