2011- :Head of the Group “Immune response to pathogens and altered-self” and of the Team “Innate Immune proteins at the host-pathogen interface” at the Institute for Structural Biology (IBS) of Grenoble
2009-2010: Head of the Laboratory of Molecular Enzymology (LEM) at the IBS
1992-2008: Research scientist at LEM/IBS; responsible for the “Complement lectin pathway” team since 1998 (INSERM Research Director since 2005)
1986-1987: Post-doctoral fellow, Laboratory of Structural Biology, University of Florida, Gainesville
1978-1992: Immunochemistry Laboratory of the CEA-Grenoble (PhD student, post-doc, then INSERM research scientist (CR))
We are interested in soluble innate immune recognition proteins (the defence collagens C1q, mannan-binding lectin (MBL) and ficolins), which play a crucial role by sensing the extracellular environment and activating effector mechanisms involved in the clearance of pathogens and damaged host cells. Although these proteins have different recognition specificities, their common hallmark is the ability to trigger the complement cascade through activation of associated homologous proteases. They also act as bridging molecules through interaction with various cell surface molecules thereby facilitating phagocytosis of the targets. These effector mechanisms are subverted by certain pathogens which use molecular mimicry to evade the host innate immune system.
Our main objective is to better understand the molecular interplay of C1q, MBL and ficolins at the host-pathogen interface, through the structural and functional analysis of the interactions involved in (i) pathogen recognition, (ii) immune effector mechanisms (iii) subversion strategies used by pathogens. This understanding is crucial for the future development of novel therapeutic or vaccinal strategies.