Structural Glycobiology and Neurobiology

Heads Yves BOURNE, Pascale MARCHOT

Latest Publications

Carnitine is a pharmacological allosteric chaperone of the human lysosomal α-glucosidase (2021) Iacono R, Minopoli N, Ferrara MC, Tarallo A, Damiano C, Porto C, Strollo S, Roig-Zamboni V, Peluso G, Sulzenbacher G, Cobucci-Ponzano B, Parenti G, Moracci M. J Enzyme Inhib Med Chem 36 2068-2079 PMID:34565280
First insights into the structural features of Ebola virus methyltransferase activities (2021) Valle C, Martin B, Ferron F, Roig-Zamboni V, Desmyter A, Debart F, Vasseur JJ, Canard B, Coutard B, Decroly E. Nucleic Acids Res 49 1737-1748 PMID:33503246
Comparative mapping of selected structural determinants on the extracellular domains of cholinesterase-like cell-adhesion molecules (2021) Comoletti D, Trobiani L, Chatonnet A, Bourne Y, Marchot P. Neuropharmacology 184 108381 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

...All publications

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.