Latest Publications
- Comparative mapping of selected structural determinants on the extracellular domains of cholinesterase-like cell-adhesion molecules (2020) Comoletti D, Trobiani L, Chatonnet A, Bourne Y, Marchot P. Neuropharmacol in press PMID:33166544
- The neuroligins and the synaptic pathway in Autism Spectrum Disorder (2020) Trobiani L, Meringolo M, Diamanti T, Bourne Y, Marchot P, Martella G, Dini L, Pisani A, De Jaco A, Bonsi P. Neurosci Biobehav Rev 119 37-51 PMID:32991906
- Biochemical characterization of a glycosyltransferase Gtf3 from Mycobacterium smegmatis: a case study of improved protein solubilization (2020) Bakli M, Karim L, Mokhtari-Soulimane N, Merzouk H, Vincent F. 3 Biotech 10 436 PMID:32999813
- The Ig-like domain of Punctin/MADD-4 is the primary determinant for interaction with the ectodomain of neuroligin NLG-1 (2020) Platsaki S, Zhou X, Pinan-Lucarre B, Delauzun V, Tu H, Mansuelle P, Fourquet P, Bourne Y, Bessereau J-L, Marchot P. J Biol Chem 295 16267-16279 PMID:32928959
- Snapshots of ADP-ribose bound to Getah virus macro domain reveal an intriguing choreography (2020) Ferreira-Ramos AS, Sulzenbacher G, Canard B, Coutard B. Sci Rep 10 14422 PMID:32879358
- Report from the 26th Meeting on Toxinology, "Bioengineering of Toxins", Organized by the French Society of Toxinology (SFET) and Held in Paris, France, 4-5 December 2019. (2020) Marchot P, Diochot S, Popoff MR, Benoit E. Toxins 12 31 (pp 1-30) PMID:31947870
- An evolutionary perspective on the first disulfide bond in members of the cholinesterase-carboxylesterase (COesterase) family: Possible outcomes for cholinesterase expression in prokaryotes. (2019) Chatonnet A, Brazzolotto X, Hotelier T, Lenfant N, Marchot P, Bourne Y. Chem Biol Interact 308 179-184 PMID:31100280
Our research projects address the molecular architectures and functional mechanisms of carbohydrate-active enzymes (CAZymes), sensor domains and lectins, and of enzymes, receptors and cell adhesion molecules with a neurobiological interest.
The CAZymes govern the hydrolysis, conversion or recognition of sugar moieties from glycoconjuguates widely found in animals, fungi, plants and bacteria. These conjugates are involved in key biological processes such as development, fertilization, quality control of protein folding, host-pathogen recognition, immune response, and they can be linked to diseases such as neurodegenerative metabolic diseases. In collaboration with the “Glycogenomics” team we pay particular attention to those glycoside hydrolases that are of interest for biomedical and biotechnological applications.
We also address the function, recognition properties and structure of receptors, enzymes and adhesion molecules involved in central and peripheral neurotransmission, with particular interest for their structure-function relationships, specificity of partner and ligand recognition, conformational dynamics and functional regulation. In particular we have accumulated expertise in the study of the enzyme acetylcholinesterase and of the extracellular ligand-binding domain of the nicotinic receptor to acetylcholine whose malfunctioning has been correlated with neurodegenerative diseases, and to cell adhesion molecules structurally related to the cholinesterases or to other families of proteins and associated with developmental neuronal deficiencies.
Our methodological approaches involve recombinant protein expression in prokaryotic and eukaryotic systems and complementary biochemical, biophysical, functional and structural (X-ray crystallography and electron microscopy) characterization means.