Daniel Ladant

This project aims to describe the hydrodynamic and thermodynamic properties of the CyaA toxin and the conformational changes it undergoes during its translocation process across the lipid membranes of Bordetella pertussis (secretion) and of […]

We are interested in investigating the effects of molecular crowding, i.e., excluded volume effects, mimicking the effects of high concentrations of macromolecular solutes found in biological fluids on biochemical properties of proteins. In particular, […]

CyaA-based therapeutic cancer vaccines Based on our discovery that a bacterial protein, the adenylate cyclase (CyaA), binds to dendritic cells (DCs), we have developed a highly efficient vector capable of targeting a wide range […]

CyaA, a 1706 residue-long protein, is one of the major virulence factors produced by B. pertussis and plays an important role in the early stages of respiratory tract colonization. This toxin uses an original […]

  Other research projects are aimed at exploring the regulatory role of different nucleotides such ppGpp and pppGpp that are both thought to act as second messengers in many complex cellular responses to nutritional […]

  A second main line of research of the team is focused on the characterization of protein-protein interactions by exploiting a bacterial two-hybrid screening technology (BACTH) that we have previously developed (Karimova et al., […]

  From an applied perspective, we have shown in collaboration with the team of C. Leclerc, (Immune Regulation and Vaccinology, Institut Pasteur) that CyaA can be engineered to serve as a potent non-replicating vector […]

  The CyaA toxin is a 1706 residues-long bifunctional protein (Figure 1): the calmodulin-activated, catalytic domain is located in the 400 amino-proximal residues, whereas the carboxy-terminal 1306 residues are responsible for the binding of […]