The fifth Glyco Morning event will take place at Cermav on Friday, November 17th from 10 to 12. The invited speaker is David Vocadlo, from the Simon Fraser University, who will give a talk on “Chemical Biology Tools to Perceive and Perturb within Living Systems Carbohydrate Structures and Carbohydrate Processing Enzymes Involved in Neurodegenerative Diseases”. Two young glycoscientists from Glyco@Alps, Milène Nitenberg (Cermav) and Rana El Masri (IBS) will kick off the event with short talks.

Invited speaker

Chemical Biology Tools to Perceive and Perturb within Living Systems Carbohydrate Structures and Carbohydrate Processing Enzymes Involved in Neurodegenerative Diseases

David Vocadlo, Simon Fraser University, Canada

The carbohydrate structures found in every kingdom of life are emerging as a frontier area of chemical biology. I will discuss our work on the creation of new chemical biology tools for studying these structures and the enzymes that process them within cells and in animal models, with a particular view to understanding and combating neurodegenerative diseases. Topics will be selected from the synthesis, analysis, and deployment of; (i) a new family of fluorescence-quenched substrates that permit quantitative imaging of glycoside hydrolase activities in live cells by high content imaging and high throughput screening, (ii) the design, synthesis, and creation of potent and selective inhibitors of carbohydrate processing enzymes active in cells and in vivo that are protective in Alzheimer disease models, and (iii) new chemical genetic methods to map protein glycosylation to the genome.

Young scientists talks

Biogenesis of photosynthetic membranes: structure-function study of MGD1, a galactolipid synthase from Arabidopsis.

Milène Nitenberg, Cermav

Resume will come soon

The recognition of heparan sulfate by extracellular endosulfatase HSulf2: a cooperative hunting process

Rana El Masri, IBS

Sulfs are novel extracellular sulfatases that catalyze specific desulfation of heparan sulfate (HS) proteoglycans, thereby regulating their interactions with various signaling molecules. Sulfs contain two domains: a catalytic domain (CAT) that include the enzyme active site, and a hydrophilic domain (HD) that is responsible for high affinity binding to HS substrates. Despite their involvement in major human pathologies such as cancer, Sulfs have remained elusive and poorly understood enzymes. Recently, we have identified an enzymatic mechanism by which Sulfs catalyze the processive and orientated desulfation of HS and finely regulate the polysaccharide biological properties. Here, we have characterized the implication of HSulf2 domains in the interaction with HS. We found that the deletion of the HD domain dramatically impaired the activity of the enzyme but did not completely alter the binding to HS. We then identified epitopes within the CAT domain that are required for the endosulfatase activity. Altogether, these results provide further insights into the enzyme/substrate recognition process and contribute to the understanding of the fundamental role played by these enzymes in the regulation of HS activity.