Biochemistry of Macromolecular Interactions
Biochemistry of Macromolecular Interactions - Daniel LADANT
Activities of the Unit
Our research interests are focused on the study of the molecular mechanisms that underlie protein-protein and protein-membrane interactions, using as a model system a bacterial toxin, the adenylate cyclase (CyaA) produced by Bordetella pertussis. CyaA has an original mode of invasion of eukaryotic target cells and besides it is an efficient vaccine vehicle to induce specific cell-mediated immune responses. Our goal is to unravel the biochemical and biophysical basis of these processes. We are also exploiting a CyaA-based two-hybrid screening technology, previously developed in our group, to study the assembly of multi-molecular membrane-associated protein machineries.
1. G. Karimova, C. Robichon, D. Ladant (2009) Characterisation of YmgF, a 72 residue-long inner membrane protein that associates to the Escherichia coli cell division machinery. J Bacteriol. 191 :333-346
2. A. Chenal, J. I. Guijarro, B. Raynal, M. Delepierre, D. Ladant (2009) RTX calcium-binding motifs are intrinsically disordered in the absence of calcium: Implication for protein secretion. J Biol Chem. 284 : 1781-1789.
3. J.C. Karst, A.C. Sotomayor Pérez, J.I. Guijarro, B. Raynal, A. Chenal, D. Ladant (2010) Calmodulin-Induced Conformational and Hydrodynamic Changes in the Catalytic Domain of Bordetella pertussis Adenylate Cyclase Toxin. Biochemistry 49 :318-328.